Food Allergy, Intolerance and Sensitivity
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Introduction
Food Allergy
Food Intolerance
Overview
Non-IgE-Mediated Immune System Response to Food
Overview
Coeliac / Celiac Disease
Metabolic Food Intolerance
Introductionn
Lactose Intolerance
Fructose Malabsorption and Fructose Intolerance
Sugar Alcohol Intolerance
Diabetes mellitus
Phenylketonuria
Pharmacological Reactions
Amino Acids as Food Additives
Glumatic Acid, Glutamate and MSG
Monosodium Glutamate
Protein Glutamate
Free Glutamate
Free Glutamate and Glutamic Acid as Excitotoxins
Side Chain Charge
Side Effects of excessive free glutamate consumption
Ways to combat the effects of excessive free glumate
Aspartame/NutraSweet
General Digestive Enzyme and Stomach Acid Deficiencies
General Food Considerations
Gluten and Gluten-Free Diets
Milk Dairy
Other Food Types
Natural Selection
Good vs Bad Foods
Detection
Observation, Elimination, Reintroduction
Hydrogen Breath Test
Antibody Tests
Genetic Testing for Celiac Disease
Intestinal Malabsorption Testing
Treatment
Elimination Diets
Supplemental Digestive Support
Immunotherapy
Stress Management
Chelation Therapy
Antimicrobial Therapy
Antioxidant Therapy
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Introduction:
There are several different definitions for what constitutes a Food Allergy and what consitutes Food Intolerance. This section shall attempt to bring together the various concepts to provide a high level overview of the subject matter. In general, Food Sensitivity is the term used to describe both Food Allergy and Food Intolerance.
Food intolerance is harder to identify on account of its slower acting nature and often cause downstream problems, localised gastointestinal inflammation and a drain on one's energy reserves if not regulated and treated properly.
Below are some useful information web sites on food allergies and intolerances.
www.allergyuk.org
www.foodintoleranceawareness.org
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Food Allergy:
In a general sense, a Food Allergy can be classed as an immediate immune system response, specifically the Immunoglubin IgE, to consuming a certain food protein, even in tiny amounts. A Food Allergy response can occur within seconds or minutes of consuming the item. It can even occur as the food touches the lips or tongue, before the food has actually entered the oesophagus.
http://en.wikipedia.org/wiki/Food_allergy
http://en.wikipedia.org/wiki/IgE
http://en.wikipedia.org/wiki/Histamine
IgE is one of the body's primary immune defences against real or perceived threats or 'invaders'. In this instance, the food proteins in question are confused with the very similar viral DNA proteins. The immune system detects these food types as antigens or allergens, and the immune system produces large amounts of IgE antibodies, which attach themselves to specialised white blood cells, which secrete histamine (the chief inflammatory agent) and cytotoxic and inflammatory chemicals.
Whilst this predisposition toward misinterpretation may sometimes be of genetic origin or of infant immunity adaptation, there are many other factors involved in the immune system developing this characteristic. In 2008, The Food Allergy & Anaphylaxis Network estimated that 4% of the US population suffered from food allergies.
Symptoms of Food Allergy are distinctive and acute in nature, and can include:
In extreme cases, it can be life threatening (i.e. anaphylactic shock), the severity of the body's IgE immune response being sufficient to hypotension (blood pressure drop), loss of consciousness and possibly death. In such cases, an Adrenaline (Epinephrine) is used by Ambulance or Accident and Emergency staff as an injection to control the allergic reaction. However, in the vast majority of cases, a mild version of one or more of the other symptoms is experienced immediately after coming into contact with the food, the allergic reaction just subsides with time.
Another term for Food Allergy is Rapid-Onset Food Allergy. Whilst the term Food Allergy is used to describe IgE-mediated immune system response to a certain food type, it could imply to some that this is the only type of adverse immune response possible to certain non-contaminated food types. There are slower acting, chronic responses to eating certain food types that can develop anywhere from 30 minutes to 48 hours after eating, involving other types of immune system response, but these are generally referred to as Food Intolerance
Examples of the main food types that tend to cause roughly 90% of the IgE mediated allergic responses in those who suffer from Food Allergies include the following.
The other 10% of food allergies (the less common ones) involves the proteins of certain food sources. One example is a rice allergy. This tends to be more common in East and South East Asia where rice forms a large piet of the staple diet of the average person. Celery allergies tend to be more common in Central European populations.
There may be some cross-sensitivity with foods, for example, those allergic to crustaceans or oysters may tend to also be allergic to squid.
Food allergies can operate through airborne matter from problem foods, and through the skin (touching the food type with your hands or lips), and not just through the actual ingestion of the foods. This may affect workers in food processing industries who may suffer from skin disease, asthma, rhinitis and conjunctivitis.
In general the more concentrated the protein fraction of the food is, the more noticeable the allergic reaction and symptoms will be. For example, consuming reasonable quantities of wheat bran or rice bran will likely produce more of an allergic reaction in individuals who suffer from these allergies than their usual flour or wholegrain counterpart, as the protein concentration is higher. However, there is not always a logical pattern to follow. To a large extent, it may depend on the brand or source of the food substance, and also its possible level of contamination with other grains. A similar pattern may be noticed with supplements, some working well with the body, others doing nothing and others still provoking a mild immune system-type response - for the same active ingredient (differing in quality, preparation and other additives etc.)
For example, I myself experience an immediate allergic reaction upon eating a porridge made with NOW Foods Rice Bran (immediate onset of a sore throat which lasts several hours). I can feel the 'sour' nature of the protein in my mouth and feel an instant IgE reaction with the porridge in my mouth. There is no swelling of any kind, just a continual sore throat. However, I do not experience any such reaction when taking a protein supplement rich in Rice Protein and Rice Bran, Thorne Research's MediClear. MediClear was also kinesiologically tested on me and found at that point in time to be what the body wanted. It is unlikely that a food stuff that caused a Food Allergy response would test positively using this method. I have tried a few brands of wholegrain rice and rice milk, which are less concentrated sources of rice protein/gluten, and does not experience any noticeable allergy symptoms with these.
Another example is Coconut. I have found that I had a similar reaction to dessicated Coconut, with a sore throat coming on within minutes. However, I do not observe these symptoms with Coconut oil, which contains no protein (possibly contain some faint traces of Coconut protein).
Similarly, I experience a similar sour sensation when tasting porridge made from The Oatmeal of Alford (Kiln Fried, Stone Ground) and immediate onset of a sore throat upon eating that lasts for several hours, similar to the above (i.e. an IgE-mediated food allergy response). However, I experience significantly reduced symptoms with porridge made from other brands of oats (e.g. Organic Quaker Oats, E.Flahavan & Sons Porridge Oats, Jordan Organic Oats); or even with a more concentrated Oat protein/gluten source such as Mornflake Oatbran. Gluten-Free Oats (or in other words, Oats free of any Wheat, Barley or Rye contamination - but still containing the glutens naturally found in Oats) still produced an allergic reaction.
Similarly, those who suffer from a milk allergy will likely experience less of a reaction from goat's milk than cow's milk, as the protein fraction is lower.
There may be possible minor food intolerance issues associated with these foods I have cited as examples, but that is a different story (which could be down to general digestive inefficiency and/or IgG type reactions). Of course, the fact that I am experiencing a sore throat with the aforementioned proteins in certain forms is a general indicator to avoid those forms, and perhaps also related forms that may still be causing immune system responses but that which are not noticeable, but still not really desirable from a physiological perspective.
If we are talking about IgE mediated 'incorrect' immune reactions (Allergies) in general, not just food related, then the response may build up as the body comes into contact with more of the allergen, through inhalation or through contact or proximity to the skin, as opposed to ingestion with food allergies when a proportionately higher concentration is taken into the body in a short period of time. Common genergl IgE type allergens include:
Those with severe IgE-mediated allergies should consider wearing a Medic Alert bracelet, pendant or tag with details of their allergies, and perhaps blood type and any other relevant information.
http://en.wikipedia.org/wiki/Oral_allergy_syndrome
Hazelnut is a food type that is sometimes identified in IgG blood testing as being a food that one reacts to. However, some commentators argue that this is a reaction, but not an allergic one (despite the test result). The Hazelnut protein is irritating to the tongue and it titillates the palate in small doses. This is why Hazelnuts are often used by Chocolatiers as opposed to other nuts. I have always wondered why Hazelnuts were used as they were never his favourite nut particularly.
One could however interpret this behaviour of hazelnuts as being reflecive of Oral Allergy Syndrome, that is a cluster of allergies (including IgE) in the mouth (typically burning sensation or itching of lips, mouth and/or pharynx) to eating certain fruits, nuts and vegetables, typically noted in hayfever sufferers who have cross-reaction with compounds in these foods that appears similar to birch pollen. These foods can include: apples, hazelnuts, peaches, cherries, almonds, pears, carrots, and celery. The symptoms are arguably somewhat different to those the majority of people who eat hazelnuts without itchy lips etc. It is more of a mild (physical) irritation to the tongue as opposed to an immune system-mediated response that affects more parts of the head and throat.
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Food Intolerance:
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Overview:
Food Intolerance, or non-IgE mediated Food Hypersensitivity, is a term used to describe a number of different possible, chronic, slow acting symptoms and processes that result from the consumption of a certain food type, a reaction occurring anything between 30 minutes or up to 48 hours after the food is consumed. The amount of a food substance required to trigger this response may vary, but is usually much larger than that required to trigger a food allergy response as described above.
The definition of Food Intolerance is quite broad, and includes most types of adverse reactions to food, with the exception of fast acting IgE mediated immune response and psychological derived reactions and responses to food. The conditions or reactions encompassed by the term Food Intolerance are summarised below. Some of these classifications are rather arbitrary, but it is a good starting point.
Symptoms of Food Intolerance include the following.
Fatigue in the context of CFS means more than one's usual level of fatigue, hours or days after consuming certain foods. Other individuals may sense the fatigue or general malaise a few hours after eating it or so.
If one is eating the foods in question every day or every other day, then it one may not notice the dips so much as one may well be in a constant low ebb - abstaining from the offending foods may result in a decrease in one's day to day level of fatigue.
Symptoms may vary in severity between individuals and be dependent on the volumes of the foods in question, and the concentrations of the ingredients that cause intolerance contained in them. Symptoms may persist for up to 3 days or so (in some cases up to 2 weeks) after cutting out all foods that are the main causes of intolerance (if this is possible - see below). Many of the symptoms may go unnoticed by the patient, or if they are noticed, may simply be accepted as part of one's physiological make-up and not attributed to being caused by one's diet.
Because of the slow nature of the reaction to the food, it is clearly more difficult to determine the precise offending food that is causing this response, if indeed one believes that a food source may be the problem, which may not be immediately obvious to a doctor or a patient. IgE-mediated Food allergies are generally much easier to identify on account of their rapid onset, immediately after consuming the particular food type.
The reaction to the consumption of these foods tends to arrive between 3 hours after first consuming the food and up to 3 days afterwards. According to Allergy UK, up to 45% of the UK population is affected by food intolerance.
Other terms for Food Intolerance, or Non-IgE-Mediated Food Hypersensitivity, include Non-Allergic Food Hypersensitivity, Pseudo-Allergic Reactions, Slow-Onset Food Allergies. Clearly some of these terms are slightly misleading as some imply that slow acting immune responses are not 'true allergies' and other terms for Food Intolerance imply that all the types of Food Intolerance are 'allergies' or immune system related, which is not true either. Food Intolerance is a little like CFS, it is useful for describing symptoms, but not very useful when it comes to correctly describing the causes or mechanisms of those symptoms.
http://en.wikipedia.org/wiki/Food_intolerance
Food Intolerance has been found to be associated with other medical conditions, including:
Food Intolerance is still not taken very seriously by medical professions in the UK:
'In the UK, scepticism about food intolerance as a specific condition influenced doctors' (GPs') perceptions of patients and of the patients' underlying problems. However, rather than risk damaging the doctor-patient relationship, when GPs chose, despite their scepticism, and tempered by an element of awareness of the limitations of modern medicine, to negotiate mutually acceptable ground with patients and with patients' beliefs. That as a result, whether due to a placebo effect, secondary benefit, or as a biophysical result of excluding a food from the diet, the GPs acknowledged benefit, both personal and therapeutic.'
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Non-IgE Mediated Immune System Response to Food
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Overview
The term Food Allergy is used to denote fast acting, IgE-mediated immune system reactions to food only, rather than embracing the entirety of different adverse immune system responses to food, the fast acting and more acute, and the slower acting and more chronic. All Non-IgE Mediated Immune System Responses to Food, being slower acting, are classed as being Food Intolerances, a term which includes other types of slow reaction included a lack of necessary enzymes and toxicological responses etc.
