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There
is some confusion in the terms applied in articles and conversations about
Celiac Disease, gluten, gliadin, and food intolerance. The terms Celiac, gluten, and gliadin each
have general and specific definitions, and knowing which one is being used is
important for full understanding of articles and research on the subject. The following Glossary is provided to give
some orientation as to how these important terms are used. A companion essay is available that
introduces The
Basic Factors of Gluten Sensitivity and Celiac Disease and how these
factors cause and contribute to illness.
Another
shorter glossary is found on http://www.naspgn.org/sub/celiac_disease.asp.
· Specifically, gluten is the storage protein
found in grains of wheat. But other
similar proteins are also called gluten in a general sense and are widely found
in grains and in at least one fruit (this fruit happens to be Buckwheat, but
Buckwheat is neither a wheat or a grass).
· In the general sense, glutens are a family of
very useful, very cheap, and very tasty proteins. Because wheat gluten is so useful, cheap, inexpensive,
cheap, tasty, and cheap, it can be found added to most packaged or
restaurant foods.
· The “gluten” from each type of glutinous seed
is a little bit different and has its own name, but all are loosely called
“gluten”. Likewise, tolerance to these
different proteins varies between people.
The point is that some glutens may be safe for some people to eat while
others are not.
· More people have health problems with wheat
gluten and very similar glutens in rye and barely than with other types of
gluten and more people have health problems with wheat gluten than with any
other single staple foodstuff. Most
other glutens are generally well tolerated (but not always).
· The chemical problem in Celiac Disease and
Gluten Intolerance is a specific fragment of wheat gluten, a family of
sequences of amino acids called Gliadin. Very similar fragments that also cause injury
are found in rye and barley (also in oats but that is a special
case).
· Gliadin is a molecule found on the surface of
the Adenovirus (ặd΄-ən-ō-vī΄-rəs), which
causes common lung infections.
Gliadin’s job is to dig the virus into and between cell walls. Many humans
have the dominant genes needed to made antibodies that bind to gliadin and
rapidly stop any Adenovirus infection.
This is a great survival trait for people who live or work
indoors in winter with many other humans.
· Gliadin is also found in large quantities in wheat gluten. When gliadin in gluten becomes water
soluble, it is free to bind to cells.
If the victim can make antibodies to gliadin, the body then treats those
cells as a virus infection.
· Gliadin triggers an immune response when it contacts
any of a number of cells in the body of genetically susceptible
individuals. This response damages the
surrounding tissue and thereby has the potential to set off many other heath
problems throughout the body.
· Gliadin is classified as a member of a family
of sequences called prolamines.
Prolamines in rye and barley glutens are have their own technical names,
but they are often just called gliadin because they are chemically similar and
have the same toxic reactions (the actually prolamin from rye is secalin, from
barley hordein and from oats avenin).
· Gliadin is very unique among foods in that it contains
substantial lengths of poly-glutamine. Prolamines in other grains associated with milder
gluten sensitivity happen to contain shorter lengths of poly-glutamine.
· Gliadin molecules in gluten
are not very water soluble, and so they are not very digestible unless they are
subject to such processes as fine grinding, baking, fermentation, and chemical
treatment and synthesis.
· If the gliadin remains intact within the
digestive tract (and it is a particularly stable molecule) it can bind to the
intestines, especially if the intestine lining is weak or flawed. Significant amounts of gliadin eaten can cross
the intestine into the blood stream.
· Since the 1970’s, more chemically treated
gliadin is in the diet. In the 80’s,
Americans increased the amount of wheat they ate; having been told it was
healthier than meat. In the 1990’s,
additions of “vital gluten” and gluten-based flavors were increased in
manufactured foods. In the 2000’s
Kansas State University Grain Science Department (and other places) works to
increase gliadin content in wheat and may attempt introduction of gliadin in
other grains such as rice.
Poly-glutamine
(poly-Q) is a chain where the molecule glutamine (Q) is repeated many times within
a protein. This is actually quite rare.
