biology homework

The Great Grain Conundrum by

Mark J Donohue

We’ve all heard it before – eat plenty of whole grains to stay healthy. “They” say the consumption of

whole grains is needed to keep your heart healthy and to prevent colon cancer. That whole grains are

chalk full of B-vitamins and fiber. That whole grains are complex carbohydrates (rather than refined or

simple) which are digested slowly so as not to cause a spike in blood sugar.

And if that wasn’t enough, whole grains are the foundation to the USDA’s food pyramid. Not to mention

the fact that wheat is referred to as the “staff of life” because for thousands of years the consumption of

wheat has been found in virtually every society on the planet.

The Conundrum

Despite what you’ve heard or

what the USDA’s food pyramid

indicates… scientific findings are

finding the “staff of life” (wheat

and other grains) are now

becoming too be known as the

staff of illness and the staff of pre-

mature death… not life.

This shift is occurring due to a

number of compounds – proteins

- found in grains and their adverse

or toxic effects they have on the

human body. Therefore, one

might expect these compounds to

be referred to as toxins. But this

has an alarmist sounding connotation, Figure: New revamped USDA Food Pyramid 2005

therefore these compounds are

instead referred as antinutrients. Some of the antinutrients found in grains and their biologically

negative antinutrient effects are:

Phytic Acid Wheat Germ Agglutinin (WGA)

Goitrogens Opioid Peptides

Gluten Amylopectin - A

Zonulins, Leaky Gut & Leaky Brain Advanced Glycation End-Products (AGEs)

Phytic Acid (Phytate)

Phytic acid is the storage form of phosphorus found in many plants, especially in the bran or hull of

grains, beans, nuts and seeds. Humans are unable to digest phytic acid so the phosphorus is essentially

trapped in the compound making it unavailable to the body. The antinutrient effects of phytic acid takes

place once it arrives in the intestines where phytic acid can:

 Inhibit mineral absorption (chelating agent) of iron, zinc, calcium & magnesium thereby causing

mineral deficiencies. Phytic acid also chelates the vitamin – niacin (B3).

 Interfere with enzymes needed to digest food. Enzymes such as pepsin needed to digest proteins

and amylase needed to digest carbohydrates. Phytic acid also inhibits the enzyme trypsin, which is

needed for protein digestion in the small intestines.

Phytase is the enzyme that neutralizes phytic acid and liberates phosphorus. Humans do not produce

enough phytase to safely consume large amounts of phytate foods. However, humans are able to

tolerate a small amount of phytic acid – in the range of 100 – 400 mg per day. Also, probiotic lactobacilli

and other healthy digestive microflora can produce phytase. Meaning, humans who have good intestinal

flora will have an easier time with these foods.

Luckily, phytase also co-exist in plant foods that contain phytic acid and can be partially freed-up by

soaking, sprouting, and fermenting these foods. Cooking can also reduce the amount of phytic acid to

some degree.

 Living With Phytic Acid, by Ramiel Nagel, The Weston Price Foundation (more in-depth article) Link

 Fermented Foods & Digestion: How to Avoid Phytic Acid, YouTube (1:47) Link

Goitrogens

Goitrogens are compounds found in foods that can suppress thyroid activity by interfering with iodine

uptake. Long term exposure/consumption can lead to an enlargement of the thyroid gland called a

goiter. The goitrogens contained in most foods, such as cruciferous vegetables, can be reduced by

cooking. However, with the grain millet, which has strong goitrogenic effects, cooking actually increases

the goitrogenic effect.

Also, though wheat, rye and barley do not contain goitrogens, they do contain high levels of gluten

(discussed below). Gluten has been show to be implicated in several autoimmune diseases. One of these

autoimmune diseases is called Hashimoto’s thyroiditis, where the immune system attacks the thyroid

gland.

Gluten: Gliadin & Glutenin

Gluten is a protein found in wheat which gives elasticity to dough and a chewy texture to baked goods.

Gluten is actually a composite of two storage proteins - prolamin and glutelin. Prolamins are so named

due to their high content of the amino acids proline and glutamine, while glutelin acts as glue (elasticity)

holding prolamins together.

There are several types of prolamins and glutelins found in grains, meaning there are several types of

gluten which varies from grain to grain. However, by definition “technically” gluten is a term applied

specifically to the prolamin-glutelin combination found in WHEAT. The type of prolamin found in

wheat is called – gliadin - which has been implicated as the main environmental factor in causing Celiac

disease. The glutelin found in wheat is called – glutenin – and is the leading cause of wheat allergy.

Gluten Spectrum Disorders

 What is Gluten, Dr. Alesio Fasano, YouTube, Nice Overview (2:42) Link

1. Wheat Allergy – 10% of food allergy. An immune reaction which can be to gluten, but more often

occurs in response to other wheat proteins (i.e. globulins, albumins, glutenins, etc.). This immune

reaction is mediated by the IgE class of antibodies.

The problem is that most food allergies (including wheat) are not IgE mediated, but rather are IgG

reactions, which usually show up hours or even days after ingestion of the allergen. They are

generally not nearly as dramatic as the more severe IgE reactions, and usually result in constipation,

diarrhea, bloating, water retention, fatigue, etc.

However, when left unrecognized and untreated food (wheat) allergies can lead to chronic and

debilitating disease.

2. Celiac Disease – also known as Celiac Sprue or gluten-sensitive enteropathy, is an immune mediated

disease that affects about 1% of the U.S. population (2-3 million) or 1 in 133 people. This immune

reaction occurs in individuals after consumption of one of the gluten grains (generally recognized -

wheat, rye, barley) and only in those individuals who are genetically susceptible. Celiac disease

damages the lining (villi) of the upper (duodenum) and middle (jejunum) portion of the small

intestines. Rarely does it affect the lower portion of the small intestines (ileum).

Celiac disease classifications:

A. “Classic” Celiac disease: where intestinal symptoms are dominate, i.e.

diarrhea/constipation, belly distention, weight loss, loss of appetite/voracious appetite,

vomiting, mouth ulcers, etc.

B. Atypical Celiac disease: characterized by symptoms outside the intestinal tract, i.e. fatigue,

anemia, irritable, depressed, neurological findings, muscle/join pain, skin rashes, etc.

C. Silent Celiac disease: no apparent intestinal symptoms or atypical symptoms.

Left undiagnosed and untreated, celiac disease can lead to the development of other autoimmune

disorders, as well as osteoporosis, infertility, neurological conditions and cancer.

“Unfortunately, there is an increased mortality rate for people with Celiac disease,

exceeding that of the general population, due mainly to malignancies. Current research

shows a statistical risk that is 33 times greater for small intestinal adenocarcinoma, 11.6

times greater for esophageal cancer, 9.1 times greater for non-Hodgkin’s lymphoma, 5

times greater for melanoma, and 23 times greater for papillary thyroid cancer.” (Green

2010)

3. Gluten Intolerance/Sensitivity (not a disease) – Do not have celiac disease or wheat allergy, but do

develop symptoms after ingesting gluten. This is a diagnosis of exclusion – after celiac disease and

allergy to gluten have been excluded. Symptoms are similar to that of Celiac disease – abdominal

pain, fatigue, headaches, “foggy mind”, tingling in extremities, schizophrenia, autism, etc..