Of course, IgE and non-IgE immune responses can occur within the same patient to the same food type, but at slightly different times, i.e. the IgE symptoms being noticed immediately upon ingestion and the non-IgE symptoms being noticed slightly later.
http://en.wikipedia.org/wiki/Food_allergy
Wikipedia defines Food Allergy according to three groups:
Some of the latter two groups are hereditary (genetic) in nature, others are merely conditioned or acquired.
Non-IgE-mediated Immune System Responses to certain Food Types could be classed as Non-IgE-mediated 'Food Allergies'. Some commentators use the term 'Delayed-Onset Food Allergies' to describe Food Intolerance as a whole, although this is misleading as it associates non-immune system modulated Food Intolerance reactions (e.g. inadequate enzyme production) with Non-IgE-Mediated Immune System Responses to Food. Some may complain about the use of the term 'Allergy' as it should primarly refer to IgE reactions, as per Wikipedia's definition of Allergy below.
http://en.wikipedia.org/wiki/Allergy
However, there is a certain amount of leniency in defining what is an 'Allergy', as per the 3 groups of Allergy referenced above. I therefore stick to the term 'Non-IgE Mediated Immune System Response to Food' which is what we are actually talking about here - where there can be no room for confusion. Secondary Immune System Response to Food could also be another possible term, although perhaps less formal and precise than the above.
It is primarly the non-IgE mediated immune responses that we shall examine in this section, specifically IgA and IgG. The severity of the different immunological reactions to food differ between foods, and between individuals, as well as how they combine with other Food Intolerance and other factors.
Non-IgE Mediated Immune System Responses do not occur in isolation to other types of Food Intolerance and can occur concurrently with Metabolic, Pharmacological and Toxin-Mediated Reactions to Food. Their combined action may provide the broad spectrum of symptoms that we experience as Food Intolerance. And indeed, they can also exacerbate a downward spiral of General Digestive Enzyme and Stomach Acid Deficiencies and indeed the other types of Food Intolerance.
The foods that cause Non-IgE Mediated Immune System Responses in susceptible individuals tend to from the same food groups as those that provoke IgE mediated food allergies (Classic or True Food Allergies) as listed above. The reactions are based on the misrecognition of certain types of protein as viral DNA proteins, the same as Classic Food Allergies.
http://en.wikipedia.org/wiki/Food_intolerance
'Food antigens contact the immune system throughout the intestinal tract via the gut associated lymphoid system (GALT), where interactions between antigen presenting cells and T cells direct the type of immune response mounted. Unresponsiveness of the immune system to dietary antigens is termed "oral tolerance" and is believed to involve the deletion or switching off of reactive antigen-specific T cells and the production of regulatory T cells (T reg) that quell inflammatory responses to benign antigens.'
Immunoglobulin G (IgG) is a monomeric immunoglobulin. Each IgG has two antigen binding sites. It is the most abundant immunoglobulin and is equally distributed in tissues liquids and blood, constituting 75% of serum immunogloblulins in humans. IgG molecules are synthesised and secreted by plasma B cells. IgG forms part of the body's secondary immune system, the primary being mediated mainly by IgM.
http://en.wikipedia.org/wiki/IgG
Typically IgG-mediated reactions are much more common than IgE mediated reactions, but are much less well researched and understood. Most occurrences are very mild and go undetected or relatively symptomless (which is a matter of perception in many individuals with a less than perfect diet and lifestyle). Many may choose to ignore the presence of some of the milder IgG reactions, and pay attention and make dietary changes accordingly when they are found to have more severe IgG reactions to certain food types. However, milder IgG reactions may be indicative of other types of immunological reactions to these foods or other foods, and indeed may over time drain one's energy reserves and put a strain on the immune system and body in general. Most commonly, IgG antibodies/immunoglobulins are detected in the blood, through an IgG blood test. IgG-mediated immune reactions to food tend to occur in some of the food types that we consume most regularly, but as a species are not perhaps best physiologically adapted to (e.g. most commonly grains and milk). IgG antibodies are found in those individuls who do not have (significant) food intolerances (who do not notice any symptoms).
Of course the foods that create these Non-IgE-Mediated Immunological Food Intolerance reactions do so in their protein form, which is the non-digested or semi-digested form, in the digestive tract, and what is absorbed into the bloodstream is (hopefully) only amino acids (assuming that Leaky Gut Syndrome (LGS) is not present. LGS can be caused by a number of possible factors, including excessive Candida albicans growth, which can further fuel Non-IgE Mediated Immunological Responses to Food. In addition, LGS is one potential downstream consequence of too much immune system regulated inflammation in the digestive tract, caused by excessive Eosinophil hyperactivity and inflammatory cytokines being released by them. This is one feature of severe cases of Celiac Disease (Gliadin Protein Intolerance). LGS is examined in more detail on the Digestive Disorders page.
Therefore one would assume that the majority of IgG antibodies would be present in the digestive tract rather than in the blood, although in more severe cases, the levels may well rise higher in the blood. Some commentators have criticised IgG blood tests as they often come back negative when the actual picture in the body as a whole, and also the digestive tract, tells a different story. Nevertheless, IgG blood tests can still be a useful tool in diagnosing Non-IgE-Mediated Immunological Food Intolerances.
YorkTest states that Food Intolerance can be detected by measuring IgG antibodies in th blood, in their Foodscan 113 Food Intolerance Test report, which is a test for IgG antibody reaction to 113 food types. It is presented as a Food Intolerance Test, but it is really just tested one aspect of Food Intolerance - which is still useful, but it is more of an introductory type test into Food Intolerance. YorkTest also state that Food Sensitivity can also arise from mechanisms that do not involve the immune system, such as enzyme deficiencies (e.g. lactose intolerance) or chemical sensitivies such as reaction sto food additives (e.g. tartrazine (E102) and sunset yellow (E110). YorkTest use the terms Food Intolerance and Food Sensitivity interchangeably, the latter being arguably a more ambiguous term.
www.yorktest.com/en/allergy-or-intolerance
Immunoglobulin A (IgA) is an antibody that plays a critical role in the immunity of mucosal membranes. IgA in the mucosal linings are larger in number than all other types of antibodies combined. Between 3g and 5g is secreted into the intestinal lumen every day. There are two subclasses of IgA, IgA1 and IgA2, and can exist in a dimeric form, known as secretory IgA (sIgA). The secretory part protects the immunoglobulin from being degraded by proteolytic enzymes, e.g. in the digestive tract, so it can survive in the intestines and protect against harmful microbes.
http://en.wikipedia.org/wiki/IgA
IgA antibodies/immunoglobulins are produced mainly in the digestive tract. They are the digestive tract's main immunological defense. They are secreted by the intestinal walls into the intestinal lumen (the hollow centre of the intestines) and mix in with the Chyme and Stool, which passes through the GI tract, slowly being digested, before being expelled from the body via the anus. IgA antibodies cannot be readily reabsorbed from the digestive tract. The purpose of these antibodies is to combine with any detected protein threats, interpreted to be of viral origin, in order to neutralise them and prevent them being absorbed from the GI tract into the bloodstream. This may well result in some of the IBS type symptoms as unabsorbed proteins are fermented by bacteria in the colon. Antibodies operate in a kind of lock and key manner, matching the exact type of protein they are created to bind with.
The immune cells of the digestive tract comprise the largest body of immune cells in the body. The GI tract has an enormous surface area and is arguably one of the main possible mode of entry into the body by foreign pathogens, perhaps even more so than the lungs. The GI tract comprises probably the majority of the body's immune system, in relative terms. Without IgA antibodies being released into the digestive tract, one would be highly susceptible to gastro-intestinal viruses and other forms of infection, e.g. bacterial, fungal etc. Certain individuals in tests have been shown to produce very few IgA antibodies, which is of course an immune system deficiency.
However in Food Intolerance patients, the level of IgA antibodies tends to be elevated, that is only the IgA antibodies that correspond to certain food types. It is thought that measuring IgA antibodies in the stool is a useful measure of Immunologically-Mediated Food Intolerance, and can show us what IgA antibodies are present in too high a concentration in the stool, thus indicating this type of Food Intolerance response before signs and symptoms are evident in the blood with overactivity and overproduction of other antibody types (to the particular food types).
Whilst anti-Gliadin antibodies are found in the blood samples of approximately 12% of the general US public, the studies of Kenneth Fine, M.D., of Enterolab, have shown that perhaps up to 30% of a group of 'otherwise normal people' from the US and Overseas have detectable levels of these antibodies in their stool samples. This figure rises to as high as 50% in patients suffering adverse symptoms or from high risk populations (those with higher incidences of Gliadin sensitivities). This would seem to confirm the above hypothesis regarding IgA levels in the stool vs the blood, and backing up the idea that the stool is the most sensible place to look for IgA antibodies.
If one has an non-IgE-mediated immune system sensitivity or response to certain food types, e.g. Gliadin or Dairy, and one eliminates these food sources from one's diet, i.e. one goes on a Gluten-free or Milk-free diet (and does not consume any hidden sources of Gliadin), then the production of the IgA antibodies corresponding to these food types does not go down immediately to lower levels. Of course, without these particular food sources in the GI tract, they have nothing to attack (often besides the digestive tract itself), but the body still produces them as it is 'expecting' them. Research shows that these antibodies continue to be produced in the digestive tract (and possibly elsewhere) for up to 1-2 years after a person has ceased consuming the corresponding food items. The levels of the corresponding antibodies in the blood tend to drop off more rapidly, in 3-6 months typically. Controlled reintroduction may be one method of adjusting to these proteins without the production of these corresponding antibodies, as may low dose immunotherapy. However, if one starts to eat these food sources in copious quantities in a non-systematic and uncontrolled manner, then the levels of the antibodies are likely to increase to their former levels very rapidly. It may vary according to the individual of course, and a 'Gluten challenge' may not necessarily guarantee immediate increase in relevant antibody levels for detection if Gluten is reintroduced heavily for 1-2 weeks.
https://www.enterolab.com/StaticPages/Frame_Faq.htm
Enterolab have stated in an email correspondence with me that the body generates IgA antibodies if one is intolerant or sensitive to a particular food (food intolerance and sensitivity being used interchangeably here also); but that the body will generate either IgE or IgG antibodies/immunoglobulins if one is allergic to a particular food, depending on the food and severity of the response. Arguably it is probably both for a Classic Food Allergy. Whether one chooses to classify IgG-Mediated Immune System Response then as an Allergy, a Group 3 Allergy or Food Intolerance is perhaps a matter of classification. However, Enterolab stress the difference in causation between IgA and IgE reactions.
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Coeliac or Celiac Disease
Celiac Disease, a.k.a. Celiac Sprue or Coeliac Disease, is classified as an autoimmune disorder, and is essentially an adverse immune system response to Gluten (i.e. Gliadin/Gluten Intolerance). It can affect genetically predisposed individuals of all ages, from middle infancy onwards. Celiac Disease is the result of a combination of the action of Anti-Gliadin Antibodies (AGAs) against the presence of ingested Gliadin , but more importantly the production of Anti-Tissue Transglutaminase Antibodies (anti-tTG antibodies). Whilst non-Celiac sufferers can have AGAs, i.e. Gliadin/Gluten Intolerance, they do not have measurable levels of anti-tTG antibodies, which are a genetic-based response in Celiac sufferers to the ingestion of Gliadin. Celiac Disease is therefore a specific type of Gliadin(Gluten)-intolerance.
http://en.wikipedia.org/wiki/Celiac_disease
Approximately 0.5-1% of the population of the USA suffer from Celiac Disease. There are a number of genes that are involved in controlling the excessive immune response to Gliadin (Gluten), that may lend an individual predisposed or more likely to develop such a condition, and according to the studies of Kenneth Fine, M.D., of Enterolab, is found in approximately 60% of Americans. There may be other, currently undefined genes, that control whether such a toxic reaction occurs and if and to what extent damage will occur to the intestines and other tissues or not. Research suggests that as many as 30% of Americans may be Gluten sensitive, with 1 in 225 having the sensivity as severe to cause the intestinal damage associated with Celiac Disease. Please seee the Genetic Testing section below for more discussion of the Celiac genes present in the US population.
