In my last post, we explored What is Gluten? And while we got pretty in-depth in describing the whole beast (complete with an infographic!), I hope that most of you got the take-away points from it. And that is, today, when we test for gluten in our foods, we are testing for only a tiny fraction of the gluten compound (alpha-gliadin), so if any other fraction of gluten exists in that food, we probably won’t find it.
This is true when testing for celiac disease, too. Most tests that doctors use look for antibodies to alpha-gliadin, and this is what they base their diagnosis of celiac disease on. But what if you react to other fractions of gluten? Alpha-gliadin is only one component of the gliadin portion of gluten. What if you react to beta-gliadin or some other gliadin portion? There is even evidence that people can react to the glutenin portion of gluten as well. The other half of gluten. The one that no tests are looking for.
That’s just a quick recap of the What is Gluten article. But we’re not done yet. There’s even more to the story of wheat and gluten.
Why Dicke, et al. ever decided that we have to isolate the one portion of wheat that was causing celiacs trouble, is mysterious. His pursuits probably were in the best interest of his patients and medicine at-large. He was presumably looking for a way to make a “gluten-free” diet less inconvenient to mothers of the era, since grains were (and still are) a major part of the diet and cheap to come by.
But it turns out that gluten (including gliadin AND glutenin) may not be the only portion of wheat that is problematic. The same study that found antibody reactions to the glutenin portion of gluten (which we aren’t testing for, remember), also found antibody reactions to albumins and globulins, the non-gluten portion of wheat flour!  In addition, several studies have shown that wheat starch (which some countries allow on a gluten-free diet) may also affect celiacs and the gluten sensitive. , #gluten may not be the only portion of #wheat that is problematic. #glutenfree #grainfree Click To Tweet
Here is the infographic again, in case I’ve started to lose you with the taxonomy:
Not only that, the germ portion of the wheat grain contains a lectin called Wheat Germ Agglutinate (WGA), which has its own set of problems. This is the portion of the wheat that becomes a new plant, if the wheat seed is planted. It is found in “whole grain” bread (together with the bran and flour). Wheat germ is also sold as a nutritional supplement that people often sprinkle on their morning cereal for an added nutritional boost. This is the part that is supposedly separated out from gluten, in the washing process. It is the true seed of the wheat plant, which has been very well designed to stand up against predation in the interest of species preservation.
The problem is, one study found traces of WGA in gluten , showing that separating wheat into its different components, is not as simple as industry would have us believe, just as “wheat starch sometimes contains residual levels of detectable gluten even though most of the wheat protein has been removed during manufacturing.” 
But even more important, some studies have found antibodies to WGA in celiac patients , surmising that in fact perhaps “WGA may [actually] be involved in the pathogenesis of CD.” So if albumins, globulins and WGA are also causing problems in celiacs, why are we spending so much time on trying to go gluten-free?
Again, we are missing the forest for the trees. We need to take a step back and look at wheat in general.
First, what is a lectin, anyway? Lectins are a specific class of proteins found in many foods that have the ability to clump together red blood cells or bind to bodily organs like “super glue.”  This process is called agglutination. It’s the same process that antibodies undertake with red blood cells when they find a foreign invader in the blood. They clump the “bad” blood together and send it on its way, to be later either neutralized or destroyed by white blood cells.
Food lectins (or dietary lectins) not only can agglutinate blood, but they can also bind with bodily organs such as the lining of the stomach or the intestinal tract. Peter D’Adamo offers a simple explanation of how the process works:
Once the intact lectin protein settles someplace in your body, it literally has a magnetic effect on the cells in that region. It clumps the cells together and they are targeted for destruction, as if they, too, were foreign invaders. This clumping can cause irritable bowel syndrome in the intestines or cirrhosis in the liver, or block the flow of blood through the kidneys – to name just a few of the effects.
Just to be clear, lectins are not just inert proteins that we have a hard time ingesting. They are actively engaging (usually in a bad way) with our body! I find this amazing. Lectins seem to have an agenda of their own. They are so alive that WGA has actually been found to be still “biologically active in human feces!” 
While “different lectins target different organ and body systems,” WGA is the most studied of the cereal grains, and as Loren Cordain says, its effects “upon tissues and organs are astonishingly widespread,” affecting “virtually every cell in the body” including the “alimentary tract (mouth, stomach, intestines), pancreas, musculoskeletal system, kidney, skin, nervous and myelin tissues, reproductive organs, and platelets and plasma proteins.” 
So just what is WGA capable of doing to our bodies?
Sayer Ji does a great job of summarizing (and citing) the astounding documented effects of WGA in his article, Opening Pandora’s Bread Box: The Critical Role of Wheat Lectin in Human Disease. To name a few: inflammation, anti-nutritive effects, autoimmunity, endocrine disruption (with a “particular affinity for thyroid tissue”), neurotoxicity and decreased gastrointestinal function.
Additionally troubling is the fact that WGA has been shown to “increase intestinal permeability and activate the immune system.”  Some studies have shown that “WGA causes some damage to the small intestine of rats,” and that WGA can cross the intestinal wall and enter the blood stream. We all know what intestinal permeability (leaky gut) can do to us.