The Center for Celiac Research estimates that approximately six percent of the U.S. population, or

18 million people suffer from gluten sensitivity. This group reacts with some of the same symptoms

as people with celiac disease, but gluten-sensitive individuals typically test negative for celiac

disease in diagnostic blood tests and show no signs of the damage to the small intestine that defines

celiac disease. Point being, if you have Celiac disease you are gluten intolerance. But it is possible to

be gluten intolerant and not have Celiac disease. The causes of gluten intolerance are not known,

and this condition has not been well-studied scientifically.

Gluten Grains

Normally when we digest protein, it gets broken down in the stomach and small intestine into single

amino acids or dipeptides (two amino acid molecules) that are readily absorbed by the small intestine.

But the gluten molecule is resistant to the enzymes that break down proteins – peptidases. It is simply

not digested well by humans. As a result, we are left with a long peptide chain, composed of 33 amino

acids, that is the toxic gliadin fraction.

It has been well established, meaning there is no controversy that wheat, rye and barley are the “gluten

grains”. And that these grains are responsible for the development of wheat allergies, Celiac disease and

gluten intolerance and the long list of symptoms associated with these disorders.

“Modern wheat is the altered offspring of thousands of genetic manipulations, crude

and sometimes bizarre techniques that pre-date the age of genetic modification. The

result: a high-yield, 2-foot tall "semi-dwarf" plant that no more resembles the wheat

consumed by our ancestors than a chimpanzee (shares 99% of the same genes that

we do) resembles a human. I trust you can tell the difference that 1% makes…

… The obvious outward differences are accompanied by biochemical differences.

The gluten proteins in modern wheat, for instance, differ from the gluten proteins

found in wheat as recently as 1960. This likely explains why the incidence of celiac

disease has quadrupled in the past 40 years. Furthermore, a whole range of

inflammatory diseases, from rheumatoid arthritis to inflammatory bowel disease,

are also on the rise. Humans haven't changed -- but the wheat we consume has

changed considerably.” (Davis 2010)

The grain with the most controversy is oats. Whether oats is a gluten grain or not depends on who you

ask or what medical study one might be looking at. Over the years some have said oats do contain

gluten while others have claimed otherwise. Currently oats are claimed to be safe as long as they have

not been contaminated with wheat gluten during processing and are certified as gluten free. While at

the same time “they” seem to contradict themselves by also claiming that:

“there are very small amounts of the amino acid sequences (of gluten) in oats and

that if consumed in large quantities can cause celiac disease in a very small number

of people.”(Kagnoff 2008)

To complicate things even further the gliadin in wheat gluten may be further subdivided into 4 sub-

fractions. The gliadin proteins are divided into alpha, beta, gamma and omega gliadins. With the alpha,

beta, and gamma gliadins being toxic to a person with Celiac disease and gluten sensitivity, while omega

gliadins appear to be safe.

 Celiac Disease & Gluten Sensitivity with Dr. Tom O’Bryan, Interviewed by Underground Wellness,

YouTube – Very Informative (25:04) Link

“A milligram of gluten a day keeps the villi healing away”

 Gluten Sensitivity and Celiac Disease – Webinar with Dr. Tom O’Bryan, Hawthorn University

YouTube Channel - Very Informative (1:10:54) Link

“You can’t have a little gluten… you can’t be a little pregnant… but we all forget

about memory B cells… and the method by which our immune system is activated to

protect us in vaccinations is by producing memory B cells to measles, mumps and

rubella… so that if you’re ever exposed to measles again there’s a memory B cells

that says this is not a good thing I better fight this and it activates the immune

system to make antibodies to measles, mumps, rubella or whatever the

immunization was for… that’s gluten… that if you have gluten sensitive enteropathy

celiac disease you’ve got memory B cells… so you can’t have a little.”

“Gluten sensitivity - if it manifest in the intestines it will be celiac disease… and we

know from many studies… there are over eighteen thousand studies showing celiac

disease can manifest in other autoimmune diseases – dermatological, cognitive,

hepatic, cardiac, neurological, endocrine, musculoskeletal… I don’t know a system in

the body that may not be affected by celiac disease. There is another mechanism

that may occur and that is that gluten sensitivity can trigger these autoimmune

diseases without going through the mechanism of celiac disease.”

 Celiac Disease is NOT the same thing as Gluten Sensitivity, by Dr. David Clark, YouTube (5:25) Link

“Celiac disease is one kind of gluten sensitivity… it’s not the only kind of gluten

sensitivity”

 Rubio-Tapia A., Murray J.A., Celiac Disease, Current Opinion in Gastroenterology, Mar;26(2):116-22

Current Overview of Celiac disease (2010) Link

“In the last year, work has shown that the prevalence of CD has increased

dramatically, not simply due to increased detection. Also, undiagnosed CD may be

associated with increased mortality.”

 Chirodo F.G., Presence of High Levels of Non-Degraded Gliadin in Breast Milk from Healthy

Mothers, Scandinavian Journal of Gastroenterology, 33(11):1186-1192 (1998) Link

“Breast feeding plays a key role in the development of the immune system…

… In conclusion, non-degraded gliadins were detected in milk and colostrum

samples from healthy mothers in a normal diet. Great variability was observed in

the gliadin concentration, with levels surprisingly high in many samples. Gliadin

levels were higher than those reported for other dietary antigens. High levels of

gliadin/anti-gliadin IgA immune complexes were also detected.”

Zonulins, Leaky Gut & Leaky Brain

Gluten intolerance or Celiac disease can manifest anywhere in the body and therefore can present its

self as anyone of a list of numerous symptoms. Bottom line - gluten intolerance and Celiac disease are

systemic conditions. This occurs primarily because gluten’s inflammatory effect in the gut causes

intestinal cells to die prematurely and causes oxidation on those cells. This effect creates a leaky gut

(intestinal permeability); a leaky gut can allow bacterial proteins and other toxic compounds to enter in

to the blood stream and general circulation.

For example – if gliadin enters the blood stream the immune system will mount an attack against this

invading protein. This is fine and good except gliadin can be similar in structure to other proteins found

in tissues of such organs as the thyroid or the pancreas. This in turn means that the antibodies produced

by the immune system to attack gliadin will now see thyroid and pancreas tissue as invaders. Once these

tissues are attacked it creates autoimmune condition/disease like hypothyroidism and type 1 diabetes.

Antibodies against gluten have also been shown to attack heart tissues and cause heart disease.

“While trying to develop a cholera vaccine, they had found a protein they called

zonulin. It is a protein that disrupts the protective tight junctions in the small

intestine and the blood brain barrier and is excessively produced, by some

individuals, in response to ingesting wheat and other grains with analogous

proteins, rye and barley”. (Hoggan 2010)

Also once in general circulation gluten/gliadin is a strong hormone disrupter. And if all that isn’t enough

gluten has been strongly associated with cancer – it is potentially cancer causing.