Transglutaminase is family of enzymes that catalyse the formation of a covalent bond between a free amine group (e.g. from lysine groups found in a protein or peptide) and the gamma-carboamid group (e.g. from glutamine groups found in another protein or peptide). The bonds formed by transglutaminase are highly resistant to proteolytic degradation. Tranglutaminase enzymes are generally found in the intestines and also in the tissues. It is referred to as 'meat glue' in the food processing industry. They play an important part in blood clotting.
http://en.wikipedia.org/wiki/Transglutaminase
One subclass of Transglutaminase is known as Tissue-Transglutaminasen (TG2 or tTG). It is classed as an 'auto-antigen'. It's natural affinity to binding with Gliadin, and the resulting protein crosslinking stimulates the immune B-cell responses that eventually result in the production of the problematic overproduction of the ATA IgA and IgG antibodies (examined below).
Whilst associated with Celiac Disease, high levels of Tissue Transglutaminase enzymes are found in sufferers of Huntingdon's and Parkinson's Disease. A study by Griffin M, Casadio R, Bergamini CM. 'Transglutaminases: nature's biological glues'. Biochem J 2002;368:377-96 suggests that tTG plays an important role in inflammation, degenerative diseases and tumor biology.
http://en.wikipedia.org/wiki/Tissue_transglutaminase
In Celiac Disease, antiendomysial antibodies (EMAs) are produced. These mainly consist of Anti-Transglutaminse Antibodies (ATAs) against the enzyme Transglutaminase and Tissue-Transglutaminase. ATAs are types of IgA and IgG antibodies, and their relative proportions in Celiac Disease sufferers depends on the phenotypes involved. Please note that these EMAs are different to Anti-Gliadin Antibodies (AGAs), consisting of IgA and IgG antibodies, that attack Gliadin directly. IgA antibodies can be found in the stool and also the blood to a lesser extent, and the presence of anti-tTG antibodies in high numbers can predict the onset of Celiac Disease. anti-tTG antibody production can also be stimulated by the presence of the Rotavirus protein VP7. A Rotavirus is a genus of double-stranded RNA virus from the Retroviridae family and is known to cause diahrrea.
http://en.wikipedia.org/wiki/Anti-transglutaminase_antibodies
'For tTG autoimmunity (CD), T-cells are generated against wheat gliadin and similar gluten proteins of the trib Triticeae. The T-cells are defined by the ability to react to HLA-DQ8 and DQ2.5 restricted antigens and gliadin is one of the antigens. Gliadin is a favored dietary substrate for transglutaminase because of many enzyme reaction sites on gliadin. In disease, transglutaminase reacts with gliadin forming a linkage. In forming this bond transglutaminase becomes linked to T-cell epitopes on gliadin. B-cells with surface IgM that react to transglutaminase can present it with bound gliadin peptides to T-cells which stimulate B-cell maturation and proliferation to plasma cells making IgA or IgM.'
www.enterolab.com/StaticPages/Faq_Result_Interpretation.htm
According to Dr Kenneth Fine of Enterolab, 'the main perpetrator of the immune response to gluten is not antibody but T lymphocytes (T cells) producing tissue-damaging chemicals called cytokines and chemokines. How much antibody is produced at the stimulus of T cells differs in different people. Furthermore, some people simply do not or cannot make alot of intestinal IgA antibody even though gluten may be stimulating a severe T cell-mediated immune response. Unlike antibody levels, the numeric value of malabsorption test results are an indicator of severity of intestinal damage.'
Enterolab stated in an email correspondence to me that cytokines and chemokines can cause damage to the intestinal villi. This is observed in IgA deficient individuals. In addition, cytokines and chemokines can circulate anywhere in the body to cause oxidative damage elsewhere, which is why systematic and multisystem symptoms (of inflammation) are observed in gluten sensitivity (whether AGA and/or ATA derived).
http://en.wikipedia.org/wiki/Gluten_immunochemistry
'The release of IL15 [Interleukin 15 - a cytokine] is a major factor in coeliac disease as IL15 has been found to attract intraepithelial lymphocytes (IEL) that characterize Marsh grade 1 and 2 coeliac disease.[6] Lymphocytes attracted by IL-15 are composed of markers enriched on natural killer cells versus normal helper T-cells. One hypothesis is that IL-15 induces the highly inflammatory Th1 response that activates T-helper cells (DQ2 restricted gliadin specific) that then orchestrate the destructive response, but the reason why inflammatory cells develop prior to gliadin specific helper cells is not known.[7] The IRP response differs from typical responses that stimulate IL15 release, such as viral infection. In addition, other cytokines such as IL12 and IL2, which are typically associated with T-helper cell stimulation, are not involved. In these two ways the innate peptide activation of T-cells in celiac disease is strange. IL-15 appears to induce increases in MICA and NKG2D that may increase brush-border cell killing.'
These IgA and IgG ATAs can also be classified in the following manner based on their properties (the Transglutmainse isoform being targetted).
ATAs are found most frequently in certain autoimmune diseases, e.g. juvenile diabetes, and in almost all cases of Celiac Disease. The above estimate of 0.5% to 1% of the US population being Celiac Disease sufferers is based upon the statistic of 1% of the population having pathogenic levels of ATA. ATAs are
www.absoluteastronomy.com/topics/Anti-transglutaminase_antibodies
The antibodies implicated in Celiac Disease, i.e. IgA and IgG, are discussed at the link below.
www.absoluteastronomy.com/topics/Anti-gliadin_antibodies
There may be no detectable symptoms of the IgA ATA immune response to Gliadin, with symptoms typically becoming noticeable when the immune reaction over time has begun to damage the intestines, with resulting Food Intolerance type symptoms. These symptoms derive from the resulting malabsorption or improper digestion of dietary nutrients (i.e. metabolic food intolerance - discussed below), and can include abdominal pain or bloating, diarrhea, constipation, wind or nauseous feeling (with or without vomiting). Fine postulates that acid reflux and heartburn may also be a possible symptom. Other symptoms could include fatigue, joint pains, mouth ulcers, bone pain, abnormal menses and even temporary infertility. It is the downstream effects of the IgA ATA immune response to Gliadin and the damage it causes to the intestinal villi and the resulting symptoms that is generally referred to as Celiac Disease.
Kenneth Fine has suggested that the intestinal damage caused by Celiac Disease (or otherwise elevated Anti-tTG antibodies) is responsible for a significant increased risk of cancer of lymphoma of the small intestine. Indeed, he believes there is a strong correlation between autoimmune disease development and the continued consumption of Gliadin in Gluten sensitive individuals.
https://www.enterolab.com/StaticPages/Frame_Faq.htm
Fine also suggests that 'Non-celiac gluten sensitivity syndromes are no less severe than ones accompanied by villous atrophy, in terms of symptoms they may cause, accompanying autoimmune diseases in other parts of the body, and resultant disability.'
http://www.enterolab.com/StaticPages/Frame_TestToOrder.htm#Genetic_testing
In an email correspondence to me, Enterolab have stated that Dr Fine has found that anti-casein antibodies can actually cause some of the same damage and symptoms (of villous atrophy) as anti-Gliadin antibodies (AGAs), which are often more harmful than the effects of the anti-tTG antibodies produced in reaction to the fusion of tTG and Gliadin.
Enterolab also stated that Dr Fine uses the the 'Gluten-Sensitive' to describe those that produce IgA antibodies in reaction to Gluten, i.e. Anti-Gliadin Antibodies (AGAs). Some of the people who produce AGAs also produce anti-tTG antibodies. As mentioned above, the damage to the intestinal villi does come immediately, but lags behind anti-tTG antibody production and may not be detectable (using conventional methods) until the damage has been done. Clearly one does not need to have intestinal damage present in order to be considered 'Gluten-Sensitive', but the more damage that is present, the more likely one is to be diagnosed with Celiac Disease and classified as a Celiac. By this logic, some Celiac patients or those who exhibit the same symptoms may not necessarily be producing significant anti-tTG antibodies, but much of the damage may be caused by Anti-Casein Antibodies and anti-Gliadin antibodies etc. (i.e. Milk and Gliadin/Gluten Sensitivity).
In the UK, the National Institute for Health and Clinical Excellence (NICE), whilst immersed in controversy over some of its arguably inappropriate recommendions for CFS treatment, does actually recommend the screening for Celiac Disease in patients with newly diagnosed CFS (Clinical Guideline 53) and IBS (Clinical Guideline 61).
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Metabolic Food Reactions
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www.bbc.co.uk/health/conditions/foodintolerance1.shtml
Humans are of course the only animal to consume milk after weaning age, and in particular the milk of other animals, namely the milk of the domesticated cow (Bos primigenius). And indeed the only animal to expose other animal's milk to high temperatures before consumption (pasturisation), which may modify the protein structure. If milk was so vital to an adult's diet, grown men would continue to breast feed from their mothers into their old age, presumably?
The most common of the type of Metabolic Food Intolerance is Lactose Intolerance, i.e. a 'deficiency' in the Lactase enzyme. Calling it a deficiency in this context is not quite correct and is looking at the glass half empty rather than half full. Having low levels of the lactose enzyme as an adult mammal or indeed human is normal and 'natural', whereas having the capability to produce an increased number of Lactase enzymes in the GI tract is a form of adaptation. This may be for genetic reasons; because of the population group one derives from geographically (phenotype adaptation); and/or for historical reasons (depending on one's exposure to the said carbohydrate type during one's early childhood).
If the intestinal tract does not produce enough Lactase in response to the amount of Lactose consumed (i.e. being 'Lactose Intolerant' or simply consuming too much milk and dairy), then the remaining Lactose will work its way down the intestinal tract and be consumed/fermented/rotted by bacteria, that switch to lactose metabolism, producing hydrogen, carbon dioxide and methane. This fuelling of the dysbiotic and pathogenic micro-organisms in the colon can result in their multiplication, especially if consumed regularly. This creates a variety of unpleasant symptoms, including IBS.
Lactose Intolerance affects approximately 10% of the population of Northern Europe, cow's milk is staple food source for virtually all children and regular food source for most adults in this region.
Lactose intolerance may be caused or worsened also by Celiac Disease, which shortens the intestinal villi that are responsible for producing Lactase.
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Fructose Malaborption and Fructose Intolerance
Fructose is a monosaccharide sugar, also known as a fruit sugar. Fructose is either found in the Fructose form or bound to Glucose as Sucrose (a.k.a. sugar), as a disaccharide, in various food types. Fructose is found in fruit, honey, corn syrup, HFCS, maple syrup and to a lesser extent in vegetables. The highest Fructose containing fruits, with the exception of dried fruits that are more concentrated forms of fruit, include mango, papaya and apple. Please see the chart below for Fructose levels in fruits.
http://hubpages.com/hub/High-Fructose-Foods
Fructose is absorbed from the digestive tract differently to other sugars. Whilst sucrose is digested by the enzyme Sucrase and broken into its constituent parts Glucose and Fructose, there is no digestive enzyme for Fructose as it is already a simple sugar. Its absorption from the digestive tract into the bloodstream is dependent on the present of two carrier proteins, GLUT2 and GLUT5.
Sugar Alcohol Intolerance
[This section is somewhat one sided and will be updated shortly. Xylitol is also pre-biotic and useful in preventing and treating bacterial infections, and is somewhat controversial on account of some poor quality sources and excessive dosing]
A number of Sugar-free, sugar alcohol-based sweetners (sugar substitutes) are available on the market. These include Sorbitol, Mannitol and Xylitol. The reason these are low calorie sweetners is that they are very poorly digested and absorbed in the digestive tract, and are thus relatively 'inert' despite being sweet to the taste. They are thus used in a variety of products, including sweets and some medicines, particularly sublingual and chewable supplements, which often contain both Sorbitol and Mannitol, and sometimes all 3 (as well as Stevia)! Always read the label on sublingual and chewable supplements.
Unfortunately, as these sugar-alcohol sweeteners are poorly digested and absorbed, they pass through the digestive tract, and are digested to some degree by the bacteria in the colon, resulting in excess wind. These alcohol sugars are also laxative in their action, as dissolved particles in the chyme and stools attract water from the intestinal walls and bloodstream, and excessive consumption may also result in diarrhea. In general, alcohol sugars are to be avoided and a much better choice (for occasional use) is the plant-based Stevia, which does not produce these symptoms.
http://www.foodintol.com/food_intolerance/hot_ibs.htm
http://en.wikipedia.org/wiki/Lactose_intolerance#Overview
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Diabetes mellitus
Diabetes (mellitus) as you probably already know is a condition whereby the body does not produce enough insulin (Type I Diabetes), or where the cells do not utilise unsulin properly (Type II Diabetes). Gestational Diabetes is a temporary condition that affects some pregnant mothers who have high blood glucose levels. Insulin is of course the pancreatic hormone that enables cells to absorb glucose in order to undergo respiration and produce energy. Thus the excessive or mistimed consumption of sucrose for a diabetic may result in hyperglycemia (too high blood sugar) and excessive water loss (in an attempt to dump glucose), dehydration and electrolyte loss. This is a form of maladaptation to sugar intake or foods very high in sugar.
http://en.wikipedia.org/wiki/Diabetes
A number of nutrition and herbal based methods have been successfully employed by a number of Diabetes Type I and II sufferers to overcome their Diabetes. Diabetes is often caused in the first place by excessive consumption of foods and drinks containing refined sugar.