Long poly-glutamine chains are really only found in three places:
1)
Normal
transcriptional regulation proteins, which are found especially in the central
nervous system and which are normally short lived and regulated by Ubiquitin.
2)
Specific
protein "mutations" associated with degeneration
of the central nervous system.
3)
Gliadin in
wheat (Alpha and beta). (Shorter glutamine chains are found in other grain
storage proteins.)
Excessive
long chain poly-glutamine is associated with neuron toxicity. Toxicity of poly-glutamine
is implicated in poly-glutamine
diseases, which include Huntington’s Disease and some types of ataxia. This mechanism provides (hypothetical at
this time) means by which gluten triggers, aggravates, or seems to cause degenerative
CNS disorders and provides means by which gluten mimics genetic CNS
disorders when the genetic disposition is not present.
In
reference to a person, a Celiac is specifically someone who has Celiac
Disease. Some generally call anyone
who has any gliadin
sensitivity a “Celiac” because the diet therapy is the same regardless of the
symptoms and also because gliadin sensitivity is a required precursor to
classic Celiac Disease. It is a lot
easier to refer to a person as being a “Celiac” than as “a gluten intolerant
person” or as “a gliadin sensitive person”. 
Just
as Celiac Disease has many symptoms, there is also more than one definition of
Celiac Disease. As
classically defined, a Celiac only had a chance of correct diagnosis if
that person was already wasting away.
Many
texts describe Celiac Disease as food intolerance or inability to digest
gluten,
but this is outdated since we now know about the involvement of the immune
system. The question remains whether
Celiac Disease is an allergy to gluten or an autoimmune condition
caused by gluten. Actually, gliadin
sensitivity is the common delayed
allergy to wheat gluten that usually progresses into one or more autoimmune
conditions, of which Celiac Disease is just one of many.
As
you study the relationships between gluten and any given disease, it is
important to know which definition applies to the research you are
reading. Usually, the Classic
Celiac Disease definition is used, and therefore it is likely that such a
study has not considered the broader cases of general gluten intolerance.
In
its most traditional, narrow, or specific definition, “Classic” Celiac Disease
is a diagnosis of:
1. antibodies against gluten
(allergy) OR the body’s own tissues (autoimmunity), AND
2. specific microscopic injury
to the small intestine, AND
3. malabsorption
possibly with chronic diarrhea (sprue), AND
4. clinical
response to a gluten-free diet, AND
5. return
of symptoms on return of gluten to the diet.
Clearly, this is a very narrow definition of the
condition, one that can delay treatment as the full-blown classic symptoms
often develop separately and slowly over time.
This
classic definition is convenient for researchers and primary care doctors
because of its narrowness and historical precedent. The narrow definition is
also profitable for drug manufactures as it delays application of a diet
therapy to many chronic conditions. But
the narrow definition can be worse than useless to people who suffer from some
form of Gluten
Intolerance or Gluten_Sensitivity
other than Classic Celiac Disease because its use may lead to
misdiagnosis.
This
new term is an even narrower definition of the condition. Diagnosis of CDA requires detection of
antibodies to Human tissue Transglutaminase (HtTG) in the blood. The presence HtTG antibodies indicates that
a patient’s gluten sensitivity has progressed to an autoimmune condition
against the intestines or possibly the brain or other organs containing
HtTG. According to proponents of this
test, if you to not have HtTG antibodies in the blood then you do not have
Celiac Disease -- for better or worse, such a protocol excludes from treatment
any patient whose food sensitivity has not yet progressed to intestinal
autoimmunity.
In
its most general definition, any illness, condition, or symptom
caused by sensitivity to gliadin
from gluten
could be called Celiac Disease because the basic cause and the diet therapy
would be the same in any case. The term
Atypical Celiac Disease applies to many conditions other than
malabsorption that can improve or be cured on a gluten free diet. Such conditions include nerve damage,
obesity, and thyroid and skin problems to name a very few. For a more complete list, please see the annotated
list of symptoms and health problems associated with gluten sensitivity.