 Dr. Rodney Ford – Who Needs a Gluten Test?, YouTube, More Gluten Symptoms (5:30) Link

 Fastest Way to Cure Leaky Gut Syndrome, Dr. Peter Osborne – Very Informative (45:53) Link

“… gluten causes the up regulation of the protein zonulin and zonulin causes the gut

cells to spread apart… so gluten in and of itself directly can cause a leaky gut… so

that’s one of the components of the gluten intolerance aspects… it’s not an immune

reaction, it’s a gut dismantling which then leads to subsequent immune reaction”

 Gluten Free Diet Mistake #1, by Dr. David Clark, YouTube (4:40) Link

“When you develop a gluten sensitivity almost a hundred percent of the time you

start to develop something called leaky gut… or increased intestinal permeability

which is a huge source of inflammation… G.I. symptoms are the least common

presentation of gluten sensitivity”

The Other Grains

While prolamin and glutelin are the proteins most likely to have a negative effect on the human body,

they are far from the only potentially problematic compounds. As mentioned there are several types of

prolamins and glutelins found in grains, some of which have a structure similar to that of wheat, namely

one part prolamin, one part glutelin. Because of the similarity in protein structure (amino acid

composition) they also can have the same detrimental health effects. Therefore, these grains – namely

barley and rye are also commonly referred to as “gluten grains”.

Chart: prolamine & glutelin content for some grains and its related protein content (percentage).

As for the prolamins and glutelins found in other grains like maize (corn), rice, millet, sorghum and teft;

they are poorly researched and their effect on the body is not well understood. Because of this lack of

research the term gluten is simply not applied to these grains and therefore are deemed safe for

consumption for those with Celiac disease and gluten sensitivity/intolerance. Unfortunately, whether

these grains are truly safe is currently being debated thus causing confusion and “possible” delayed

healing for those with gluten sensitivities.

“… gluten research is far from complete and there is a lot more that we do not know

about the scope of gluten proteins and the damage they can stimulate…

… Because all grains contain gluten (in different forms), and only a fraction of these

glutens have been studied, it is foolish to assume that traditional gluten free

substitutes are safe for consumption for the gluten sensitive individual.” (Osborne

2010)

 Helms, S., Celiac Disease and Gluten-Associated Diseases, Alternative Medicine Review, 10(3):172-

192 (2005) Good Overview Link

“Specific gluten-containing foods are the primary immune system instigators in

Celiac disease (CD) and gluten-associated diseases (GAD). These include the glutens

GRAIN PROLAMIN (% of Protein) GLUTELIN (% of Protein)

Wheat Gliadin (33 - 45% Glutenin (40 – 46%)

Barley Hordein (25 – 52%) Glutelin (52 – 55%)

Rye Secalin (21 - 42%) Glutelin (25 – 40%)

Oats Avenin (12 - 14%) (23 – 54%)

Maize(corn) Zein (47 - 55%) (38 – 45%)

Rice Orzenin (2 - 7%) (78%)

Millet Panicin (40%)

Sorghum Kafirin (48%) (37%)

Teft Penniseiten (11%)

present in all forms of wheat, including durum, semolina, spelt, kamut, malt,

couscous, bulgar, triticale, einkorn, and faro, as well as in related grains – rye and

barley…

… Gliadins seem to generate the strongest immune response in susceptible

individuals and therefore, have comprised the majority of current research.

Although rice, buckwheat, corn, oat, and other grains contain glutens, they are not

specific to CD/GAD etiology, but rather, may contribute to escalating

symptomatology in sensitive individuals by creating and sustaining an inflammatory

response.”

 Thompson T., Questionable Foods and the Gluten-Free Diet: Survey of Current Recommendation,

Journal of the American Dietetic Association, 100(4):463-465, April 2000 Link

(Survey chart shows why patients are so confused and why their health may not be improving)

Figure: The Gramineae/Grass Family Click to view larger image

 Gluten Sensitivity, by Dr. Peter Osborne, Glutenology YouTube Channel – Very Informative (37:07)

Link

“Grains are the seeds of grass. The seed has a bran casing, a starchy endosperm

which contains 90% of the protein and a small germ nucleus which is the plant

embryo, waiting to grow. Any flour made from the starchy endosperm contains

prolamins and is potentially toxic to the grain sensitive /intolerant person…

… in a nutshell, gluten is a protein found in all grains… there are grains like rice,

millet and sorghum that are classically considered gluten free based on that original

observation from more than 60 years ago and the problem with it is that nobody has

gone back to study these other grains…

… we have studied corn about a dozen times and every time we study corn gluten…

we find that corn gluten causes damage to people with gluten sensitivity…

… we have a couple of small studies on rice that shows that rice causes inflammation

of the colon…

… Gluten Sensitivity can cause over 200 conditions… only one of them is Celiac

disease…

… Gluten Sensitivity - in actuality symptoms can be and usually are systemic”

 Gluten Free Paleo Diet Discussed on Fox News Interview with Dr. Peter Osborne,

Glutenology YouTube Channel – Very Informative ( 5:56) Link

 Cabrera-Chavez F., et al, Maize Prolamins Resistant to Peptic-tryptic Digestion Maintain Immune-

recognition by IgA from some Celiac Disease Patients, Plant Foods for Human Nutrition, 67(1):24-30

(2012) Link

“Maize is used as an alternative to wheat to elaborate foodstuffs for celiac patients

in a gluten-free diet. However, some maize prolamins (zeins) contain amino acid

sequences that resemble the wheat gluten immunodominant peptides and their

integrity after gastrointestinal proteolysis is unknown…

… Results concur to indicate that relative abundance of these zeins, along with

factors affecting their resistance to proteolysis, may be of paramount clinical

relevance, and the use of maize in the formulation and preparation of gluten-free

foods must be reevaluated in some cases of celiac disease.”

 Kristjansson G., et al, Gut Mucosal Granulocyte Activation Precedes Nitric Oxide Production:

Studies in Coeliac Patients Challenged with Gluten and Corn, GUT, June;54(6):769-774 (2005) Link

“In all coeliac patients rectal nitric oxide (NO) concentration increased after gluten

challenge and reached a peak after 15 hours (mean 9464 ppb). Six of ten patients

showed an increase in NO production 15 hours after rectal corn gluten challenge but

this was much smaller than after gluten challenge (mean 368 ppb). No increases

were seen in the control group after either challenge…

… The observation that corn gluten challenge induced an abnormal NO reaction in

some of our patients with CD is intriguing as maize is considered safe and is

recommended as the substitute cereal in a gluten free diet.”

 Davidson I.W., et al, Antibodies to Maize in Patients with Crohn’s Disease, Ulcerative Colitis and

Coeliac Disease, Clinical and Experimental Immunology, Jan;35(1):147-8 (1979) Link

“The incidence of antibodies to maize using an immunofluroescent technique has

been found to be 14% in controls, 33% in Crohn’s disease, 50% in Ulcerative Colitis

and 44% in Coeliac disease.”

 Troncone R., et al, An Analysis of Cereals That React with Serum Antibodies in Patients with

Coeliac Disease, Journal of Pediatric Gastroenterology and Nutrition, 6(3):346-350 (1987) Link

“When the coeliac sera were tested for antibodies against the prolamins of other

cereals, they exhibited titers to oats (49.8), barley (45.9), and maize (44.7) similar

to those measured against wheat gliadins. Significantly lower levels could be

demonstrated against rice (20.3)…

… nevertheless, untreated coeliac patients show significantly higher titers against

wheat gliadin as well as against other wheat proteins and other cereal prolamins,

even those considered harmless for coeliac patients. “

Cross-Reactions

Cross-reactivity, which is the tendency to react to substances either genetically or structurally similar to

gluten or that our immune system has merely learned to associate with gluten, is an added concern.

