The misrecognition process of autoimmunity can begin with a bacterial protein that gets into the bloodstream, but it can also start with a grain protein. The gliadin protein and the transglutaminase enzyme of the liver or pancreas bear a strong resemblance to one another, so the presence of gliadin in the bloodstream can trick the immune system into causing autoimmune hepatitis or autoimmune pancreatitis.
This is big. This is as big as identifying and capturing the Mafia don responsible for dozens of gangland-style murders and millions of dollars of contraband, convicting him and putting him away for life. It means that we now have a direct path linking gliadin and related grain prolamin proteins with autoimmune conditions. This sequence of events is not limited to people with coeliac disease or gluten sensitivity; this applies to everyone. Susceptibility will vary based on genetic factors, but it is separate and distinct from the gastrointestinal disruption caused by coeliac disease. It means that a person with no abdominal symptoms from wheat consumption – no heartburn, bowel urgency, colitis, etc. – and who tests negative for coeliac disease or gluten sensitivity can still develop the joint deformity of rheumatoid arthritis years later or the neurological impairment of multiple sclerosis at the age of 45.
Prolamins and Transglutaminase: Dead Ringers
Remember the 1964 Bette Davis film Dead Ringer, in which one sister, Edith, estranged and angered with her twin, Margaret, shoots her in the head and then covers up her crime by assuming the killed twin’s identity? I don’t think any better allegorical description for autoimmunity could be crafted, right down to Ms Davis’s talent for portraying unpopular characters.
The human body relies on a class of enzymes called transglutaminases, which are found in the intestinal lining, pancreas, joints, brain, skin and other organs. Transglutaminase enzymes are responsible for the simple task of removing a nitrogen-containing (amine) group from the amino acid glutamine in the proteins that you consume. In an odd twist of fate, human transglutaminase enzymes resemble the gliadin protein of wheat, as well as the related prolamin proteins of rye, barley, corn and oats. In other words, if their structures are laid out side-by-side, there is an eerie overlap in sequence among all of them, such that the body’s immune response can’t tell the difference: they are immune dead ringers.1 This has been called ‘molecular mimicry’: two unrelated and different proteins with different purposes, but with sections of shared structure that fool the immune system.
Antibodies expressed against grain prolamins – and thereby against transglutaminase – are associated with inflammatory bowel diseases, pancreatitis, joint and muscle inflammation, skin rashes and other autoimmune and inflammatory conditions.2 This explains how and why grain consumption causes so many autoimmune and inflammatory diseases other than coeliac disease. For example, children with type 1 diabetes (an autoimmune condition of the pancreas) are more likely to express antibodies against the transglutaminase enzyme, also associated with increased potential for autoimmune conditions outside of the pancreas.3
It is as unsettling as one twin shooting the other, this relationship between something plant and something human that’s close enough to fool even the finely tuned discriminating powers of the human immune system. But such is the unnatural relationship between humans and the seeds of grasses.
Even before the details of increased intestinal permeability were sorted out by Dr Fasano’s team, it had been known for many years that the list of autoimmune conditions attributable to wheat, rye and barley is formidable. These dangerous and sometimes fatal conditions are enough to make you spit out your last bite of raisin bread.
Addison’s disease
Alopecia areata
Ankylosing spondylitis
Antiphospholipid antibody syndrome
Autoimmune haemolytic anaemia
Autoimmune hepatitis
Autoimmune inner ear disease
Autoimmune lymphoproliferative syndrome
Autoimmune thrombocytopaenic purpura
Behçet’s disease
Bullous pemphigoid
Cardiomyopathy (dilated, or congestive)
Chronic fatigue syndrome
Chronic inflammatory demyelinating polyneuropathy
Coeliac disease
Cold agglutinin disease
CREST syndrome
Crohn’s disease
Dermatomyositis
Discoid lupus
Essential mixed cryoglobulinaemia
Food protein-induced enterocolitis syndrome
Graves’ disease
Guillain–Barré syndrome
Hashimoto’s thyroiditis
Idiopathic pulmonary fibrosis
Idiopathic thrombocytopaenic purpura
IgA nephropathy
Insulin-dependent diabetes (type I)
Juvenile arthritis
Ménière’s disease
Mixed connective tissue disease
Multiple sclerosis
Myasthaenia gravis
Myocarditis
Pemphigus vulgaris
Pernicious anaemia
Polyarteritis nodosa
Polychondritis
Polyglandular syndromes
Polymyalgia rheumatica
Polymyositis dermatomyositis
Primary agammaglobulinaemia
Primary biliary cirrhosis
Psoriasis
Raynaud’s syndrome
Reiter’s syndrome
Rheumatoid arthritis
Sarcoidosis
Scleroderma
Sjögren’s syndrome
Systemic lupus erythematosus
Takayasu’s arteritis
Temporal arteritis
Ulcerative colitis
Uveitis
Vasculitis
Vitiligo
Wegener’s