Type I Diabetes is genetically similar to Celiac Disease in 7 unusual genetic regions according to the latest research in a study of 20,000 volunteers. Both early-onset diabetes and Celiac disease are caused by improper immune system adaptation. Celiac Disease affects approximately 1% of the UK population as opposed to Diabetes which affects 0.5%.
http://www.guardian.co.uk/science/2008/dec/11/diabetes-food-health
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Phenylketonuria:
Phenylketonuria is a genetic disorder characterised by a deficiency in the hepatic enzyme Phenylalanine Hydroxylase (PAH). This enzyme metabolises the amino acid Phenylalanine to the amino acid Tyrosine. When PAH is deficient, Phenylalanine accumulates in the digestive tract and some is converted into the metabolites Phenylacetate, Phenylpyruvate and Phenethylamine. This may result in a deficiency of Tyrosine in the body as well as bacterial catabolism of Phenylalanine in the digestive tract.
http://en.wikipedia.org/wiki/Phenylketonuria
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Pharmacological Reactions:
Many fermented or aged foods are high in free glutamate, which in their natural unfermented state would otherwise not contain significant amounts of free glutamate. Examples include:
Whilst certain forms of extremely aged soy beans or their processed derivatives may be higher in free glutamate, there are certain health benefits from fermented soy products. Fermented soy tends inhibit the effects of phytic acid (IP6 - an 'anti-nutrient which prevents mineral absorption), increases the availability of isoflavones and also contains probiotic bacteria (in its live or raw form). However, fermented soy is still likely to contain as many phytoestrogens as unfermented soy, which are endocrine disrupting chemicals, and so excessive consumption of fermented soy is probably not a good idea in any case.
Examples of 'good' soy therefore include tempeh, natto, fermented tofu and soymilk, live soy milk kefir, live soy yoghurt - those products that have not been fermented so long; and possibly miso and soy sauce - in moderation (these are the fermented types of soy that have been aged for a very long time). You can taste the free Glutamate in these products, to get an idea of their relative concentrations, and there is little evidence of this taste in soy kefir for example, but a very strong taste in Miso. Miso also contains a significant amount of salt which may accentuate this flavour.
http://articles.mercola.com/sites/articles/archive/2004/08/04/fermented-soy.aspx
Hydrolysis is a process whereby bonds are broken down chemically. In the case of hydrolysed protein, they are normally broken down enzymatically (using bacterial proteases). This results in a more bitter taste as more of the protein is in its constituent amino acid form. Hydrolysed protein is not usually 100% hydrolysed, and only a part has actually been hydrolysed, the rest remaining unhydrolysed. This may mean that the taste is not so bitter and more palatable. Hydrolysis of proteins (into hydrolysate) generally results in higher levels of free glutamate. Hydrolysed protein tends to contain glutamate at levels between 5 and 20%! Hydrolysed protein (e.g. hydrolysed soy protein) is sometimes used in place of MSG as a food additive as a flavour enhancer, but is rarely declared clearly on food labels as 'containing glutamate'.
This is why tomato sauces and fermented type sauces, and yeast extract based stocks are commonly used in cooking and added to processed food products.
Examples of hydrolysed proteins that are very high in glutamic acid include:
These are often present in dried packet soups or flavouring sachets. Some manufacturers may declare such products as 'MSG free'! Hydrolysed soy protein is often found in vegetarian and vegan 'meaty tasting' food products.
Much fuss is made by some anti-MSG campaigners about the non-hydrolysed soy and whey protein isolates and concentrates, and soy lecithin with respect to Glutamate content. One may want to take this with a pinch of salt, as the hydrolysed versions of these proteins are more of concern. Lecithin is largely oil and carboyhydrate based and contains very little protein.
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Glutamic Acid and Free Glutamate as Excitotoxins:
L-Glutamate (or Glutamic acid) is the most important excitatory neurotransmitter in the brain and plays an important part in brain chemistry. It is released by many different types of neurons and stimulates other neurons at the synapses. The excitatory neurotransmitters act to stimulate the next neuron (i.e. postsynaptic neuron) to fire an electrical impulse.
Inhibitory neurotransmitters tend to inhibit firing of neurons. The most important of these is GABA, which is synthesised from the amino acid Glutamine in the presence of Active Vitamin B6 (P5P). GABA is examined more on the Adrenal and Endocrine Systempage. Taurine is another, which performs many vital functions in the body, including nutritional metal transport into the cells. Taurine is examined in more detail on the Nutritional Deficiencies page.
GABA and Glutamate levels are balanced in the brain both in terms of absolute concentrations and relative ratios in a healthy individual. A P5P deficiency can thus result in an elevated Glutamate to GABA ratio in the brain and elevated levels of excitotoxicity. Excitotoxicity is the term used when the levels of the excitatory neurotransmitters are too high, at which point the level of neuronal activation or induced firing of neurons become neurologically damaging. Excitotoxins are a group of neurotoxins.
http://learn.genetics.utah.edu/content/addiction/reward/pathways.html
'Glutamate and GABA (gamma-aminobutyric acid) are the brain's major "workhorse" neurotransmitters. Over half of all brain synapses release glutamate, and 30-40% of all brain synapses release GABA. Since GABA is inhibitory and glutamate is excitatory, both neurotransmitters work together to control many processes, including the brain's overall level of excitation. Many of the drugs of abuse affect either glutamate or GABA or both to exert tranquilizing or stimulating effects on the brain.'
www.msgtruth.org/whatisit.htm
High levels of glutamic acid have been shown in animal studies to cause damage to parts of the brain unprotected by the blood-brain barrier, leading to a variety of chronic diseases.
http://en.wikipedia.org/wiki/Excitotoxin
'Excitotoxicity is the pathological process by which nerve cells are damaged and killed by glutamate and similar substances. This occurs when receptors for the excitatory neurotransmitter glutamate such as the NMDA receptor and AMPA receptor are overactivated. Excitotoxins like NMDA and kainic acid which bind to these receptors, as well as pathologically high levels of glutamate, can cause excitotoxicity by allowing high levels of calcium ions (Ca2+) to enter the cell. Ca2+ influx into cells activates a number of enzymes, including phospholipases, endonucleases, and proteases such as calpain. These enzymes go on to damage cell structures such as components of the cytoskeleton, membrane, and DNA.
Excitotoxicity may be involved in spinal cord injury, stroke, traumatic brain injury and neurodegenerative diseases of the central nervous system (CNS) such as Multiple sclerosis, Alzheimer's disease, Amyotrophic lateral sclerosis (ALS), Parkinson's disease, Alcoholism and Huntington's disease. Other common conditions that cause excessive glutamate concentrations around neurons are hypoglycemia and status epilepticus.'
I have personally experienced excitotoxicity, but in particular, when taking a supplement with a high Glutamate content, when excitotoxicity-based inflammation is already present, led to a bad headache and visual disturbances such as seeing extra shadows where there were none. This was relieved to some extent by taking some L-Theanine or GABA, but the excitotoxicity levels drop down to their 'normal' levels after a few hours.
There are four main classes of receptor that are stimulated by excitatory neurotransmitters. These are the AMPA receptors, kainate receptors, metabotropic receptors and N-methyl-D-aspartate (NMDA) receptors (discussed on the Nitric Oxide, Superoxide and Peroxynitrite page in regards to its role in excessive Nitric Oxide production).
http://en.wikipedia.org/wiki/Glutamic_acid_(flavor)#Excitotoxicity
Elevated free glutamate levels may also be linked to bipolar disorder (manic depression) and glutamate blockers such as Lamictal are sometimes used in its treatment. Trends that show increased suicide levels in US teenagers after its introduction into commercially prepared food sources and also huge increases in suicide rates in China may be illustrative of the effects of high free glutamate intake, or it may be a coincidence and explained on account of other factors.
http://www.msgtruth.org/foodfor.htm
Scientists are however not in agreement over the sensitivity of humans to excitotoxins, with some scientists believing that they do not affect humans, whereas others believe that humans are actually 4-5 times more susceptible to the effects of excitotoxins than primates and rodents. We can however look at examples of those suffering the effects of high free glutamate (including MSG) intake and their neurological symtoms. Links have also been made between MSG intake and increased obesity and raised blood glucose and insulin levels (akin to type 2 diabetes), although this is not solely on account of eating more processed foods, as MSG studies in rats illustrate.
www.msgtruth.org/body.htm
CFS and ME are believed to be hyper-excitory states, often with insufficient GABA production, resulting in neurological damage over time. Excessive free glutamate and MSG consumption in such cases is clearly an extremely a very bad idea.
Excitotoxins, e.g. NMDA, are also examined in the Peroxynitrite section on the Cardiac page.
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Side Chain Charge:
Of all the Essential, Semi-Essential and Non-Essential Amino Acids, only two have a negative side chain charge at pH 7, Glutamic acid and Aspartic Acid (the excitotoxins). All the other amino acids described above have a positive or neutral side chain charge at pH 7.
http://en.wikipedia.org/wiki/Amino_acid#Table_of_standard_amino_acid_abbreviations_and_side_chain_properties
Some have speculated that because of this negative side chain charge, these two non-essential amino acids are selectively more readily absorbed at the expense of other amino acids. If this is the case, the undigested protein, combined with an impaired digestive system in individuals with CFS, could result in an excess of undigested protein which in combination with a high refined sugar intake could lead to excessive candida overgrowth.
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Side Effects of excessive free glutamate consumption:
Some commentators report that the side effects such as 'hangover' type headaches associated with excessive MSG consumption are down to excessive salt intake and insufficient water intake.
www.food-info.net/uk/intol/msg.htm
Some studies have found symptoms including a temporary worsening of asthmatic symptoms, headache, nausea, chest pain, burning sensations, tingling, numbness, rapid heartbeat, drowsiness and weakness, at dosages of between 0.5 - 2.5g of MSG.
www.msgtruth.org/contents.htm
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Ways to combat the effects of excessive free glumate:
Besides decreasing one's intake of free glutamate, in terms of hydrolysed protein, MSG or yeast extract containing products, which is of course the obvious remedy to any problems associated with high free glutamate levels, there are a number of biochemical means to protect oneself or at least to make oneself more resilient.
There are a number of pre-disposing factors that can make an individual more susceptible to 'neurotoxicity' associated with excessive free glutamate levels. By addressing some of these, where applicable, one can reduce the effects. Some of these include vitamin B6 and B12 deficiencies, magnesium deficiency, Coenzyme Q10 deficiency, excessive vitamin A intake (vitamin A toxicity), and also taurine deficiency. Decreased liver function, diabetes and/or autism can also predispose one to excessive sensitivity. By ensuring one's intake of these is sufficient for one's requirements, and ensuring that one's is not taking in too much vitamin A and assisting proper liver function, one can negate much of the negative effects of one's free glutamate intake.
www.msgtruth.org/remedies.htm
www.msgtruth.org/why.htm
As mentioned previously, an amino acid analysis profile can be useful in determining if one's glutamate levels are too high or not, and indeed the overall balance of amino acids in the body; as indeed there are blood tests to verfiy the levels of the above cofactors and vitamins. Please see the Identification page for more information.
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Asparatame/NutraSweet:
Aspartyl-Phenylalanine-1-Methyl Ester, a.k.a. Aspartame, E951 or by the brand name NutraSweet, is an artificially synthesised , non-saccharide, amino acid-based sweetener. Aspartame (or APM) is the methyl ester of the dipeptide of the amino acids aspartic acid and phenylalanine. It is 180 times sweeter than sugar, weight for weight, but with no calorific content. Like many other peptides, aspartame may hydrolyze (break down) into its constituent amino acids at a temperature of 85F or 29.5C) or under high pH (alkalinity), including the carcinogen formaldehyde and the toxins formic acid and methanol. It is thus unsuitable for baking.