Some
cases of Atypical Celiac Disease might only be diagnosed by diet test
or by detection of anti-gliadin anti-bodies anywhere in the body. Because the gut is not fully involved,
antihuman tissue transglutaminase (TTG) and endomysial antibody (EMA) tests may
be negative.
All
forms of Celiac Disease are also forms of Gluten
Intolerance, Gluten
Sensitivity, or Gliadin
Sensitivity. Ironically, it turns
out that Atypical Celiac Disease is 5 to 10 times more common
than “Typical” Celiac Disease!
Silent
Celiac Disease is the condition where a person has blood test
results that show celiac disease and also has injured small
intestines, but has no recognized classic or atypical symptoms (or the
symptoms may so very mild as to be barely noticeable).
When
Celiac Disease is silent, it may develop more classically or atypically at any
time later in life.
Latent
Celiac Disease is the condition where a person has blood test
results that show celiac disease but has normal small intestines and no recognized
signs of malabsorption
or diarrhea. However, the severity of
malabsorption and diarrhea symptoms in Celiac Disease are greatly dependent on
diet and medical history and are in some part dependent on the severity of the
gliadin sensitivity. The patient has to
be particularly vigilant that a doctor doesn’t consider the blood tests to be
false in these cases.
When
Celiac Disease is latent, it may develop more classically at any time later in
life. The Latent Celiac probably has other immediate health injuries that could
benefit from a gluten free diet.
While
we are here, the term Celiac Sprue is an older name for Celiac Disease. Sprue is a condition of chronic diarrhea,
emaciation, and anemia, caused by defective absorption of nutrients from the
intestinal tract. Classic Celiac
Disease is the most common form of Sprue other than Tropical Sprue, but most
cases of Gluten
Intolerance would not be characterized as sprue.
It
is interesting that many places refer to gluten intolerance or Celiac Disease
as a genetic disorder. The
ability to make antibodies to gliadin is a dominant gene and it is a perfectly
good defense against a common virus.
This is a survival trait, not a disorder. Is not the problem really wheat, which is a genetically
manipulated grain that was not quite perfectly adapted for human food?[1]
Consider
this scene: An infantryman with a laser designator is specifically trained to hunt
for and recognize an enemy tank by its characteristic shape. When the infantryman contacts and recognizes
an enemy tank, he shines his laser designator on the tank. A combat aircraft drops a smart bomb that
tracks the laser designation on the tank.
Now,
in terms of the immune system, the tank is a germ with a characteristic
“shape”, the smart bomb is a Killer T-cell, and the specifically trained
infantryman with a laser designator is the antibody.
Antibodies are made so one end is coded to match a specific protein on the surface of a specific germ while the other end is made to trigger a Killer T-cell. When an antibody contacts a germ that matches its code, it latches onto the germ. When a Killer T-cell contacts an antibody on a germ, it “blows up” and releases a poison right next to the germ.
The
problem is, an antibody will latch to anything that fits its code. An antibody evolved over 100 million years
to fight off an adenovirus infection can’t tell an adenovirus from a matching
piece of wheat protein.
By
the way, inflammation is often the collateral damage caused by the
Killer T-cell “smart bomb”.
An
allergy is an abnormally high sensitivity to certain substances, such as
pollens, foods, or microorganisms.
However, it seems conventional that an allergy is particularly a
sensitivity that involves an immune reaction.
Familiar allergies are reactions to things in the air like pollen and
mold, and immediate reactions to food where you “swell up and drop dead”. However, common food allergies are mostly
delayed reactions where noticeable symptoms develop over hours or days, even
months or years. It is very difficult
to recognize the causes of delayed allergic reactions.