Once multiple food sensitivities take over, they can cause a very vicious cycle that only worsens with

time and becomes extremely difficult to correct.

Some of the most common “potentially” cross-reactive compounds are:

Casein Kamut

Oats (including “gluten free”) Yeast

Rye Coffee

Barley Chocolate

Spelt

Though not as common other compounds that have been shown to cross-react with gluten are:

Corn Millet

Sesame Tapioca

Buckwheat Amaranth

Quinoa Rice

Sorghum Potato

 The Danger of Milk Products and Gluten Sensitivity, by Dr. David Clark, YouTube (5:19) Link

 The Danger of Yeast and Gluten Sensitivity, by Dr. David Clark, YouTube (5:08) Link

 The Danger of Coffee & Gluten Sensitivity, by Dr. David Clark, YouTube (5:02) Link

Nutritional Deficiencies

The primary target for gluten is the small intestine. Damage to the intestine not only causes leaky gut

but also causes poor absorption of nutrients. This occurs because the villi become inflamed and

eventually atrophy, thus making it impossible for the proper absorption of nutrients. This in turn causes

nutritional deficiencies manifesting as a long list of medical symptoms. The most common nutritional

deficiencies in gluten intolerance and Celiac disease are:

 Iron

 Folate

 Vitamin B12

Testing

About 35-40% of the population may experience gluten sensitivity/intolerance. However, the crux of

the issue - many of us simply don’t know whether we fall into the 60-65% of the population that can

tolerate gluten or into the 35-40% of the population that can’t. So it’s important that we find out

through antibody testing.

Antibodies are proteins that are produced by the immune system to fight viruses, bacteria, and other

organisms that infect the body. Sometimes, however, the body produces antibodies against non-

infectious substances in the environment (for example, in hay fever) and even against its own tissues

(autoimmunity). Researchers have discovered that people with celiac disease who eat gluten have

higher than normal levels of certain antibodies in their blood.

Before being tested for gluten antibodies you must first be currently on a gluten containing diet for the

tests to be accurate. The immune response that your body produces is its response to being exposed to

gluten in the diet and its subsequent effect on the intestinal mucosa. If there is no gluten in the diet,

then there is no response that can be measure.

A brief change in diet will not have a noticeable effect. If you have been gluten free for a week or so, it

will not make any great difference. The response might be marginally less but the difference is

insignificant because the body has not had time to respond to the change. Conversely, if you have been

gluten free for a protracted period of time and decide to be tested, a brief challenge of a couple of

weeks is not enough to elicit a response and get an accurate test.

Definitions

 Specificity – if a test is 100% specific, it means there is nothing else – no other medical condition

that can cause the positive result.

 Sensitivity – if a test is 100% sensitive, it means that everyone with the disease has a positive

test.

Anti-Endomysial Antibodies (AEA) or Endomysial Antibodies (EMA) - IgA

IgA class anti-endomysial antibodies are very specific, occurring only in celiac disease. These antibodies

are found in approximately 100% of patients with active celiac disease. IgA endomysial antibodies are

more sensitive and specific than gliadin antibodies for diagnosis of celiac disease.

“One study evaluating endomysial antibodies showed that the sensitivity of this

marker was 100% in patients with total villous atrophy, but the value plummeted to

31% in patients with CD who had partial villous atrophy”

This is not an automated test and is therefore subject to interpretation by the lab tech.

Anti-Tissue Transglutaminase Antibodies (tTG) – IgA & IgG

Recently, (1998) the endomysial antigen targeted by the anti-endomysial antibodies was identified as

the protein cross-linking enzyme known as tissue transglutaminase (tTG). tTG is the enzyme that

converts gliadin into a more toxic molecule. This has enabled the production of an antigen specific ELISA

assay (automated) incorporating tTG as a reliable and objective alternative to the traditional and

subjective Immunofluorescence based assays.

This is a test that has been very well received in the professional community. It is an ELISA, like the anti-

gliadin antibody test and, as such, is not subject to interpretation like the IFA. If the tissue

transglutaminase antibody test is positive, then a diagnosis of Celiac disease can be made and a biopsy

will not provide any new information on how to treat the patient.

In summary, the tTG ELISA is measuring the same thing that the endomysial IFA is measuring but with a

method that is more sensitive and specific and not subject to interpretation.

Anti-Gliadin Antibodies – IgA & IgG

Anti-gliadin antibodies are less reliable and have a high false positive rate. Thus a person with an

abnormally elevated anti-gliadin antibody level does not necessarily have celiac disease. Nevertheless,

anti-gliadin antibody levels are useful in monitoring the response to treatment because anti-gliadin

antibody levels usually begin to fall within several months of successful treatment of celiac disease with

a gluten free diet.

Both IgA and IgG anti-gliadin antibodies (AGA) are detected in sera of patients with Celiac disease. IgG

anti-gliadin antibodies are more sensitive but are less specific markers for disease compared with IgA

class antibodies. IgA anti-gliadin antibodies are less sensitive but are more specific.

IgA positive - a positive result is a strong indication that the patient has the disease but a negative result

does not necessarily mean that they do not have it. False positive results are rather uncommon but false

negative results can occur.

IgG positive - means that they will show positive results more readily but there is not as strong a

correlation with celiac disease. It is less specific. Patients with other conditions but not afflicted with

celiac disease will occasionally show positive results.

A sensitive testing protocol includes testing for both IgA and IgG anti-gliadin antibodies since a

significant portion of celiac patients (approx. 2-5%) are IgA deficient. This combined IgA and IgG anti-

gliadin antibody assay has an overall sensitivity of 95% with a specificity of 90%. The type of test used to

detect the anti-gliadin antibodies is called an ELISA.

Deaminated gliadin peptides (DGP)

Patients with Celiac disease create antibodies to gliadin, but these antibodies can also be found in other

conditions and in normal people. It is known that tTG deaminates… meaning it acts on and enhances the

gliadin peptide in patients with Celiac disease.

Deamidated gliadin peptide (DGP) antibodies tests developed in 2007 looks specifically for these

antibodies and in combination with Tissue transglutaminase (TTG) antibodies - have better accuracy

than native gliadin antibodies

Total IgA antibodies

Celiac disease patients are 10 -15 times more likely to exhibit IgA deficiency. If a patient is IgA deficient

the EMA and tTA test will come back negative, regardless as to whether you have CD or not.

IgA deficiency occurs in 1 in 700 individuals in the general public and occurs in 1 in 50 individuals with

CD. Therefore, individuals with IgA deficiency need to be tested for IgG antibodies.

Genetic Testing

The most established genetic test is specific to celiac disease and not necessarily for a wheat allergy,

non-celiac gluten sensitivity or a broader gluten intolerance. But it can help either verify the presence of

celiac disease or identify people who may be predisposed to developing celiac disease.

The test looks for the HLA-DQ2 and HLA-DQ8 genes. If one or both genes are present, the individual is at

far greater risk of developing celiac disease at some point in his or her life. Most Celiac patients (more

than 90%) carry the DQ2 gene. Fewer than 10% carry the DQ8 gene.

