response, as it does for a significant portion of the
population. Gliadin, one of the main proteins in gluten,
looks a lot like a microbe to our immune cells. When it is
present in the gut, our immune system sends out antibodies
in a manhunt for antigens—physical attributes that our
stadium security guards are trained to look out for. The
problem is, antigens on foreign substances (like gliadin) can
look uncomfortably similar to the markings on our own
cells. This is called molecular mimicry and may be an
attempt by pathogens to better fit into the host environment
—because even pathogens have a drive to survive! This
means that when the body’s immune system creates
antibodies to fight antigens, our own tissues can fall under
friendly fire.
This can often occur to a family of enzymes called
transglutaminases. Present throughout the body,
transglutaminases are important for keeping us healthy, and
their dysfunction has been implicated in Alzheimer’s
disease, Parkinson’s disease, and ALS.^15 They’re also found
in particularly high concentration in the thyroid, which gets
attacked in autoimmune thyroid conditions such as
Hashimoto’s disease and Graves’ disease. Unfortunately,
transglutaminase enzymes have molecular markings very
similar to gliadin antigens. In a susceptible person, eating
gluten may lead the body to attack not only gliadin, but also
the transglutaminase enzymes.
While it can’t be said that gluten is the cause of a
mutinous immune system for every person, a recent study
found the prevalence of celiac disease in patients with
autoimmune thyroid disease was two- to fivefold compared