Food intolerance is sensitivity to a specific food or set of
foods. But there are several different
forms of sensitivity. Glucose
intolerance is the weakened ability of cells to absorb glucose (also known as
Type 2 Diabetes). Lactose intolerance
is the inability to digest lactose. The
immune system reacting to a specific protein in a food is a delayed allergy,
but is still a form of food intolerance.
Most technically, gluten intolerance is sensitivity to gluten.
A problem is that some out-of-date publications say that Gluten
Intolerance or Celiac Disease is food intolerance, not an allergy
(probably because the author was not yet familiar with the role of the immune
system in Gluten Intolerance). But
other publications say that Celiac Disease is an allergy, not food
intolerance.
Gluten intolerance is an allergy.
But whereas most recognized allergies involve fast IgE type antibody
reactions, Gluten intolerance involve slower IgA and IgG type antibody
reactions. But the general symptoms of
this reaction are such that that the localized IgA and IgG gluten allergy
reaction in the gut look a lot like a digestion problem.
In fact, gluten intolerance does cause other food intolerances,
such as to lactose (milk sugar), but also to many other starches, proteins, and
fats, because gluten intolerance damages the body’s ability to digest food.
There has been a tendency to describe Gluten Intolerance as the
inability to digest wheat gluten. A
Celiac can probably digest gliadin just as well as anybody (i.e., poorly), at
least until the immune reaction damages the gut and then the Celiac has more
trouble digesting a lot of things. When
a person drinks milk he can’t digest, bacteria go crazy on the undigested milk
sugar and make gas and toxins. This
condition is commonly recognized as lactose intolerance. But when a Celiac eats gliadin,
he likely also has trouble digesting milk because of the injuries caused by the
reactions to gliadin,
so it might just look like the Celiac has a digestive problem rather than an
immune problem.
From
http://bmj.bmjjournals.com/cgi/content/full/318/7200/1710
“Marsh's
"modern" definition of gluten sensitivity is to be recommended:
"a state of heightened immunological responsiveness to ingested
gluten in genetically susceptible individuals."10 Such
responsiveness may find expression in organs other than the gut.
Gastroenterologists, dermatologists, neurologists, and other physicians
need to be aware of these developments if the diagnosis and treatment
of the diverse manifestations of gluten sensitivity are to be
advanced. The aetiology [study of causes or origins] of such diverse
manifestations presents the next challenge.”
The
reaction to gluten is brought about by a person’s ability to make anti-gliadin
antibodies. If a person has
anti-gliadin antibodies in the body, then that person is gluten and gliadin
sensitive, and that person’s immune system will kill any tissue that is
contacted by gliadin. Sometimes,
anti-gliadin antibodies can be detected in the blood, and this has been part of
the conventional diagnosis for Celiac Disease.
The problem is, blood testing for anti-gliadin antibodies in the
blood has proven unreliable[2]. However, it has recently been demonstrated that it is much more reliable
to test for anti-gliadin antibodies in the stool than in the blood[3].
In
an autoimmune condition, the immune system treats some part of the body just as
if that part is some sort of infection or cancer. (It may well be that most Autoimmune Conditions are actually
reactions against remains of damaged tissue or some other chemical
associated with tissue repair rather than reactions against healthy tissue.)
Anything
relating to, or affecting the endomysium is called endomysial. The endomysium
is the fine connective tissue sheath surrounding a muscle fiber and also nerve
fibers. Autoimmune reaction to the
endomysium is associated with Classic Celiac
Disease. The presence of antibodies
to the endomysium could cause an autoimmune attack to muscles and nerves. This would also weaken the defenses of
nerves against other toxins.
Tissue
transglutaminase is a very important enzyme that helps repair
damaged tissue. Elevated levels of tissue
transglutaminase occur where there is tissue damage or inflammation. Concentration of tissue transglutaminase
also normally occurs in the brain. Autoimmune reaction to tissue
transglutaminase is associated with Classic Celiac
Disease. The presence of antibodies
to tissue transglutaminase could cause an autoimmune attack at any wound or
site of inflammations, slowing healing and perpetuating chronic inflammation. Concentration of tissue transglutaminase
also normally occurs in the brain, so autoimmunity to tissue transglutaminase
could trigger immune attack in the brain.