So it might be an understatement, when Cordain says “the potential for this lectin to disrupt human health is high.” 
I’m pretty sure I’m not going out on a limb when I say: wheat in any form is not good for us! So why are we digging so deep into the anatomy of gluten and trying desperately to separate such fractions out of wheat? Is it because no one wants to believe that we need to give up all of wheat, the so-called “staff of life,” forever?
Why are we hellbent on calling it a gluten-free diet, when there is so much more of the wheat grain that affects us? Why don’t we just call it a wheat-free diet?
Well obviously, by doing that, we are neglecting to include the other “gluten” grains that Dicke observed were also causing reactions in his patients. Even if it’s just anecdotally, we do know that barley, rye and oats are also problematic for celiacs and the gluten sensitive. So why not just call it a grain-free diet, then? Forget the lectins, the globulins and albumins, the gliadin-fractions and other grain prolamins, and all those other amino-acid sequences. For just a minute. Why don’t we just call it a grain-free diet?
Well…. that does make some sense. But do we know if all grains are bad? While it’s not yet clear the extent to which other grains affect us, it is clear that:
b) Lectin activity has also been demonstrated in rye, barley, oats, corn, and rice. 
c) People DO heal on a grain free diet. We know this not only from anecdotal stories of people who have healed on a Paleo diet, but actual clinical evidence as well.
Whether this is because our inherently gluten-free grains are cross-contaminated with gluten (or albumins or globulins or WGA or WTF-other-amino-acid-sequence they want to look for); or because other grains may end up being as problematic as wheat, we can’t yet say for sure. More research needs to be done.
But in the meantime, if you’ve gone gluten-free and you’re still not feeling better, you may need to go beyond gluten-free. Going completely wheat-free is a no-brainer. Going completely grain-free can’t hurt either.
 M Kieffer, P Frazier, N Daniels and R Coombs. Wheat Gliadin Fractions And Other Cereal Antigens Reactive With Antibodies In The Sera Of Coeliac Patients. Clin. Exp. Immunol. (1982) 50, 651-660.
 K HOZYASz. European “gluten-free” solid foods for infants may be a risky food for celiacs. Journal of the American Dietetic Association – May 2002 (Vol. 102, Issue 5, Page 637.
 L Chartrand , P Russo, A Duhaime, E Seidman. Wheat starch intolerance in patients with celiac disease. Journal of American Dietetic Associaton. 1997 Jun;97(6):612-8.
 J Kolberg, L Sollid. Lectin activity of gluten identified as wheat germ agglutinin. Biochem Biophys Res Commun. 1985 Jul 31;130(2):867-72.
 S. L. Taylor, Ph.D., and J. L. Baumert, Achieving Gluten-Free Status Ph.D. Food Safety Magazine. December 2013/January 2014.
 K. Fälth-Magnusson, K.-E. Magnusson. Elevated levels of serum antibodies to the lectin wheat germ agglutinin in celiac children lend support to the gluten-lectin theory of celiac disease.ediatric Allergy and Immunology. Volume 6, Issue 2, pages 98–102, May 1995.
 L. M. Sollid, J. Kolberg,* H. Scott, J. Ekt 0. Fausai & P. Brandtzaeg. Antibodies to wheat germ agglutinin in coeliac disease. Clin. exp. Immunol. (1986) 63, 95-100.
 P D’Adamo. Eat Right 4 Your Type: The Individualized Diet Solution to Staying Healthy, Living Longer & Achieving Your Ideal Weight. G.T. Putnam’s & Sons. New York. 1996. p.23.
 L Cordain. Cereal Grains: Humanity’s Double-Edged Sword. Simopoulos Ap (Ed): Evolutionary Aspects Of Nutrition And Health. Diet, Exercise, Genetics And Chronic Disease. World Rev Nutr Diet. Basel, Karger, 1999, Vol 84, P.46.
 L Cordain. 1999. P.45.
 K. de Punder and L. Pruimboom. The Dietary Intake of Wheat and other Cereal Grains and Their Role in Inflammation. Nutrients 2013, 5, 771-787
 A. Pusztai, S. W. B. Ewen, G. Grant, D. S. Brown, J. C. Stewart, W. J. Peumans, E. J. M. Van Damme And S. Bardocz. Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins. British Journal of Nutrition (1993), 70, 31 3-32.
 L Cordain. 1999. P.47
 Intestinal Damage from Celiac Disease Persists in Adults, Even with Gluten-free Diet. National Institute of Diabetes and Digestive and Kidney Diseases. September 2011. http://celiac.nih.gov/TissueDamage.aspx
 Lanzini A, Lanzarotto F, Villanacci V, Mora A, Bertolazzi S, Turini D, Carella G, Malagoli A, Ferrante G, Cesana BM, Ricci C. Complete recovery of intestinal mucosa occurs very rarely in adult coeliac patients despite adherence to gluten-free diet. Aliment Pharmacol Ther. 2009 Jun 15;29(12):1299-308.
 L Cordain. 1999. P.52.
 Hollon J, Cureton P, Martin M, Puppa E and Fasano, A. Trace gluten contamination may play a role in mucosal and clinical recovery in a subgroup of diet-adherent non-responsive celiac disease patients. BMC Gastroenterology 2013, 13:40