The Great Grain Conundrum by Mark J Donohue .docx

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)
http://en.wikipedia.org/wiki/Antinutrient
http://upload.wikimedia.org/wikipedia/commons/e/eb/MyPyrami
dFood.svg
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:

calcium & magnesium thereby causing
mineral deficiencies. Phytic acid also chelates the vitamin –
niacin (B3).
od. 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.
Foundation (more in-depth article) Link
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.
http://en.wikipedia.org/wiki/Phytic_acid
http://en.wikipedia.org/wiki/Pepsin
http://en.wikipedia.org/wiki/Amylase
http://en.wikipedia.org/wiki/Trypsin
http://en.wikipedia.org/wiki/Phytase
http://www.westonaprice.org/food-features/living-with-phytic-
acid
http://www.westonaprice.org/food-features/living-with-phytic-
acid
http://www.youtube.com/watch?v=M6rzGntPo80
http://en.wikipedia.org/wiki/Goitrogen
http://en.wikipedia.org/wiki/Goitre
http://en.wikipedia.org/wiki/Millet
http://en.wikipedia.org/wiki/Autoimmune_disease
http://en.wikipedia.org/wiki/Hashimoto%27s_thyroiditis
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
(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.

http://en.wikipedia.org/wiki/Gluten
http://en.wikipedia.org/wiki/Prolamin
http://en.wikipedia.org/wiki/Glutelin
http://en.wikipedia.org/wiki/Proline
http://en.wikipedia.org/wiki/Glutamine
http://en.wikipedia.org/wiki/Gliadin
http://en.wikipedia.org/wiki/Glutenin
http://www.youtube.com/watch?v=WEL8w6BMt3A
http://en.wikipedia.org/wiki/Wheat_allergy
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.
http://en.wikipedia.org/wiki/Celiac_disease
http://www.amazon.com/Celiac-Disease-Revised-Updated-
Edition/dp/0061728160/ref=sr_1_1?s=books&ie=UTF8&qid=13
37216910&sr=1-1
37216910&sr=1-1
http://en.wikipedia.org/wiki/Gluten_sensitivity
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.
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”
http://www.amazon.com/Wheat-Belly-Lose-Weight-
Health/dp/1609611543/ref=sr_1_1?ie=UTF8&qid=1337215045&
sr=8-1
http://www.youtube.com/watch?v=AxBZ5E8Ilf8&feature=relate
d
http://www.youtube.com/watch?v=DvK9KZy1xaw
– 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.”
ase 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”
-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.”
-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.”
http://www.youtube.com/watch?v=sJl0uqm3TkE
http://www.youtube.com/watch?v=PJk5saBx1jQ&feature=relate
d
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2830645/?tool=p
ubmed
http://informahealthcare.com/doi/abs/10.1080/00365529850172
557
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.
– Who Needs a Gluten Test?, YouTube,
More Gluten Symptoms (5:30) Link
– 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”
(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”
http://www.amazon.com/Cereal-Killers-Celiac-Disease-Gluten-
Free/dp/1449918204/ref=sr_1_2?s=books&ie=UTF8&qid=13372
16357&sr=1-2
http://www.youtube.com/watch?v=FtxfV49YYZM&feature=BFa
&list=UU1Wwy_XzJvXeAZ3WKbLf3Uw
http://www.youtube.com/watch?v=No358zDy34c&list=UUoiSo5
WDJmRxOf2cqgC7DSg&index=13&feature=plcp
http://en.wikipedia.org/wiki/Zonulin
http://www.youtube.com/watch?v=0BooZh7ex-
8&list=UUONvCuEp5KKiJ9zy33Duw9A&index=3&feature=plp

p_video
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)
-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%)
http://www.glutenfreesociety.org/
http://www.glutenfreesociety.org/
http://www.thorne.com/altmedrev/.fulltext/10/3/172.pdf
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.”
-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
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…
http://www.sciencedirect.com/science/article/pii/S00028223000
01425
http://www.jci.org/articles/view/30253/figure/2
http://www.youtube.com/watch?v=cv5RwxYW8yA&list=UUoiS
o5WDJmRxOf2cqgC7DSg&index=25&feature=plcp
… 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”
nterview

with Dr. Peter Osborne,
Glutenology YouTube Channel – Very Informative ( 5:56)
Link
-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.”
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.”

http://www.youtube.com/watch?v=drBSac1r8C8&list=UUoiSo5
WDJmRxOf2cqgC7DSg&index=19&feature=plcp
http://www.springerlink.com/content/d6723t3n722317x5/fulltex
t.html
ubmed
h
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.”
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
http://www.ncbi.nlm.nih.gov/pubmed/371884
http://journals.lww.com/jpgn/Abstract/1987/05000/An_Analysis
_of_Cereals_That_React_with_Serum.7.aspx

David Clark, YouTube (5:19) Link
Clark, YouTube (5:08) Link
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:

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.
http://www.youtube.com/watch?v=qKBq9RJof6I&feature=relate
d
http://www.youtube.com/watch?v=vYmaOvzj01w&list=UUONv
CuEp5KKiJ9zy33Duw9A&index=2&feature=plpp_video
http://www.youtube.com/watch?v=9jv3l8HJwew
http://en.wikipedia.org/wiki/Antibodies
Definitions
– if a test is 100% specific, it means there is
nothing else – no other medical condition

that can cause the positive result.
ty – 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
http://en.wikipedia.org/wiki/Transglutaminase
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.

http://en.wikipedia.org/wiki/Deamination
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
- Sensitivity/Specificity Chart -
Link
– Test Result Chart Link
Prospects, Internal Medicine Journal,
2008 Oct; 38(10):790-9 Current Discussion on Testing Link
– Testing for Celiac Disease, YouTube (6:42)
Link
– Lab Test for Gluten Sensitivity, YouTube (3:12)
Link

– Celiac Testing, YouTube (2:01) Link
- Link
- 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.
http://en.wikipedia.org/wiki/HLA-DQ2
http://en.wikipedia.org/wiki/HLA-DQ8
http://www.csaceliacs.info/diagnosis_of_celiac_disease_sensitiv
ityspecific.jsp
http://labtestsonline.org/understanding/analytes/celiac-
disease/tab/test
http://www.youtube.com/watch?v=wF7p4mexes4
http://www.youtube.com/watch?v=oatogM_Um6k
http://www.youtube.com/watch?v=xUAQNcSNC_Q
http://www.enterolab.com/StaticPages/TestInfo.aspx
http://cyrexlabs.com/
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.
http://en.wikipedia.org/wiki/Wheat_germ_agglutinin
http://en.wikipedia.org/wiki/Lectin
http://www.amazon.com/Eat-Right-4-Your-
Type/dp/071267716X/ref=sr_1_1?s=books&ie=UTF8&qid=1338
584518&sr=1-1
http://en.wikipedia.org/wiki/N-Acetylglucosamine
http://en.wikipedia.org/wiki/N-Acetylneuraminic_acid
http://en.wikipedia.org/wiki/N-Acetylneuraminic_acid

http://en.wikipedia.org/wiki/Glycocalyx
http://en.wikipedia.org/wiki/Ricin
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.
Wheat, by Dr. Joseph Mercola, Mercola.com
Very Informative Article Link
Joseph Mercola, Mercola.com
Very Informative Article Link
– The Dark Side of Wheat, Interview
with Sayer Ji, Glutenology YouTube
Channel (32:53) Very Informative Interview Link

PUNK: 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
lla 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.”
–

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…
http://en.wikipedia.org/wiki/Atomic_mass_unit
http://articles.mercola.com/sites/articles/archive/2011/07/05/oth
er-nonwheat-grains-can-also-hurt-your-health.aspx
http://articles.mercola.com/sites/articles/archive/2011/07/04/can
-eating-this-common-grain-cause-psychiatric-problems.aspx
http://www.youtube.com/watch?v=6Bo6pssG6As
http://www.youtube.com/watch?v=UQ5t6r_FiT4&list=UUAvk1k
wKwwBTmIEXNtjjB-Q&index=9&feature=plcp
http://www.datapunk.net/visualizations/lectins/lectin.pl
http://www.greenmedinfo.com/toxic-ingredient/wheat-germ-
agglutinin-wga
http://www.biomedcentral.com/1472-6823/5/10
“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.”
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”

ubmed
-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.”
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.”
http://www.ncbi.nlm.nih.gov/pubmed?term=antinutritive%20eff
ects%20of%20wheat-germ%20agglutinin%20and%20other
http://www.ncbi.nlm.nih.gov/sites/entrez/3827897?dopt=Abstra
ct&holding=f1000,f1000m,isrctnuw
-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.
-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.

http://www.jstor.org/stable/1690399?seq=1
http://en.wikipedia.org/wiki/Endorphin
http://en.wikipedia.org/wiki/Euphoria
http://en.wikipedia.org/wiki/Opiate_receptor
http://en.wikipedia.org/wiki/G_protein-coupled_receptor
http://www.youtube.com/watch?v=NB7YfAvez3o
http://en.wikipedia.org/wiki/Narcotic
http://en.wikipedia.org/wiki/Opioids
http://en.wikipedia.org/wiki/Agonist
http://en.wikipedia.org/wiki/Opium
http://en.wikipedia.org/wiki/Heroin
http://en.wikipedia.org/wiki/Morphine
http://en.wikipedia.org/wiki/Codeine
http://en.wikipedia.org/wiki/Alkaloids
http://en.wikipedia.org/wiki/Analgesics
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:
– stops pain and slows
breathing, and provides euphoria.
– also gives a feeling of euphoria
– relieves depression
– 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 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)
http://en.wikipedia.org/wiki/Opiate
http://en.wikipedia.org/wiki/Opium_poppy
http://en.wikipedia.org/wiki/Mu_Opioid_receptor
http://en.wikipedia.org/wiki/Delta_Opioid_receptor
http://en.wikipedia.org/wiki/Kappa_receptor
http://www.youtube.com/watch?v=2DNj8vfVACE
http://en.wikipedia.org/wiki/Schizophrenia
sr=8-1
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)
http://en.wikipedia.org/wiki/Casein
http://en.wikipedia.org/wiki/Rubiscolin
sr=8-1

sr=8-1
16357&sr=1-2
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.”
– 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.