Malnourishment
is the problem where some nutrition is missing in the diet, which results in
health problems from nutritional deficiencies.
Malabsorption
is the problem where the nutrition is present in the diet, but it is not being
absorbed. This is a bigger problem than
simple malnutrition! Sure, you get
deficiency problems, but you also get problems caused by undigested food
decaying and fermenting in your gut for days (imagine alcohols, acids, and much
worse forming in your gut).
In
malabsorption, a some types of fats, starches, sugars, or proteins can’t be
absorbed completely. They can’t be
absorbed because of inflammation or loss of tissues that normally absorb
certain nutrients or produce the enzymes needed to break down certain
nutrients. This brings about several
problems:
First,
there are the same nutritional deficiencies that happen with malnutrition.
Second,
the patient or doctor might not suspect a deficiency because the nutrients are
known to be in the diet, resulting in a missed diagnosis.
Third,
and this a very important feature of malabsorption, food not absorbed
remains in the intestinal flow where it can become rancid and acidic or become
rich food for excessive bacteria and yeast. Fermentation of unabsorbed
food produces excess gas. Rancid food chemicals and bacterial toxins
irritate the intestine and surrounding organs. Inflamed intestines
increase that body's requirements for antioxidant vitamins and further reduce
the intestine's ability for absorb nutrients.
A doctor not trained to recognize malabsorption may not recognize it in
this case.
Specific
malabsorption may be diagnosed as specific food intolerances, but the real
culprit is the gliadin that causes secondary intolerances. The doctor that was taught that gluten
intolerance is rare would not consider investigation of the underlying problem.
Forth,
general or specific food cravings may be initiated by the malabsorption,
possibly resulting in overeating and all attendant complications of obesity.
The doctor might recommend diet and exercise weight reduction rather than an
investigation of the cause of the weight gain.
A
Hydrolyzed Vegetable protein is a protein obtained from various foods (like
soybeans, corn or wheat) and broken down into amino acids by a chemical process
called acid hydrolysis. Hydrolyzed plant or vegetable protein is used as a
flavor enhancer in numerous processed foods like soups, chilis, sauces, stews
and some meat products like frankfurters. The whole point of these additives is
to spoof the nervous system into thinking that the processed food is high in
protein on a habit-forming manner. Some
hydrolyzed vegetable proteins act directly on nerves and some like MSG actually
kill nerves in high quantities.
Normally,
the body’s digestion does its own job of breaking proteins down into
water-soluble amines, which the body then absorbs and recombines into new
proteins. Eating Hydrolyzed Proteins
presents some foreign proteins to the body in a whole water-soluble form that
the body is not generally prepared to manage.
If these foreign proteins enter the body, say, over an intestine perforated
by the gliadin reaction, then these foreign proteins can interfere with body
chemistry in many ways.
Furthermore,
when Hydrolyzed Vegetable Protein is made from wheat (sometimes without
notification to the consumer), this converts the gliadin
into its most toxic water-soluble form.
Hey, Calontir!
[1] “Cereal Grains: Humanity’s Double-Edged Sword”, Loren Cordain, Simopoulos AP (ed): Evolutionary Aspects of Nutrition and Health, Series: World Review of Nutrition and Dietetics, Basel, Karger, 1999, vol 84, pp 19–73.
[2] “False Negative Serological Results Increase with Less Severe Villous Atrophy”
Digestive Disease and Science, 2004 Apr;49(4):546-50. (Found on Celiac.com)
[3] “Early Diagnosis Of Gluten Sensitivity: Before the Villi are Gone” Transcript of a talk given by Kenneth Fine, M.D. to the Greater Louisville Celiac Sprue Support Group, June 2003.