Approximately 30% of the population have these genes.

Bottom Line

After being altered by the enzyme tTG, gliadin is able to bind more effectively with proteins in the

immune system that recognize and protect the body from foreign substances. In some genetically

predisposed individuals (with HLA-DQ2 & 8 gene), this activates an immune response that begins to

destroy the cells in the vicinity. The immune cells inappropriately recognize and end up destroying what

they were designed to protect – autoimmunity

 Celiac Sprue Association - Sensitivity/Specificity Chart - Link

 Lab Test On Line – Test Result Chart Link

 Anderson R.P., Coeliac disease: Current Approach and Future Prospects, Internal Medicine Journal,

2008 Oct; 38(10):790-9 Current Discussion on Testing Link

 Dr. Snyder – Testing for Celiac Disease, YouTube (6:42) Link

 Dr. Osborn – Lab Test for Gluten Sensitivity, YouTube (3:12) Link

 Dr. Guandalini – Celiac Testing, YouTube (2:01) Link

 LAB: EnteroLab - Link

 LAB: Cyrex Laboratories - Link

NOTE: just because you test negative for celiac disease does not mean with certainty that you still do

not have some form of gluten intolerance.

Wheat Germ Agglutinin (WGA)

Wheat Germ Agglutinin (WGA) is a lectin found in the germ of wheat. Lectin (a protein) is a defense

mechanism for the wheat plant, designed to ward off its natural enemies such as fungi and insects.

Lectins are a powerful way for organisms in nature to attach themselves to other organisms in nature.

Unfortunately, this protein is also very resistant to breakdown by living systems (humans), and it easily

accumulates in tissues where it interferes with normal biological processes and acts as an anti-nutrient.

“Lots of germs, and even our own immune systems, use this super glue to their

benefit. For example, cells in our liver’s bile ducts have lectins on their surfaces to

help them snatch up bacteria and parasites. Bacteria and other microbes have

lectins on their surfaces as well, which work rather like suction cups, so that they

can attach to the slipper mucosal linings of the body. “ (D’Adamo 1998)

Typically, sprouting, fermenting or digestion can help to negate some of the harmful effects of such anti-

nutrients. However, WGAs are resistant to these types of processes. For this reason, WGAs exist even in

“healthy” sprouted breads and may be in their highest concentrations in whole-wheat varieties. WGA

lectin is an exceptionally tough compound as it is formed by the same disulfide bonds that make

vulcanized rubber and human hair so strong, flexible and durable.

What is unique about WGA lectin - it can do direct damage to the majority of tissues in the body without

requiring a specific set of genetic susceptibilities or immune-mediated reactions. This may explain why

chronic inflammatory and degenerative conditions are endemic to wheat-consuming populations.

WGAs do their damage by binding/attaching to N-Acetyl-glucosamine and N-Acetyl-neuraminic

acid/Sialic Acid within the body. All animals (humans) use N-Acetyl-glucosamine as a foundational

substance for building the various tissues in the body. For example – the production of cartilage,

tendons, and joints depend on the structural integrity of N-acetyl-glucosamine. Epithelial cells, which

line the body’s mucous membranes, secrets the protective compound called glycocalyx which is

composed largely of N-acetyl-glucosamine and sialic acid.

Each grain of wheat contains about 1 microgram of WGA. That seems hardly enough to do any harm.

Lectins, however, are notoriously dangerous even in minute doses and can be fatal when inhaled or

injected directly into the bloodstream. According to the U.S. Centers for Disease Control it takes only

500 micrograms (about half a grain of sand) of ricin (a lectin extracted from castor bean casings) to kill a

human. A single, one ounce slice of wheat bread contains approximately 500 micrograms of WGA, which

if it were refined to its pure form and injected directly into the blood, could prove deadly.

The Problem with WGA Lectins

The digestive system can absorb molecules up to 1,000 kilo daltons in size. WGA lectins are very small at

36 kilo daltons and therefore have no trouble entering into the circulation and doing damage.

 These Five Foods May Cause Problems VERY Similar to Wheat, by Dr. Joseph Mercola, Mercola.com

Very Informative Article Link

 3 Ounces of This a Day May Be Harming Your Brain, by Dr. Joseph Mercola, Mercola.com

Very Informative Article Link

 Wheat Germ Agglutinin – The Dark Side of Wheat, Interview with Sayer Ji, Glutenology YouTube

Channel (32:53) Very Informative Interview Link

 Lectins with Dr. Peter D’Adamo, YouTube (8:37) Link

 DATAPUNK: Lectin Classifications, Totally Cool Interactive Lectin Taxonomy Chart Link

WGA Lectin Publications

Below are a couple of publications indicating WGAs effects in humans. More WGA publications can be

found at – GreenMedInfo.Com: WGA

 Dalla Pellegrina C., et al, Effects of Wheat Germ Agglutinin on Human Gastrointestinal Epithelium

Insights from an Experimental Model of Immune/Epithelial Cell Interaction, Toxicology and Applied

Pharmacology, 2009 June 1; 237(2):146-153 Link

“We observed that WGA… can increase individual cell permeability… it alters the

integrity and permeability of the epithelium layer allowing small molecules to cross

the epithelial barrier.”

 Jonsson T., et al, Agrarian Diet and Diseases of Affluence – Do Evolutionary Novel Dietary Lectins

Cause Leptin Resistance?, BMC Endocrine Disorders, 2005 Dec.; 5(10) Link

“Leptin acts as a signal to the brain to inhibit food intake and enable the storage in

adipocytes of surplus calories while simultaneously protecting peripheral non-

adipose tissue from toxic effects of intracellular lipid overload. Leptin also affects

the growth of blood vessels and bone; the immune system; glucose- and fat

metabolism and the reproductive system…

“Lectins are proteins abundant in the virus, bacteria, animal and plant kingdom,

which bind reversibly to specific sugar structures. Different classes of plants, such as

mono- and dicotyledonous, have different classes of lectins with differing

biochemical properties, and there is a subclass of lectins only found in grasses like

cereals. Many plant lectins are thought to play a role in the plants defense against

being eaten. Accordingly, plant lectins have an obvious preference for binding to

sugar structures of animal, fungal or microbial origin, and are usually at highest

concentrations in plant parts essential for reproductive success such as seed germs.

The intensively studied lectin wheat germ agglutinin (WGA), which protects against

insects and fungi is present in wheat seed in both the germ and the gluten part of

endosperm.”

“Cereal lectins are specific to cereals, they are present in our food, they enter our

systemic circulation and have many reported effects in our body including the

binding to receptors, such as the insulin receptor, the epidermal growth factor

receptor and the interleukin 2 receptor. Cereal lectins could thus cause leptin

resistance either indirectly, through effects on metabolism central to the proper

functions of the leptin system, and/or directly, through binding to human leptin or

leptin receptor, thereby affecting the function. The intriguing possibility of direct

interaction between lectin and the leptin receptor could alter the function of the

leptin receptor and translate into diseases of affluence.”