http://xa.yimg.com/kq/groups/18630837/685088275/name/Exorp
hins.pdf
http://www.youtube.com/watch?v=z1L84EQ9S5k
http://en.wikipedia.org/wiki/Casomorphin
http://en.wikipedia.org/wiki/Insulin
http://en.wikipedia.org/wiki/Amylopectin
http://en.wikipedia.org/wiki/Amylase
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:

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

sr=8-1
http://en.wikipedia.org/wiki/Glycemic_index
http://care.diabetesjournals.org/content/31/12/2281.full#T1
http://www.mendosa.com/gidigest.htm
… 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)
http://www.amazon.com/The-No-Grain-Diet-Joseph-
Mercola/dp/0452285089/ref=sr_1_1?s=books&ie=UTF8&qid=13
37216585&sr=1-1
http://en.wikipedia.org/wiki/Insulin_resistance
http://www.amazon.com/The-No-Grain-Diet-Joseph-
Mercola/dp/0452285089/ref=sr_1_1?s=books&ie=UTF8&qid=13
37216585&sr=1-1
-Part 1, Dr. William
Davis, Wheatbelly Channel YouTube (19:59)
Link
-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.
Johnny Bowden PhD, YouTube (2:06)
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)
http://www.youtube.com/watch?v=WSDkJEF9aBY&context=C4
120171ADvjVQa1PpcFMRCHUEh9RbDSpP9ZmbwGn1X3RRn
YJdxCY=
http://www.youtube.com/watch?v=RmsxCN7htHM&context=C4
34342cADvjVQa1PpcFMRCHUEh9RbDZL8MRArFVAH3z5O0
VssKH8=
http://en.wikipedia.org/wiki/Glycation
http://en.wikipedia.org/wiki/Advanced_glycation_end_product
http://www.youtube.com/watch?v=S4QD4h7zSS4
http://www.youtube.com/watch?v=faDgYVHcOGM
sr=8-1
sr=8-1
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.
– 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)
http://www.youtube.com/watch?v=EVWIvbsSlUw
http://en.wikipedia.org/wiki/Glycated_hemoglobin

sr=8-1
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
http://www.amazon.com/Gluten-Free-Diet-Help-Keats-

healthbook/dp/0879835389
37216910&sr=1-1
http://www.amazon.com/Celiac-Disease-Etiology-Diagnosis-
Treatment/dp/1606926330/ref=sr_1_1?s=books&ie=UTF8&qid=
1337216179&sr=1-1
16357&sr=1-2
http://uwashington.worldcat.org/title/chemical-and-biological-
properties-of-food-
allergens/oclc/664233767&referer=brief_results
http://www.amazon.com/Food-Chemistry-Science-
Technology/dp/0824796918/ref=sr_1_9?s=books&ie=UTF8&qid
=1337217413&sr=1-9
http://www.amazon.com/Eat-Right-4-Your-
Type/dp/071267716X/ref=sr_1_1?s=books&ie=UTF8&qid=1338
584518&sr=1-1
http://www.fao.org/docrep/x2184e/x2184e00.htm#con
http://www.amazon.com/Food-Chemistry-Science-
Technology/dp/0824796918/ref=sr_1_9?s=books&ie=UTF8&qid
=1337217413&sr=1-9
http://uwashington.worldcat.org/title/gluten-free-food-science-
and-technology/oclc/437299687&referer=brief_results

http://www.amazon.com/Healthier-Without-Wheat-
Understanding-
Intolerance/dp/0976853795/ref=sr_1_1?s=books&ie=UTF8&qid
=1337216774&sr=1-1
http://www.amazon.com/Illegal-Drugs-Complete-History-
Chemistry/dp/0452285054/ref=sr_1_1?s=books&ie=UTF8&qid=
1337217373&sr=1-1
http://www.amazon.com/The-Irritable-Bowel-Syndrome-

The Great Grain Conundrum by Mark J Donohue .docx

Recommended

Recommended

More Related Content

Similar to The Great Grain Conundrum by Mark J Donohue .docx

Similar to The Great Grain Conundrum by Mark J Donohue .docx (17)

More from arnoldmeredith47041

More from arnoldmeredith47041 (20)

Recently uploaded

Recently uploaded (20)

The Great Grain Conundrum by Mark J Donohue .docx