Aspartame is commonly used in 'diet' products like Soft Drinks, but also in many other supermarket food and drink products, to improve taste without adding calories. The popularity of Aspartame is on account of the general public's taste for junk food, soft drinks (sodas or fizzy drinks) and also sugary foods, and concern about weight gain (as opposed to health concerns) associated with these types of foods and this type of diet in general. Aspartame was seemingly the 'magic pill' when it was first introduced in the late 1960s, the answer to consumer prayers. However, it is regarded as being inferior in taste to sugar and although no conclusive evidence officially exists (presumably on account of 'low concentrations' of formic acid and formaldehyde being produced during its digestion in the body, rather than examining the cumulative effects over years), studies do suggest that it may play a part in a number of health conditions and diseases. Herbal-based sweeteners like Stevia and sugar alcohol sweetners like Xylitol have unfortunately been overlooked by the food and drinks industry.
http://en.wikipedia.org/wiki/Aspartame
'Upon ingestion, aspartame breaks down into residual chemicals, including aspartic acid, phenylalanine, methanol, and further breakdown products including formaldehyde, formic acid, and a diketopiperazine. There is controversy surrounding the rate of breakdown into these various products and the effects that they have on those that consume aspartame-sweetened foods. The naturally-occurring essential amino acid phenylalanine is a health hazard to those born with phenylketonuria (PKU), a rare inherited disease that prevents phenylalanine from being properly metabolized. Since individuals with PKU must consider aspartame as an additional source of phenylalanine, foods containing aspartame sold in the United States must state "Phenylketonurics: Contains Phenylalanine" on their product labels. In the UK, foods that contain aspartame must list the chemical among the product's ingredients and carry the warning "Contains a source of phenylalanine" Ð this is usually at the foot of the list of ingredients. Manufacturers should print '"with sweetener(s)" on the label close to the main product name' on foods that contain "sweeteners such as aspartame" or "with sugar and sweetener(s)" on "foods that contain both sugar and sweetener". "This labelling is a legal requirement", says the country's Food Standards Agency.'
Aspartic acid is an excitotoxin, and may contribute to neurological damage at high concentrations in humans. Please see the MSG section above regarding excitotoxins.
A list of reported side effects from aspartame use can be found at the links below. These have been refereed to as Aspartame Disease by some independent researchers. It has also been linked to some CFS cases.
www.healthdangers.com/drugs/aspertame/aspartame-health-risks.htm
www.321recipes.com/sunday_express.html
www.antiaginglifeextension.com/health_matters_minutes/articles/aspartame.asp?a=1563&c=&p=
www.aspartamekills.com/lydon.htm
Possible links to Gulf War Syndrome and excessive formaldehyde consumption with soft drinks cans being stored outside in the desert sun for extended periods of time is discussed on the Acidosis page and at the links below.
www.aspartamekills.com/mpvalley
http://www.wnho.net/aspartameandgulfwar.htm
www.militaryspot.com/gulf-war-syndrome.htm
The Food Standards Agency in the UK issued the following statement about APM.
www.food.gov.uk/safereating/chemsafe/additivesbranch/sweeteners/55174
The web site Green Facts has made the following statements about APM, denying any scientific basis for health concerns.
www.greenfacts.org/en/aspartame
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General Digestive Enzyme and Stomach Acid Deficiencies:
As discussed above, the term Food Intolerance is usually applied to the specific digestive enzyme deficiencies and the subsequent inability to efficiently digest certain types of carbohydrate. However, as many sufferers of CFS and related conditions can vounch for, and a discussed above, the digestive system as a whole may be somewhat impaired, meaning a broader spectrum of food groups may be less efficiently digested if large volumes of food or large amounts of a particular food type are consumed at once. Some may wish to define Food Intolerance as only the former more specific type, and call the latter type a more generic type of gastrointestinal malabsorption or digestive dysfunction. Indeed such digestive dysfunction may develop as a result of the former type and also Secondary Immune Response as described above. Both are however caused largely by a lack of appropriate digestive enzymes.
A list of digestive enzymes can be found at the link below, according to the food groups digested.
www.enzymestuff.com/basicswhichenzyme.htm
Carbohydrate intolerance need not be restricted to the carbohydrates listed above. Whilst bacteria thrive most readily on undigested or unabsorbed sugars and carbohydrates in the digestive tract, they can also break down and rot proteins. This is a more generic type of food 'intolerance'. The presence of dysbiosis may also contribute to the IBS symptoms experienced by CFS sufferers for a variety of food sources.
Such food intolerances may thus be more generic in nature, being a result of inefficient digestion of certain types or multiple types of food group, because of a general deficiency in digestive enzymes, or certain classes of digestive enzymes, e.g. sufficient stomach acid levels and protease enzymes for digesting protein; lipases and bile for breaking down and digesting fats and oils, etc. Part of the problem may also be the inefficiency of absorption of nutrients from the digestive tract into the villi and into the blood stream. This may be a result of excessive a lack of enzymes to carry across nutrients from the digestive tract to the blood stream, resulting in further nutritional deficiencies and digestive dysfunction; it could be because of damage to the villi in the gut, effectively shortening them, because of Celiac Disease; it could be because of excessive build up of mucoid plaque in the colon which physically limits the amount of absorption of digested nutrients; or indeed a lack of blood supply or oxgen to the cells of the digestive tract, etc. on account of impaired cardiac output or stress.
Wind can be used as a rough guide to what types of foods are not being digested properly in the amounts they are being consumed in. The types of wind can be categorised into three main areas, depending on how it was generated.
One may indeed experience just one type of such wind, specific to the foods that one cannot digest properly, or two or three kinds, a different type of wind at different points of the day according to what one has eaten hours before.
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General Food Considerations:
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Gluten:
Triticeae is a tribe within the Pooideae subfamily of grasses, including genera with many domesticated species. The major crop genera found in this tribe are wheat, barley and rye. (Bread) Wheat contains the genomes of 3 different species, only one of them originally a wheat Triticum species. The seed storage proteins (Gluten) in Triticaeae are implicated in various food allergies and intolerances.
http://en.wikipedia.org/wiki/Triticeae
Triticeae glutens are the seed stoage proteins in the mature seeds of the grass tribe Triticeae. The term 'Gluten' is used to describe the factors in bread wheat that give rise to the sticky property that allows dough to rise and retain its shape during baking. The same or very similar proteins are found in other Triticeae genera and species, but bread wheat contains the highest content and highest level of subcomponents, being a complex mixture of 3 grass species, Aegilops speltoides (Goatgrass a.k.a. Triticum speltoides), Aegilops tauschii - subspecies - strangulata (a.k.a. Goatgrass) and Einkorn wheat (Triticum monococcum), one of the earliest domesticated species.
The grains of non-Triticeae taxa also contain seed glutens with similar properties but do not match the 'performance' of Triticeae taxa and of these, particular the Triticum species (bread wheat, durum wheat etc.) Bread wheat has been optimised by cross fertilisation and hybridisation over millennia to offer the greatest elasticity, highest protein content and also a high cold weather resisistance. Wheat growing originated in Mesopotamia and Egypt.
http://en.wikipedia.org/wiki/Triticeae_glutens
Bread wheat is an allohexaploid, an allopolyploid with six sets of chromosomes, two homologous pairs or sets from each of three different species. It has undergone several millennia of hybridisation, and is somewhat far removed from the original wild grass species that were originally found and grown in the Tigris-Euphrates river-basin.
http://en.wikipedia.org/wiki/Common_wheat
The four categories of Triticeae seed protein are as follows.
Of these four types of protein, the last two, Prolamin and Glutelin are what we consider to be constituents of Gluten in all Gluten-containing grains (Triticeae and non-Triticeae grains).
http://en.wikipedia.org/wiki/Prolamin
'Prolamins are a group of plant storage proteins having a high proline content and found in the seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein) and as a minor protein, avenin in oats. They are characterised by a high glutamine and proline content and are generally soluble only in strong alcohol solutions. Some prolamins, notably gliadin, and similar proteins found in the tribe Triticeae (see Triticeae glutens) may induce coeliac disease in genetically predisposed individuals.'
http://en.wikipedia.org/wiki/Glutelin
'Glutelins are soluble in dilute acids or bases, detergents, chaotropic or reducing agents. They are generally prolamin-like proteins in certain grass seeds. glutenin is the most common glutelin as it is found in wheat and is responsible from some of the refined baking properties in bread wheat. The glutelins of barley and rye have also been identified. Typically there are HMW and LMW glutelins in these species, they crosslink with themselves and other proteins during baking via disulfide bonds. A HMW glutelin (glutenin) of the grass tribe Triticeae can be sensitizing agents for coeliac disease in individuals who possess the HLA-DQ8 class II antigen receptor gene (not yet characterized to the epitope level.)'
http://en.wikipedia.org/wiki/Gluten
Gluten in bread wheat is a composite of two proteins, Gliadin (a Prolamin and a form of glycoprotein (sugar containing protein), and Glutenin (a Glutelin), combined with starch. It is located in the endosperms of certain grass-related grains.
http://en.wikipedia.org/wiki/Gliadin
The highest Gliadin concentrations can be found in the Triticeae grains Wheat, Barley and Rye. Giadin in bread wheat is encoded by 3 different genomes, AA, BB and DD. These produces slightly different Gliadins, which the body that can potentially produce different antibodies against. In general, Gliadin is the component of what is referred to as 'true Gluten' that is most generally associated with food allergies and intolerances.
http://en.wikipedia.org/wiki/Glutenin
Glutenin gives a grain flour its elasticity and grains high in Glutenin and Gliadin have been favoured historically as they are optimised for bread making. Gliadin is the most common constituent of Gluten that adverse immune system reactions occur with, although Glutenin can also be problematic for many.
As stated above, there are other grains and cereals of course that contain Gluten, but in a different form than in the Triticeae tribe. When most people and manufacturers refer to Gluten, they really mean Gliadin, from Wheat bread Gluten, or the Glutens of Rye and Barley, i.e. specifically the Gliadin and Glutenin content. Thus 'Gluten-free' really means Gliadin-free (and Glutenin-free), not necessarily Gluten free at all. However, most people assume or come to assume that Gluten to only mean 'true Gluten'.
Some other cereals and grains are listed below.
Maize and rice for example contain proteins that are sometimes referred to as Glutens, but they do not contain Gliadin. Avenin, the Prolamin in oats, is known to be toxic to the intestinal submucosa in some Celiac Disease patients, although it is generally considered to be the least reactive of the grains. Rice gluten is the most significantly different in its chemical structure, but some may have an allergy or intolerance to it (i.e. an immune system mediated response). Basmati rice tends to be the best tolerated form and rice bran may cause a reaction in some individuals, on account of its higher protein concentration. Wheat breadcrumbs can be found in many coated or battered foods, and also in sausages.
As a general comparison of the highest risk gluten grains for those with food intolerances, one could follow this sequence in increasing order of likelihood of reaction: maize, oats, barley, rye, spelt, bread wheat.
http://infantrefluxdisease.com/infant_acid_reflux/food-intolerance.php
www.allergyuk.org/fs_gluten.aspx
Types of Gliadin-free flour include:
These flours cannot be used as a straight swap for Gliadin-containing flour as they do not have the elasticity and will tend to crumble during bread making. However, they can be used as thickeners in sauces, and if combined with binders suach as grated apple, pectin powder, eggs and methyl cellulose, they can be used for pastries and bread-making. Alternatives include rice crackers, although these may be too high in simple carbohydrates (c/f Candida overgrowth or dysbiosis etc.) You can also buy/make buckwheat soba noodles, made with 100% wholegrain buckwheat.
Some of the highest Gliadin concentrations may be found in wheat extracts, such as wheat bran and wheat germ. Wheat bran, the outer hard casing or hull of the storage seed, is approximately 15.5% protein by weight. Wheat germ, the 'embryo' fraction of the seed, which is highest in lipids (and most susceptible to going rancid as a result), is approximately 30% protein! Normal wheat flour (based on the endosperm of the grain) is approximately 11% protein. Four used in pastry making is approximately 9% protein. Whole grain wheat flour and high gluten flour are approximately 14% protein. Wholegrain flour has a shorter shelf life than white flour on account of the germ and bran component going rancid more quickly.
Certain types of bread contain wheat flour with 'extra Gluten' added, in order to make them stronger. Examples include French sticks or French bread.
If you have a reaction to the higher protein (higher bran) versions of specific grains and cereals, then you may choose a lower protein form of them which you do not have any reaction to, for occasional consumption. Or perhaps just choose another grain to eat which provokes no reaction, even in the higher protein/fibre forms. There is clearly a balance between consuming enough fibre and avoiding proteins that cause you a reaction to. By consuming large quantities of a grain with little fibre is not going to do you any good if you have an issue with dysbiosis, or indeed may encourage dysbiosis over a period of time. Indeed, a lack of fibre may also cause an excessive build up of mucoid plaque. So if you are cutting out fibre in one area, you should make sure you are getting it from another source. And eating large amounts of any 'white' grain is perhaps not the best way of consuming carbohydrates, as complex carbohydrates are better. There is therefore potential for conflict with the Anti-Candida Diet and the Gluten Free Diet. As Food Intolerance can fuel the growth of dysbiotic and pathogenic micro-organisms, then one may well need to keep both in consideration, as even on an Anti-Candida Diet, if you are eating foods that you are intolerant to, then you are still fuelling the bacteria and attempts to kill them off may be ineffective.