 Freed D., Do Dietary Lectins Cause Disease?, British Medical Journal, 1999 April 17; 318(7190):

1023-24 Link

“Lectins are carbohydrate binding proteins present in most plants, especially seeds

and tubers like cereals, potatoes, and beans. Until recently their main use was as

histology and blood transfusion reagents, but in the past two decades we have

realized that many lectins are (a) toxic, inflammatory, or both; (b) resistant to

cooking and digestive enzymes; and (c) present in much of our food. It is thus no

surprise that they sometimes cause “food poisoning.” But the really disturbing

finding came with the discovery in 1989 that some food lectins get past the gut wall

and deposit themselves in distant organs…

… Wheat gliadin, which causes coeliac disease, contains a lectin like substance that

binds to human intestinal mucosa, and this has been debated as the “coeliac disease

toxin” … On the other hand, wheat lectin also binds to glomerular capillary walls,

mesangial cells, and tubules of human kidney and (in rodents) binds IgA and

induces IgA mesangial deposits. This suggests that in humans IgA nephropathy

might be caused or aggravated by wheat lectin”

 Pusztai A., et al, Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamne-

specific lectins, The British Journal of Nutrition, 1993 July; 70(1):313-21 Link

“Recently it has been shown that the agglutinin from the wheat germ (WGA) has

high anti-insect activity in vitro and therefore, the transfer of its gene into crop

plants has been suggested to increase their insect-resistance. However, previous

limited studies have already shown that WGA causes some damage to the small

intestine of rats, indicating that its nutritional and gastroenterological properties

will have to be thoroughly tested in single-stomached animals before its use as a

natural insecticide could be considered safe….

“… The inclusion of WGA lectins in the diet significantly depressed the growth of

rats…

… The thymus atrophy observed in rats fed with diets containing WGA may be

particularly damaging for the proper functioning of the immune system…

… Although WGA is present in staple foods derived from cereals its concentration is

only about 300 mg/kg wheat germ… it is not unexpected that at this low normal

level… no toxic effects of WGA have been observed. However, the nutritional

evaluation of the effects of WGA at the dietary inclusion of 7 g/kg clearly showed

that the lectins reduces the utilization of dietary proteins, induces wasteful growth

of both the small intestine and pancreas, causes thymus atrophy and depress the

growth of rats. Moreover, it is particularly worrying that detectable amounts of

functionally and immunochemically-intact WGA are transported across the

intestinal wall and may reach the systemic circulation. The long-term effects of this

systemic absorption of WGA on immune function, metabolism and health are

unknown.”

 Kolberg J., et al, Immunoblotting Detection of Lectins in Gluten and White Rice Flour, Biochemical

and Biophysical Research Communications, 1987 Feb. 13;142(3):717-723 Link

“In the dry wheat grain WGA is found in the embryo portion, but it is reported to be

absent from the endosperm. After industrial milling the embryonal proteins are

found in the wheat germ fraction, whereas the flour fraction contains endosperm

proteins such as gluten. Our finding of a WGA-like lectin in the latter fraction is

therefore surprising…

… One possibility might be that both WGA and the rice lectin cause increased

intestinal permeability which permits passage of large molecules that are antigenic.

However, only gluten contains molecules that are able to elicit immune responses

leading to Celiac disease.”

 Mishkind M.L., et al, Localization of Wheat-Germ Agglutinin—Like Lectins in Various Species of the

Gramineas, Science, 1983 June 17; 220(4603):1290-2 Link

“Barley and rye embryos contain N-acetylglucosamine binding lectins that are virtually

indistinguishable by biochemical and immunological criteria from the well-

characterized wheat lectin, WGA…

… Our data demonstrate, however, that in addition to the characteristics noted by

Tsuda, the rice lectin is similar to WGA by immunological and histological criteria.”

Opioid Peptides

Endogenous Opioid Peptides - Endorphins

Endorphins are neurotransmitters that are released in the central nervous system (CNS) during times of

stress, such as physical exertion or physical injury, to protect us from pain. Because endorphins block

pain messages in the CNS, we feel less pain and a mild sense of euphoria when they are released.

Endorphins, when released in the brain, work by activating opioid receptors that are widely distributed

throughout the brain and body, especially in the nervous, endocrine and immune systems. Opioid

receptors belong to the family of G protein-coupled receptors.

 G-Protein Coupled Receptors, YouTube (0:51) Link

Fortunately, you don't have to be in great pain or suffering from injury to experience the pleasurable

feelings associated with endorphins. Exercise (“runner’s high) acupuncture, massage therapy, sex,

laughter, meditation and eating certain foods can also stimulate endorphin release. The limbic system is

rich with opioid receptors, and when endorphins reach the opioid receptors on the highly emotional

limbic system – a person will experience pleasure and a sense of satisfaction.

At least 20 types of endorphins have been discovered in humans, with beta-endorphin being the most

effective endorphin – giving the most euphoric effect.

Opioids

A class of narcotic drugs called opioids are chemically very similar to endorphins. Therefore, opioid drugs

are those having an agonist action at opioid receptors. Examples of opioid drugs are – opium, heroin,

morphine and codeine. Morphine and some other opioid alkaloids are still the only analgesics effective

for treatment of patients with extremely severe pain.

Although the term opiate is often used as a synonym for opioid, the term opiate is properly limited to

the natural alkaloids found in the resin of the opium poppy. While the broader term – opioid – refers to

semi-synthetic and synthetic drugs with opium or morphine like pharmacological effects.

The use of opioid drugs floods the opioid receptors, producing intense exaggeration of – dulling pain and

providing a feeling of euphoria. This obviously sounds nice, unfortunately these opioid drugs have one

serious side effect which is that they are highly addictive. There are several types of opioid receptors

with sub-types being reported as well. The major opioid receptors and their effects are:

 Mu receptor (main receptor) – stops pain and slows breathing, and provides euphoria.

 Delta receptor – also gives a feeling of euphoria

 Sigma receptor – relieves depression

 Kappa receptor – stops pain and causes constriction of the pupils, but with no feeling of

pleasure. Opiates that stimulate only the kappa receptor can be useful to relieve pan without

the worry of addiction.

 Opioid Pharmacology, YouTube (14:42) Link

Opioid Peptide Foods - Exorphins

Some foods containing proteins (long chains of amino acids) are broken down by digestion to peptides

(shorter chains of amino acids). If these short peptides are not broken down any further they may

mimic opioid effects in the brain of susceptible individuals. Because these peptides originate from

outside the body – exogenous – and they can have morphine like effects on the body they are referred

to as – exorphins.

Eating opioid peptide foods results in the production of exorphins which (for some people) produce a

sense of euphoria, happiness, and sleepiness as well as reduction in pain sensation. This occurs because

exorphins, like naturally occurring endorphins and opioid drugs, work by activating the opioid receptor.

Therefore, the consumption of exorphin producing opioid peptide foods may contribute to mental

disturbances (i.e. schizophrenia), appetite disorders and addictions to these foods.