True Gluten (or Triticeae tribe gluten), whilst found in fairly high concentrations naturally in wheat, barley and rye grain products, is found in significant concentrations in certain condiments and foods, as an additive or by food processing. e.g. as a stabilising agent in ice-cream and ketchup, which arguably have little nutritional value and contain refined sugar in any case. Such sources of Gluten are often referred to as Hidden Gluten.
It should be noted that the actual grass component of wheat and barley do not contain the protein Gluten, but contain proteins in other forms. Wheat grass and Barley grass are vegetables, and therefore technically speaking Gluten-free in an idealised manufacturing process. However, given the fact that some other grain products such as oats frequently contain traces of wheat (e.g. up to 70% of US oat stock is contaminated with wheat gluten), as they are either harvested at the same time as wheat or use the same processing equipment, then it is all the more likely that wheat grass and barley grass may similarly be contaminated with traces of actual Wheat or Barley grain. One may wish to consider this if one regularly consumes cereal grasse juice or powders. Some Barley Grass powders make statements such as 'Wheat Free' on the packaging - but not state Gluten Free! That is not to say that it does not contain traces of Barley grain and thus Gluten.
A widely quoted statement made by Cynthia Kupper, Executive Director of the Gluten Intolerance Group (GIG) of North America (www.gluten.net):
'According to information from USDA research chemists, specializing in wheat gluten and cereal proteins and a statement from the American Association of Cereal Chemists, gluten is found only in the seed kernel (endosperm) and not in the stem and grass leaves. If the grass is cut from a growing plant and does not include the seed kernel, it should be safe for persons with gluten intolerance to use. Wheat and barley grass are promoted as having superior nutrients, however the nutrient composition of the grasses is not superior to eating a variety of fruits and vegetables, which would be overall more healthy and less expensive than using this supplement. Bottom line is that I would stay away from it at this time and eat more fruits and vegetables!ÊMy personal and professional choice is not to use these products.Ê Instead, rely on a variety of gluten-free grains, fruits and vegetables for a nutrient-rich diet.ÊFeel that you must include a grass in your diet; I would recommend alfalfa grass instead of the wheat or barley grass.
As for sprouted wheat or other gluten-containing grains. These are sometimes used in breads that claim to be gluten-free. In talking with many of these bread companies, they claim their breads have no gluten, but none can guarantee that the seed kernels are completely removed before the sprouts are used or that their products have been tested for gluten content. This presents an unacceptable risk for persons with gluten intolerance. GIG does not recommend these products on a gluten-free diet.'
If you grow and harvest your own Wheat grass or Barley grass, growing them in a small tray or otherwise, then you can be sure they are Gluten-free of course; assuming you know what you are doing and they are harvested before the grasses have matured to the stage where they produce grains. For those who like green superfoods, one can however rest assured that algae-based foods like Spirulina are going to be 100% Gluten free!
There are sources of Gluten-free cereals, such as Hale & Hearty Gluten Free Oats. However, they are perhaps 2-3 times more expensive than ordinary oat sources. However, if one is sensitive to Gluten, then they may be an alternative. That is not to say that the given person may not be allergic to Oats or indeed Rice. For example, in January 2010, I tried one brand of organic Gluten Free Oats, and developed a sore throat a short while afterwards in a similar fashion to regular organic oats.
Certain supplements contain Gliadin on account of its resilience to stomach acid, and as such is used Gliadin is used as a delivery mechanism for certain fragile/sensitive enzymes, such as Superoxide Dismutase (SOD), which is fused with Gliadin to form GliSODin. GliSODin is a registered trademark. It is usually described in the ingredients in the relevant products as 'Superoxide Dismutase/Gliadin Complex (GliSODin), e.g. Life Extension SODzyme.
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Milk Dairy:
For a detailed analysis of the composition and digestion of Lactose, milk sugar, please see the Metabolic Food Intolerances section above.
For some individuals, the (immune system mediated) intolerance or allergy to milk may be caused by the denatured protein of pasteurised as opposed to the non-denatured protein of raw (unprocessed and non-heat treated) milk. This may also be true for whey powders that use a non-heat treated whey source. Certain whey powders included partially digested whey protein, which may also help. If the immune system is reacting to the protein component of dairy products, then clearly the higher concentration dairy products may be more problematic as they contain more protein, for example, whey protein or cheeses.
www.allergyuk.org/fs_milk.aspx
Depending on the type of food intolerance you may have towards dairy, it can affect which types of dairy products you can tolerate more than others. Avoidance is probably the best strategy, but in some cases, occasional consumption may not cause any noticeable symptoms. Milk products are 'hidden' in a variety of food types where they are not normally expected to be found.
The predominant protein in cow's milk is Casein. Casein is a type of phosphoprotein and makes up approximately 80% of the protein content in milk.
http://en.wikipedia.org/wiki/Casein
Whey, a.k.a. milk plasma, is the liquid remaining after milk has been curdled and strained. It is also the by-product of cheese or casein manufacture. Some harshly refer to it as a waste. It has a number of health benefits for those who are not sensitive to dairy. Whey protein are the globular proteins (globinstagers) isolated from massive whey, typically 65% beta-lactoglobulin, 25% alpha-lactalubmin and 8% serum albumin. Whey has the highest known biological value (BV) of any known protein (100). BV is a measure of how efficiently a substance can be digested and absorbed through the villi of the small intestine into the blood stream, maintaining its original form.
http://en.wikipedia.org/wiki/Whey
Cow's milk is quite rich in protein and less watery compared with the milk of other animals,e.g. Goat's milk, and also Human mother's milk. This is why cow's milk is favoured in general. However it is the same reason that it is thought to cause more immune system reactions in susceptible people. If you are allergic to cow's milk, consuming less of an antigen is by no means the same as consuming 'no antigen', and Goat's milk should not be considered more than just 'less problematic'. It is still likely to be a problem in susceptible individuals.
Butter may be tolerated by some as it is mostly milk fat and water, containing little protein, and others may tolerate UHT milk but not normal pasturised milk.
If the lactose content of dairy products are causing a problem (i.e. metabolic food intolerance), It is likely that hard cheeses, such as Swiss, Emmental and Parmesan, will be best tolerated as they contain no lactose (all used up in fermentation and cheese production). Otherwise, live fermented milk products such as natural yoghurt or kefir will be lower in Lactose, the probiotic bacteria and yeasts having consumed some of the Lactose already (depending on the duration of fermentation). Lactose intolerance usually means one can tolerate a small amount of lactose but more than a certain amount, it will start ot appear further down in the intestines where it should not be. Therefore, one may still be able to consume milk, but just in very small amounts, e.g. with a cup of tea. Drinking a glass of milk or having cow's milk with your breakfast cereal (which may itself often contain milk powder as well as large amounts of refined sugar).
Infants should ideally be breastfed with their mother's milk rather than being given infant formulas or warmed cow's milk, which is intended for the infants of those animals. Even soy contains too many phytoestrogens that can affect a child's hormone balance. It is amusing to think that adults think the idea of drinking the milk from a woman's breast is disgusting but would happily drink milk that came from an animal's breast. Arnold Schwarzenegger was asked in the movie Pumping Iron by an interviewer whether he drank a large amount of milk to help with his muscle growth, he responded 'When I go out, I like to have a beer. Milk is for babies!'
I am not suggesting that beer drinking is very healthy either, but it is an amusing but poignant quotation in many respects.
Growth hormones are only still used in the USA. Some commentators generalise and imply that artificial growth hormones are used in all non-organic animal farming, but this is not strictly true. Bovine Growth Hormone (BGH), a.k.a. Bovine Somatotropin (BST), is a protein growth hormone produced in cattle. A synthetic version of the hormone was first created in 1994, known as recombinant bovine somatropin (rBST) (a.k.a. recombinant bovine growth hormone or rBGH or simply artificial growth hormone). rBGH has been used to make cow's grow bigger and to produce more milk volume. Milk from rBGH treated cows contains higher levels of IGF1 (Insulin-like Growth Factor 1) and also contains small amounts of puss where the too much milk from the rBGH has caused inflammation of the udders. IGF1 has not been conclusively proven to be detrimental to human health (and linked to an increased cancer risk) although studies on rats have revealed that it has a slight element of toxicity. The brand is Posilac, currently owned by Elanco Animal Health, a division of Eli Lilly & Co. rBGH was banned in Canada, Australia, New Zealand and most of Europe by 2000. Imported milk or beef from rBGH treated animals to these countries is not permitted, but convenience foods and condiments containing dairy ingredients from the USA (regardless of source) are permitted strangely.
http://en.wikipedia.org/wiki/Bovine_Growth_Hormone
Milk can be a nutritious addition ot one's diet in moderation, if one's immune system can tolerate the protein, and one has sufficient lactase enzymes to deal with the lactose. There are many other dietary sources of Calcium, for example, Soya milk, various beans, sesame seeds, brazil nuts, hazelnuts, okra, spring greens, water cress, parsley, and some fruits. Please see the Nutritional page for more information. Some even argue that regular dairy consumption prevents the absorption of Calcium and causes osteoporosis (on account on too high a Calcium intake.
www.youngerthanyourage.com/4/ExcessiveCalcium.htm
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Other Food Types:
Hazelnut is a food type that is sometimes identified in IgG blood testing as being a food that one reacts to. However, some commentators argue that this is a reaction, but not an allergic one (despite the test result). The Hazelnut protein is irritating to the tongue and it titillates the palate in small doses. This is why Hazelnuts are often used by Chocolatiers as opposed to other nuts. I have always wondered why Hazelnuts were used as they were never his favourite nut particularly.
One could however interpret this behaviour of hazelnuts as being reflecive of Oral Allergy Syndrome, that is a cluster of allergies (including IgE) in the mouth (typically burning sensation or itching of lips, mouth and/or pharynx) to eating certain fruits, nuts and vegetables, typically noted in hayfever sufferers who have cross-reaction with compounds in these foods that appears similar to birch pollen. These foods can include: apples, hazelnuts, peaches, cherries, almonds, pears, carrots, and celery. The symptoms are arguably somewhat different to those the majority of people who eat hazelnuts without itchy lips etc. It is more of a mild (physical) irritation to the tongue as opposed to an immune system-mediated response that affects more parts of the head and throat.
http://en.wikipedia.org/wiki/Oral_allergy_syndrome
Tomatoes are a type of fruit that is frequently implicated in IgG reactions in susceptible patients. Some commentators argue that this is on account of their acidity or because of the properties of their skins (perhaps not having been washed properly and still being high (in relative terms for a person with multiple chemical sensitivities) in pesticides etc.) Sufferers tend to experience fewer symptoms when the Tomatoes are cooked than when eaten raw. Tomatoes are very high in antioxidants (as are other red fruits). Cooking tomatoes also helps to free up the lycopenes (red carotene pigment and phytochemical). Lycopene is considered helpful in preventing prostate cancer.
http://en.wikipedia.org/wiki/Lycopene
However, it should be noted that Tomatoes are rich in fruit sugars and also free glutamate, and may not be suitable for someone on an Anti-Candida Diet or who has Fructose-related disorders, or for someone who has a sensitivity to Glutamate/MSG.
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Natural Selection:
Some commentators have argued or theorised that before agricultural societies evolved, those individuals that had more sensitive immune systems were generally better adapted to the natural environment than those who did not, as they were better able to seek out and destroy viruses and other infections in their bodies. Those individuals with antibodies that were less reactive were perhaps less inclined to survive, and more likely to fall victims of Natural Selection. Thus the law of Survival of the Fittest would dictate that more individuals with sensitive immune systems survived in each subsequent generation. The genetic and phenotypic predisposition to mistaking certain protein forms as viruses is from one perspective a good thing. However, with the advent of commecial food production and agriculture, and especially with hybridisation, this characteristic of having a more sensitive immune system then becomes a potential hazard to one's health, if one is not aware of the situation, well informed and that one is consuming proteins that resemble toxic and pathogenic viruses. Thus one could argue that modern society from a Neo-Darwinian perspective encourages the weaker and less robust and punishes the naturally 'stronger', thus creating a genetic disadvantage in the human gene pool, which as discussed above, arguably affects large segments of the population, who may be more prone to developing other allergies, asthma or even autoimmune diseases.
However this is not to say that the human body cannot adapt to som extent, and the various protocols to taming the immune system described below bear witness to this fact. In addition, when it comes to non-genetic metabolic food intolerances, e.g. Lactose Intolerance, over generations, a population may develop the ability to produce more Lactase, perhaps not through 'Natural Selection' as the 'ill' do not just die off or stop having children, in general, they just have a more miserable existence.