“But the “high” of wheat is not like the high of heroine, morphine, or Oxycontin. This

opiate, while it binds to the opiate receptors of the brain, doesn’t make us high… it

make us hungry…

… This is the effect exerted by gliadin, the protein in wheat that was inadvertently

altered by geneticists in the 1970s during efforts to increase yields” (Davis 2011)

The opium poppy is not the only plant or source of natural substances that bind with the opioid receptor

in humans. Below is a list of other plants and natural sources that are consumed as foods which contain

opioid peptides:

Wheat, Rye, Barley – contains the opioid peptide - gliadin Rice – contains the opioid peptide - albumin Oats – contains the opioid peptide - avenin Milk – contains the opioid peptide - casein. Spinach – contains the opioid peptide - rubiscolins. Meat – contains the opioid peptides – cytochrophin and hemorphin

“… gluten is degraded to a mix of polypeptides… These polypeptides were

discovered to have the peculiar ability to penetrate the blood-brain barrier that

separates the bloodstream from the brain…

… Once having gained entry into the brain, wheat polypeptides bind to the brain’s

morphine receptor, the very same receptor to which opiate drugs bind.”

“The investigators speculated that exorphins might be the active factors derived

from wheat that account for the deterioration of schizophrenic symptoms.” (Davis

2011)

“The evidence now indicates that when susceptible individuals eat gluten, they

produce excessive amounts of zonulin, which opens the barriers formed by

epithelial cells, allowing exorphins to reach the bloodstream then the brain and alter

brain and immune function…

… there can be little doubt that these addictive peptides are reaching the brain and

with varying degrees of impact, wreaking havoc on the consciousness of some

hapless victims, while having little or no discernible impact on others…

… We now know that, not only do these exorphins cause addiction, thy also alter

blood flow patterns in the brain and cause excessive stimulation, all of which are

suggestive of gluten’s role in a wide range of psychiatric and neurological ailments.”

(Hoggan 2010)

 Teschemacher H., Opioid receptor ligands derived from food proteins, Current Pharmaceutical

Design,9 (16): 1331 – 1344 (2003) Link

“During the last two decades a variety of food protein fragments has been

demonstrated to elicit biological effects in various in vitro and vivo test systems. A

considerable part of these bioactive peptides are opioid receptor ligands, which may

be regarded as exogenous supplements to the endogenous opioidergic systems of

the human organism. Most of these food-derived opioid receptor ligands are

fragments of the milk proteins alpha-, beta- or kappa-casein, alpha-lactalbumin,

beta-lactoglobulin or lactotransferrin; however, also wheat gluten, rice albumin,

bovine serum albumin or hemoglobin, i.e. possible constituents of meat, and even a

protein from spinach could be demonstrated to contain fragments behaving like

opioid receptor ligands.”

 Vaccine Safety Conference Session 20 – Dr. Richard Deth, PhD, YouTube (50:56) Link

“Opiate peptides from food inhibit cysteine, methionine and glutathione uptake…

… cow’s milk is the worst.

Both casein and gluten are broken down into certain peptides that are relatively

stable. The protein casein is broken into casomorphins. The “morphins” are so

named because, like morphine, they act on the opiate receptors. The most famous

one, beta casomorphin 7 (BCM7), has seven amino acids. …

… However, the human BCM7 is markedly different than bovine BCM7 from the cow.

It turns out that the BCM7 from a cow inhibits cysteine at least twice as much as the

BCM7 from a human mother. The implications for health are profound if you start

thinking about formula feeding and all the dairy products from cows in our diet. A

diet high in dairy from cows can promote a decrease in our antioxidant capacity, our

ability to make enough glutathione.

Similarly, the protein in gluten is known as gliadin, and it also creates a seven amino

acid peptide, like BCM7.”

Amylopectin - A

Another way in which grains, especially wheat, create damage is through the blood sugar – insulin

effect. For example, the complex carbohydrates in wheat are made up of the chain of branching glucose

units called amylopectin. In the intestines amylopectin is digested by the salivary and stomach enzyme –

amylase. Amylase rapidly digests amylopectin and converts it to glucose which is then quickly absorbed

into the blood stream.

Other carbohydrate foods also contain amylopectin, but not the same kind of amylopectin as wheat.

Amylopectin from legumes is called amylopectin-C, and is the least digestible. Amylopectin-B is the form

found in bananas and potatoes and, while more digestible than amylopectin-C, still resists digestion to

some degree.

The most digestible form of amylopectin is amylopectin-A, found in wheat. Because it is the most

digestible, it is the form that most rapidly increases blood sugar. This is why, gram for gram, wheat

increases blood sugar to a greater degree than, say kidney beans or potato chips. Or in other words,

wheat products are no better and are often worse, than even simple carbohydrates such as sucrose.

“The amylopectin-A of wheat products, complex or no, might be regarded as a

supercarbohydrate, a form of highly digestible carbohydrate that is more efficiently

converted to blood sugar than nearly all other carbohydrate foods, simple or

complex…

… People are usually shocked when I tell them that whole wheat bread increases

blood sugar to a higher level than sucrose. Aside from extra fiber, eating two slices

of whole wheat bread is really little different and often worse, than drinking a can of

sugar sweetened soda or eating a sugary candy bar.” (Davis 2010)

The measurement of blood sugar after consumption of a particular food is called – the glycemic index.

Simply put the higher the blood sugar levels the higher the glycemic index. A current short list of 62

common foods – especially grains – can be found in the study below:

 Atkinson F.S., et al, International Tables of Glycemic Index and Glycemic Load Values: 2008,

Diabetes Care, Dec 2008; 31(12):2281-2283 Click “TABLE 1” Link

 The Glycemic Index, by David Mendosa, Informative Site Link

Therefore, wheat products elevate blood sugar levels more than virtually any other carbohydrate, from

beans to candy bars. This has important implications for body weight, since glucose is unavoidably

accompanied by insulin, the hormone that allows entry of glucose into the cells of the body, converting

the glucose to fat. The higher the blood glucose after consumption of food, the greater the insulin level,

the more fat is deposited.

“Historically, the hormone insulin evolved as the body’s mechanism to store excess

carbohydrate calories as fat in case of future famine. That means that insulin

aggressively promotes the accumulation of body fat…

… Not only do increased levels of insulin levels tell the body to store carbohydrates

as fat, they also tell it not to release any stored fat. This blocks you from using your

stored body fat to produce energy.” (Mercola 2004)

Figure: Amylopectin - A

And finally, the consumption of amylopectin-A from wheat induces a surge of glucose and insulin

producing a 120 minute high followed by the inevitable drop in glucose – CRASH. Crashing causes

hunger for more carbs. This creates the roller coaster scenario which most people are familiar with

which only puts more pounds of fat on the waistline. Soon, over time the constant demand for insulin

along with the additional visceral fat can create conditions such as “insulin resistance”, type 2 diabetes,

joint inflammation, heart disease, endocrine disruption among other things.

“The list of other health conditions triggered by visceral fat is growing and now

includes dementia, rheumatoid arthritis, and colon cancer. This is why waist

circumference is proving to be a powerful predictor of all these conditions, as well

as of mortality” (Davis 2010)

“By far, one of the most critical problems with grain consumption is that grains

elevate blood glucose levels, and thus trigger cravings for sweets.” (Mercola 2004)

 Wheat: The Unhealthy Whole Grain-Part 1, Dr. William Davis, Wheatbelly Channel YouTube (19:59)

Link

 Wheat: The Unhealthy Whole Grain-Part 2, Dr. William Davis, Wheatbelly Channel YouTube (19:11)

Link

As you can see Amylopectin – A can be responsible for contributing to the development of several

health conditions. Along with continual insulin spikes, one of the more important ways in which these

health conditions arise is via a process called glycation. Or more specifically – advanced glycation end-

products (AGEs).

Advanced Glycation End Products (AGEs)

Glycation is a reaction that takes place when simple sugar molecules such as fructose and glucose

become attached to proteins without the moderation of an enzyme. This results in the formation of a

new compounds called - Advanced glycation end-products (AGEs). The more grains one consumes the

higher and more frequently blood glucose increases, the more glycation occurs, the more AGEs are

produced. Anywhere glucose goes (which is everywhere) AGEs will follow.

AGEs are useless debris and cannot be burned for energy, they provide no lubricating or communicating

functions, they provide no assistance to nearby enzymes or hormones… AGEs provide no useful

function. The accumulation of AGEs in the blood and tissue eventually become the stuff that stiffens

arteries, clouds the lenses of the eyes, disrupts neural connections in the brain, causes nerve

damage/neuropathies, makes cartilage brittle, causes joint inflammation, kidney disease and skin to

wrinkle and sag, and in general accelerate the aging process.

 Glycation, What is this and how does this relate to aging, Dr. Johnny Bowden PhD, YouTube (2:06)

Link

 Formation of AGEs, YouTube (1:17) Link

The classic disorder indicative of a high blood glucose level is diabetes. And just as you might expect

diabetics also have higher blood levels of AGEs. A 60% greater level of AGEs compared to non-diabetics

to be exact. And in diabetics we see a much higher incidence of health problems.

“The story doesn’t end at greater levels of AGEs. Higher AGE blood levels spark the

expression of oxidative stress and inflammatory markers. The receptor for AGEs, or

RAGE, is the gatekeeper to an assortment of oxidative and inflammatory responses,

such as inflammatory cytokines, vascular endothelial growth factor, and tumor

necrosis factor. AGEs therefore set an army of oxidative and inflammatory

responses in motion, all leading to heart disease, cancer, diabetes, and more.” (Davis

2010)

Not to confuse things, but it should be also noted that there is a second source of AGEs other than those

that create high blood glucose levels from wheat – amylopectin A. That second source would be from

animal products such as meats and cheese. In particular animal products heated to high temperature

(i.e. broiling, frying, deep fried) increase AGE content more than a thousand fold.

 Pillar of Health #3 – Glucose & Glycation with Dr. Shawn Talbot PhD, YouTube (10:23) Link

Testing to determine the rate of AGE formation in a person’s body can be done via a simple blood test

called – hemoglobin A1c (HbA1c). Like all other proteins of the body, hemoglobin is subject to glycation.

The reaction occurs readily and like other AGE reactions is irreversible. While usually used for the

purpose of diabetes control, the HbA1c test can also serve as a simple index of glycation and AGE

formation.

“HbA1c – glycated hemoglobin – therefore provides a running index of glucose

control. It also reflects the degree you are glycating body proteins beyond

hemoglobin. The higher your HbA1c, the more you are also glycating the proteins in

the lenses of your eyes, in the kidney tissue, arteries, skin, etc. In effect, HbQ1c

provides an ongoing index of aging rate: the higher your HbA1c, the faster you are

aging.

Conclusion

Well… it appears that grains, especially wheat, are not as healthy a food as most of us have been lead to

believe. For people who are “sensitive” to gluten the research is very clear – the gluten grains of wheat,

rye and barley need to be permanently eliminated from the diet.

And though the research for the remaining grains (oats, rice, etc.) is ambiguous, there is still enough

evidence to indicate that for some people these grains will also be problematic. Therefore, it would be

wise to eliminate them for 30 day trial period to see if there is any affect.

“The history of grain is that in 1943 the FDA passed a law banning the sale of grain

without fortification… why? Because when you process grain and you give it out as

food it causes disease… it causes beriberi… it causes pellagra… and these are

diseases that kill people. So how can a food that is supposedly so good for us cause

disease unless we add synthetic vitamins to it.”

“The consequences of wheat consumption, however, are not just manifested on the

body’s surface; wheat can also reach deep down into virtually every organ of the

body, from the intestines, liver, heart, and thyroid gland all the way up to the brain

In fact, there’s hardly an organ that is not affected by wheat in some potentially

damaging way” (Davis 2010)

References

Books

Note: all books were obtained either at UW Library, King County Library, Snohomish County Library or Bastyr

University Library. A couple of books were available on line (e-books, PDFs, googlebooks). Links are provided to

give a visual of book cover and other information.

- Can a Gluten-Free Diet Help?, by Lloyd Rosenvold MD, Keats Publishing (1991) Link

- Celiac Disease a Hidden Epedemic, by Peter Green, William Morrow Publishing (2010) Link

- Celiac Disease: Etiology, Diagnosis and Treatment, Edited by Matthew Edwards, Nova Science Publishing

(2009) Link

- Cereal Killers: Celiac Disease and Gluten Free, by Dr. Ron Hoggan Ed.D., CreateSpace (2010) Link

- Chemical and Biological Properties of Food Allergens, Edited by Lucjan Jedrychowski, CRC Press (2009)

Link

- Core Topics in Pain, by Anita Holdcroft, Cambridge University Press (2005) Link

- Eat Right 4 Your Health, by Dr. Peter D’Adamo, Century (1998) Link

- Fermented Cereals: A Global Perspective by Norman Haard, Food and Agriculture Organization of the

United Nations (1999) Link

- Food Chemistry, by Owen Fennema, CRC Press (1996) Link

- Gluten-Free Food Science and Technology, Edited by Eimear Gallagher, Wiley-Blackwell (2009)

e-book Link

- Healthier Without Wheat, by Dr. Stephen Wanger, Innate Health Publishing (2009) Link

- Illegal Drugs, by Paul Gahlinger, Penguin (2004) Link

- The Irritable Bowl Syndrome Solution, by Stephen Wangen ND, Innate Health Publishing (2006)

Link

- The Mood Cure, by Julia Ross, Penguin (2004) Link

- The No-Grain Diet, Dr. Joseph Mercola, Plume (2004) Link

- Wheat Belly, by William Davis MD, Rodale Books (2011) Link

Publications

Publications are sited within the report

Videos and Audio Productions

Video and Audio Productions are sited within the report

WWW:

- Allergy Advisor Link

- AnaSpec Link

- Dr. Alessio Fasano (University of Maryland Center for Celiac Research) Link

- Dr. David Clark’s YouTube Channel Link

- Dr. Joseph Mercola Link

- Dr. Martin Kagnoff - Understanding Celiac Disease and Gluten Sensitivity: Your Gut Reaction, University of

California Television Link

- Dr. Michael Eades Link

- Dr. Peter D’Adamo – Eat Right For Your Type Link

- Dr. Peter Osborn’s – Gluten Free Society Link

- Dr. Richard & Vikki Peterson Link

- Dr. Robert McCarthy Link

- Dr. Rodney Ford Link

- Dr. William Davis – Wheat Belly Link

- GreenMedInfor.com Link

- Melissa Diane Smith (Nutritionist) Link

- Mendosa.com Link

- University of Chicago Celiac Disease Center Link

- Whole Nine Link