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Good vs Bad Foods:
Some argue that there is nothing intrinsically wrong with any of the food sources that cause food sensitivities in some individuals, and in those individuals who do not suffer from these problems, they are a good source of nutrition.
Others, such as Dr Kenneth Fine of Enterolab, and various other natural living and natural food promoters, argue that Gluten containing grains and indeed milk, are 'unnatural' food sources. Some of the reasons for this have been discussed above. In addition, the majority of the population of the USA, for example, has some genes associated with Celiac Disease, even if excessive ATA production has not yet manifested itself, and that eating Gliadin over the long term may be a high risk strategy, as one might possibly develop a propensity towards Celiac Disease later in life. Thus Kenneth Fine argues that adopting a Gliadin(Gluten)-Free Diet is a sensible strategy for preventative medicine and health.
Whether such proteins are 'toxic' as they resemble viruses is another matter. However, there is considerable evidence to suggest that consuming large quantities of gluten containing foods, especially Gliadin, and indeed dairy consumption is not something the human body is generally geared towards digestiing; nor indeed has been geared to digesting over the 10s of thousands of years we have been Homo sapiens; and many 100s of thousands of years and indeed a million or so years in pre-hominid species. These are convenience foods, in the case of wheat, that have allowed modern society to evolve. In the case of Dairy, it is perhaps more of a vice than anything else!
Wheat and dairy do not appear to be particularly good for anyone, it is perhaps more a case of how much the irritation they potentially cause bubbles over the surface into immunological and other factors that are deemed to be significant or not. It depends where you want to draw the line perhaps. This is true for many other foods of course, but particularly more so with Wheat and Dairy. There are many other food sources available and it depends on your own personal judgement and choice at the end of the day, as it is your body. But seeing as many of the reactions to foods go unnoticed, it might be wise to at least investigate whether you do have any forms of Food Intolerance or not.
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Detection:
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Observation, Elimination, Reintroduction:
One can observe the symptoms of food allergy, intolerance or sensitivity through observation of symptoms after eating certain food types, how and when they occur. Most people are familiar with their allergies if the symptoms are very severe, but if they are mild, and they are not familiar with the range of possible IgE food reactions or indeed, other immune modulated food sensitivities, and signs of food intolerance, then they may not believe there is a problem with the food types they are eating.
The easiest way to identify the potential problem foods is through testing, and totally eliminate them one's diet (e.g. start a gluten- or dairy-free diet); as otherwise the traditional 'elimination diet' involves removing one food type at a time from one's diet and observing symptom changes over many weeks, and then reintroducing it and starting on the next food type, but without any direction or prior knowledge, this is a very slow alternative.
If one eliminates certain food sources, one should only do so with the advice of a nutritionist so that one does not omit any important food groups or nutrient sources. Elimination means replacing one thing with another, in order to maintain one's calorific intake and also to ensure one is not losing sources of nutrition from one's diet. Elimination does not simply mean that one will skip breakfast because one cannot eat whatever food type one is used to eating at that time.
One example of an elimination diet is the Gluten-free or Dairy-free diet. If one is wanting to eliminate the food type to allow the symptoms of the food intolerance to subside, before one reintroduces it as a 'food challenge' to see whether there really was a reaction or not, then the recommendation is to avoid that food type for a minimum of two weeks. Some practitioners recommend 3 months, but this may perhaps pose a different type of approach, where one is looking not just to identify a food intolerance but to treat it.
One may find that one has cravings for some of the food types that one has eliminated or a possible worsening of symptoms during the first couple of days of avoidance/elmination. This is not uncommon and is nothing to be concerned about. This may be partly due to the body wanting to continue its disequilibrium and that avoidance starts to create a physiological change in the body that feels new and strange. It may also be due to excessive physiological adaptation to simple carbohydrate consumption or for other reasons. It is perhaps in some sense like breaking a bad psychological habit, the mind has cravings to go back to its own habit, even though it is not in its best interest.
During the avoidance phase, one can note any changes in how one feels, and either stick to this new regime, or experiment with reintroducing some of the suspected problematic foods (in significant quantities if one knows one does not have an IgE reaction to them - after at least 2 weeks) and notice what effect it has on the body. If one starts to feel better whilst eliminating a certain food type, then this may well indicate that one has a food sensitivity to this particular item.
Reintroduction, a.k.a. food challenge should be a single portion of that food item, and careful observation of symptoms over the next few hours. If no observable symptoms are noticed, then one may elect to eat another portion of that food type the following day. and assess for symptoms again. If the symptoms are severe, then you should avoid this food type for a prolonged length of time. This reintroduction or food challenge should verify whether one's suspicions were correct or not. If the challenge symptoms are mild, you may want to consider only eating it occasionally.
Another variant on the food challenge is to eat a very large amount of that particular food type of the day of the food challenge (after a 2 week total elimination), and then avoid it again for 2-3 days, all the while observing the effects. Continue with the avoidance of that food type and move onto the next food challenge (of the next food type, 2-3 days after the previous food challenge). This assumes that you stopped eating all the food types to be tested/challenged at the beginning.
Reintroduction of certain food types (a.k.a. food challenge) after only brief elimination may well result in a swifter and stronger response than was experienced when the food types were consumed every day or regularly. This can be useful if one is looking to simply identify a food intolerance reaction, but if one is looking to treat the food intolerance, then clearly one should try to aim for prolonged avoidance. Certain food types you may wish to avoid for months or years or indefinitely.
In general, prolonged avoidance tends to build tolerance. When you reintroduce the food type after careful avoidance for weeks or months, the reaction to the food may be diminished. However, copious and regular consumption of that food type again may well build up the adverse reaction again.
Be aware that just because you are avoiding Gliadin for example, if you are Gliadin sensitive, does not necessarily mean that your gut will improve significantly, if there are other complications involved. If you have significant levels of mucoid plaque and bacterial and candida overgrowth and you are simply eating low fibre, high carbohydrate gluten-free foods (e.g. Gluten-free comfort foods, soya milk and cornflakes), your IBS-type symptoms may not improve, and indeed may become much worse. Equally, if you are substituting foods for those you have eliminated, be aware that you may be introducing foods that you are intolerant to. You have to take all factors into consideration.
A structured approach to elimination and reintroduction, as part of taming food allergies and sensitivities, is discussed in the next section. One should determine what one's approach and strategy should be from the outset or one will invariably end up being unstructured and achieving very little at best.
It is useful to keep a food diary and note any changes in symptoms in this each day and/or each week, and one can go back and refer to this, when excluding further foods from one's diet. It is also recommended to do the above in conjunction with a qualifiied nutritionist and allergy specialist, who can provide you with advice and monitor your progress as you go along. It is a common occurrence for over-zealous parents to simply eliminate certain food types from a child's diet, often erroneously (i.e. misidentification of the problem foods) and not replace that food type with anything else suitable for the child's nutritional needs.
One should note that the presence of other diseases and conditions (e.g. microscoptic colitis) may mask the change in symptoms one would normally have experienced with an elimination diet.
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Hydrogen Breath Test:
Food Intolerance, i.e. the absence or low levels of specific digestive enzymes, can be detected formally by a Hydrogen Breath Test. This works on the basis of ingesting a fixed amount of a given type of sugar, and breathing into a Hydrogen gas detector every 20 minutes for a period of 2 hours. If the sugar is not digested properly, then there will be a rise in bacterial activity to ferment that sugar. One of the byproducts of such fermentation is Hydrogen gas, which is absorbed into the blood stream and is dissipated out of the lungs in the breath. In general, hydrogen levels tend to rise moderately if one is not intolerant, but rise massively if one is.
Please see the Tests page for more information.
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Antibody Testing:
IgA, IgE, and IgG antibody testing for a variety of food types is available in the form of blood tests and stool tests.
For IgE testing, i.e. for food allergies, a RAST (RadioAllergoSorbent Test) blood test is usually employed, to detect the levels of IgE antibodies present in blood plasma to a particular antigen or antigens being tested for. Some critics argue that most laboratories who provide IgE testing do not request/take a large enough blood sample to do the testing properly and so the blood tests often come back negative. It may be best to enquire with a particular laboratory as to their test methodology, how much blood they require and how it compares with the next one.
Whilst IgG blood tests are quite convenient, the localised IgG and IgA levels in the colon may be elevated in response to certain food types, and the levels in the blood stream may not be detectable at a given stage in one's condition. IgG blood testing is arguably still not clinically verified, and a negative or indeterminate result for IgG antibodies for Gliadin (for example) does not necessarily mean you definitely do not have a sensitivity to Gliadin. Observation of symptoms may perhaps be more reliable. However it can still be a useful tool, especially as it can cover so many possible food sources in one test, and if used in conjunction with other forms of testing and observation.
Celiac Disease Testing is usually performed by measuring levels of anti-tissue transglutaminase (tTGA) and anti-endomysium antibodies (EMA) in the blood or preferably the stools, in other words a method of detecting Celiac Disease (the resulting inflammation) before it has actually developed. These anti-tTG antibodies and anti-Gliadin antibodies are not generally found in the blood of many Celiac patients. Detection of these antibodies in the stool is however 100% reliable.
Please see the Tests page for more information.
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Intestinal Malabsorption Testing:
Intestinal malabsorption is one indicator of the progression of genetic Gliadin sensitivity to the point where symptoms of Intolerance are occuring (i.e. Celiac Disease). The shortening of the intestinal villi will result in less absorption of nutrients and thus a great proportion of unabsorbed or bacterially fermented nutrients in the stool. Of course, there are a number of other reasons why intestinal malabsorption can occur, and may be related to metabolic food intolerance (i.e. genetic or phenotypic deficiency in a particular carbohydrate enyzme, e.g. Lactase), or it may be due to a more general deficiency in enzymes that is acquired, e.g. that present in CFS, ME and Fibromyalgia patients, with deficiencies in stomach acid and enzyme production (i.e. biochemical problems resulting in these deficiencies in production). A test for intestinal malabsorption is therefore a direct measure of the intestinal damage caused by Celiac Disease, unlike Antibody levels, assuming no other factors for intestinal malabsorption are operating. In many cases an intestinal malabsorption test provides inform about both Celiac induced villi damage and also any insufficiencies in pancreatic enzyme production. It is difficult to separate out the two. Antibody tests can however tell you about damage that may be occuring now and/or that will be occurring in the future unless one changes one's diet.
There are various different stool tests available to detect for intestinal malabsoprtion, some of which are specifically for Celiac Disease (e.g. Enterolab) or geared towards dysbiosis (e.g. Doctor's Data) which still examine some of the same parameters. Regular stool tests may also shed some light on the possibility of Celiac Disease, in particular stool pH, Lymphocyte counts, the presence of (undigested) fat stains etc. Neither of these are 72 hour stool collections, collecting all stool in that period (!), as with some older types of tests, but are single collections.
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Genetic Testing for Celiac Disease:
The genes that control the immune system's reaction to Gliadin (Gluten) are the Human Leukocyte Antigens or HLAs. There are several types of HLA genes with each person, the HLA-DQB1 locus type being the most useful in determining the probability that a person may be sensitive to Gliadin. HLA-DQB1 alleles belong to the HLA-DQ2 serotype group.
The presence of the genes (or HLAs) associated with Celiac Disease and Gluten Sensitivity in the tissue Transglutaminase, when combined with Gliadin stimulates the body's immune response. Each HLA-DQx is a Human Leukocyte Antigen Serotype within the HLA-DQ serotype group. Each DQ class gene contains two heterodimers or gene pairs (alleles), which together form the DQ heterodimer, a cell surface receptor essential to the function of the immune system.
www.enterolab.com/StaticPages/Frame_Faq.htm
The older style 'serologic' type used to describe HLA-DQ genes include the numbers 1 to 4, i.e. (HLA-)DQ1, DQ2, DQ3 and DQ4; including integeric types , DQ5 and DQ6 as subtypes of DQ1; DQ7, DQ8 and DQ9 as subtypes of DQ3. Because the actual protein structure on the cells, as determined by the serologic typing, that determines the gene's biological action, genes with the same serologic type tend to function almost identically, biologically speaking, e.g. HLA-DQ3 subtype 8 (one of the main Celiac genes) compared with HLA-DQ3 subtype 7, 9 and other DQ3 sub-subtypes.
In the USA, of those suffering from Celiac Disease, the following genes seem to be implicated in causing the production of the Anti-tTG Antibody production that results in villous atrophy.
Studies to date show that for Gliadin/Gluten Sensitivity to result in Celiac Disease (i.e. the villous atrophy of small intestine), it requires at least 2 other genes also. Thus, not everyone with DQ2 or DQ8 will develop villous atrophy when ingesting Gliadin regularly.
Dr Kenneth Fine believes that anyone with thes above genes will incur some sort of immune response to Gliadin. According to Fine's latest research, when DQ1,1 and DQ3,3 are present together in the same individual, they result in far more severe immunological responses to Gliadin that if one only had one of the Celiac Genes alone (e.g. DQ2,2, DQ2,8 or DQ8,8 which tend to portend a severe form of Celiac Disease).
Considering the US population as a whole, a total of 81% have genes predisposing them to Gluten sensitivity, in varying degrees. The main Celiac genes however still constitute 43% of the US population.
Of the remaining 19%, most have DQ7,7, a pair (allele) almost identical in structure to DQ2,2 (the most predisposing of all the Celiac genetic combinations), which Fine has found have very high Anti-Gliadin Antibody counts in. He postulates that it is only really those who have DQ4,4 that have no genetic presdisposition to Gluten sensitivity at all - a rare gene combination in Northern America.
Of those with at least one DQ1 pair (allele) - the second digit denoting the second of the DQ pairs:
www.enterolab.com/StaticPages/Faq_Result_Interpretation.htm
Dr Kenneth Fine believes that because testing for the HLA-DQB1*201 locus type as opposed to testing for both it and its heterodimer HLA-DQA1*0501 is the most efficient and cost effective manner to detect for genetic predisposition. Fine has found that DQ2 positivity being the Celiac-related HLA-DQB1*0201 allele is overhelmingly more frequent that the 0202, 0203, 0204 or 0205 alleles. By linkage disequilibrium, the HLA-DQA1*0501 will usually accompany the HLA-DQB1*0201. The presence of HLA-DQ2 assessed serologically (i.e. the functional presence of any DQ2 gene product) has always shown itself to produce antibodies to bind to Gliadin, and therefore predispose a person to Gliadin sensitivity (with or without the villous atrophy).
As mentioned, 90% of Celiac sufferers have the DQ2 gene, and so a test such as Enterolab's for one of the heterodimers of the DQ2 gene will only capture 90 out of 100 genetically predisposed Celiac sufferers. However, if the test is taken in conjunction with a stool test for AGAs and ATAs, then a more complete picture can be obtained.
http://www.enterolab.com/StaticPages/Frame_TestToOrder.htm#Genetic_testing
Having the HLA-DQ genes does not definitely mean one has Celiac Disease now, but that Gliadin sensitivity is possible and a risk for the future. Genetic testing is most useful when performed in conjunction with Antibody Testing, in particular Stool Antibody Testing for Anti-Gliadin IgA Antibodies (AGAs) and Anti-tTG IgA Antibodies. HLA-DQ testing can also be useful in patients who have been on a Gluten-free diet for many years, and may not have any measurable IgA or IgG antibodies against Gluten to detect, but who may still be at risk of relapse of symptoms if Gluten is reintroduced - a Gluten challenge in such cases is unreliable.
Please see the Tests page for more information on Enterolab tests.
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Lymphocyte Proliferation Tests (LPT):
These are blood tests that isolate White Blood Cells (Lymphocytes or WBCs) and expose them to quantities of a specific food type in order to observe their behaviour. Such testing is slow and expensive and not the preferred route for most patients when it comes to Food Sensitivity Testing. Such tests include Nutron (involving a Nutron diet), Cytotoxic and ALCAT and FACT tests and are not fully scientifically validated, and may not correlate with other allergy testing methods' results.
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Applied Kinesiological and Muscle Testing
It is theoretically possible to test a variety of food types using Applied Kinesiology or Muscle Testing (or other Bio-Feedback Testing). This form of testing is discussed on the Tests page and Treatment Approach page. It is used successfully for many patients in conjunction with determining the best combination of supplements to use. However, for food types, it may be less practical, to bring food types with you to your appointment. A friend could help test them for you. It may be impractical to use this form of testing for all food types and groups, instead perhaps using it as a back up or for a specific food. The above forms of testing would probably suffice.
Bio-feedback devices are also reputed to detect the presence of allergies in the body, even those which do not yet come up on IgG testing or which one has not yet noticed, e.g. certain foods that one has been eating regularly. Bio-feedback devices are often much quicker than manual kinesiological testing.
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Treatment:
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Elimination Diets:
If one is experiencing either an allergic response, slow immune response or intolerance symtpoms to a given food type, it would be highly sensible to refrain from eating this food type in the short term, to allow the body a chance to recover and function more normally. This is especially important for foods that you experience a rapid, IgE type reaction to.
As discussed above, an Elimination Diet is a useful method of identifying a food sensitivity. One may choose to go different routes from there, and elect to either completely avoid the given food type, to consume it only very occasionally if there is only a moderate non-IgE type reaction to it, or to embark on a programme of controlled reintroduction, after a sufficiently long abstainance period. Your practitioner and/or nutritionist should be able to offer you specific advice on the amounts and frequency of consumption of the problem foods, as too much or too often could result in the return of your adverse symptoms and lower energy levels, or much worse. In general, Elimination Diets with Controlled Reintroduction are considered to be a viable strategy for gradually de-sentisiting the body to foods that the immune system reacts to, either IgE, IgA or IgG. Of course, one does so at one's own risk, and consuming too much of a food one has a potentially life threatening reaction to is not clever and can result in death. It is doubtful that Controlled Reintroduction would do anything for classic Food Intolerance, where a deficiency in Enzymes is the main problem.
There is of course nothing wrong with simply avoiding problematic foods. It doesn't 'solve' the reason for the reaction but can in the short term and long term result in a reduction in symptoms and the effects of food sensitivites and allergies. Adverse symptoms from Celiac Disease tend to resolve more quickly in the short term than general non-IgE-mediated immune reactions to food, but of course the damage to the intestine may take some time to heal. Kenneth Fine has found that Celiac Disease tends to resolve itself in 6 to 12 months once a rigid Gluten-Free Diet has been followed, with the intestinal villi restoring themselves back to their original form again. This process may be accelerated with some of the supplements used for treating Leaky Gut Syndrome. Kenneth Fine in his early research has found that many autoimmune conditions also improve with the elimination of Gliadin from one's diet. The more adversely immune stimulating foods one removes from one's diet, the greater the benefit it is likely to have on one's well being and also any autoimmune diseases present. This may depend on the individual, but common examples, as discussed above, including dietary yeast, some other grains and soy. For arthritic patients the nightshades are often particularly pertinent (e.g. tomatoes, potatoes, egg plant and red hot chilli peppers).
www.enterolab.com/StaticPages/Faq_Result_Interpretation.htm
It may also be applicable to adopt an Anti-Candida Diet and adopting certain anti-microbial treatments whilst treating Food Intolerance, to treat the downstream effects of the Dysbiosis and other harmful overgrowths that may have arisen in the colon on account of the Food Intolerance over time. As discussed in the Gluten section above, there may be some conflict between the two types of diet, so one may have to use one's common sense in balancing and harmonising the two approaches and avoiding grains where only the low fibre, high carbohydrate forms are tolerated. In addition, many 'gluten free' convenience foods being sold are high in sugar and are not really very good for you. Common sense applies, and just because something is 'vegetarian' or 'gluten free' does not make it a healthy food necessarily!
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Supplemental Digestive Support:
As discussed on the Digestive Disorders page, there are a number of available strategies to improving the quality of one's digestion generally, e.g. Peristalsis and General Digestive Enzyme and Stomach Acid Deficiencies. These include but are not limited to:
Digestive support will not likely directly affect the fast and slow immune system responses to problem foods in the short term, although better nutrient absorption and better digestion of proteins and carbohydrates will help the body in general and may serve to calm down the immune system to some extent in the long term.
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Stress Management:
The treatment of food allergies and intolerance reactions involves several components, avoidance or limitation of those food types or ingredients that cause the problems, to support the digestive tract and system, and to try to tame the body's immune system response. One component of this taming of the immune system response is to avoid certain triggers of incorrect and overactive immune system response. Stress or more specifically brain overstimulation or hyperexcitation can be one cause of elevated adverse immune system responses to certain foods. Prolonged periods of stres or intellectual and mental stimulation or computer use over many months may result in less ability to full relax or calm the brain, which may in turn result in more inflammatory type responses in the digestive tract. Excitotoxicity caused by elevated free Glutamate and Aspartate levels may also result or contribute to overstimulation or excitation of the neurons, as discussed above. Stress or overexcitation of the brain is one factor of many possible triggers in activating the immune system and excessive inflammatory response and oxidative stress.
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Chelation Therapy:
The presence of heavy metals in the body may also be implicated in adverse and excessive immune system responses to certain food items or indeed in cases of Multiple Chemical Sensitivies (and other inflammatory illnesses driven by excessive Nitric Oxide/Peroxynitrite formation). The removal of heavy metals from the body by chelation may temporarily elevate the levels of heavy metals circulating in the blood, which may temporarily elevate the degree of sensitivity to problem foods or indeed to harmful electromagnetic fields or other external adverse stimuli. In the long term, mind calming techniques, avoidance of problem foods, heavy metal chelation and/or antioxidant therapy may reduce such symptoms. It seems that many of these stimuli can result in a vicious circle of elevated inflammatory responses. In other words one needs to keep one's focus slightly wider than just food and look at all lines of causation.
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Treatment of Systematic Microbial Infections:
The presence of bacterial, fungal and parasitic infections in the GI tract, and the necessity of their eradication, have been mentioned briefly above. Pathogenic micro-organisms can also be present as systematic infections, i.e. outside of the GI, e.g. in the bloodstream, organs, and even inside the cells (intracellular). Here they can put a constant strain on the immune system and in many cases excrete neurotoxic biotoxins (i.e. neurotoxins) that interfere with nervous system function, and to some degree, our immune system function. Such organisms may be introduced into the bloodstream via the digestive tract (e.g. leaky gut syndrome), via dental infections, or via insect bites (e.g. tick bites).
Examples include Cell Wall Deficient (CWD) bacteria such as mycoplasma, Borrelia species bacteria (the primary cause of Lyme Disease), Lyme Disease co-infections such as Babesia protozoa, Bartonella bacteria species, Chlamydia pneumoniae (Cpn) etc. These infections can be detected by advanced blood smear microscopy, PCR blood tests, and also by muscle testing although these methods are not 100% reliable. Many cases go undiagnosed and this is particularly true for CFS, ME and FMS patients, where one of the main drivers of their condition may actually be a systematic infection.
Treatment is often difficult compared with eliminating undesired microbes in the GI tract, as one has to absorb the agents into the bloodstream and treat the outside as well as the inside of our cells, without causing too much toxicity or free radical damage to the cells themselves. The pathogenic microbes may also hide inside biofilms, which offer a defensive wall against antimicrobial agents.
If one has a significant pathogenic infection such as Lyme Disease, where the bacteria are excreting neurotoxins, attempts to retrain a poisoned and malfunctioning immune system are unlikely to be wholly successful, and more progress may be made in this area once the pathogens and biotoxins have been removed. If you do have Lyme Disease, it is unlikely that any of your allergies will ever get significantly better until you eradicate the infection.
A friend of mine, Paul, noted that once he eradicated the Cryptostrongylus pulmoni (roundworm) using Ivermectin (an anhelmintic drug), his hayfever disappeared completely along with most of his other allergies, and he postulates that the presence of such pathogens, particularly roundworm, are probably behind nearly all allergies.
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Antioxidant Therapy:
A vicious cycle of free radical and oxidant production may occur in the body, that spirals out of control and inflames the brainstem, causing an abnormal immune response as well as excessive excitotoxicity in the nervous system and an increase in free radical damage and inflammation in the body. This is known as the Nitric Oxide/Peroxynitrite cycle. There are many possible causes, stress and overexcitation are discussed above. The presence of heavy metals is another possible factor, discussed above also. The main treatment for elevated Nitric Oxide/Peroxynitrite is antioxidant therapy and mitochondrial support. When we say antioxidant therapy, we are interested mainly in those antioxidants that are targetted at scavenging Nitric Oxide and Peroxynitrite derivatives. This can be a combination of antioxidant rich (high ORAC value) foods as well as antioxidant supplementation; and in large quantities! With as much antioxidant diversity as possible. This is discussed on the Nitric Oxide and Peroxynitrite page. It would seem sensible to combine one's Gluten/Dairy Free Diet (or other variant of an elimination/avoidance diet) and the Anti-Candida Diet with a diet rich in antioxidants (and perhaps noting which foods are nurturing and which foods to avoid from an Oriental Medicine perspective).
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