THE INTESTINAL-MUCOSA OF CELIACS IN REMISSION IS UNABLE TO ABOLISH THE AGGLUTINATING ACTIVITY OF GLIADIN PEPTIDES ON K562(S) CELLS

The peptic-tryptic-cotazym digest of a wheat gliadin was fractionated into ten primary fractions. Subfraction 2R of fraction 9 is known to b e toxic to patients with coeliac disease. Fraction 9 and subfraction 2 R also agglutinate H562(S) cells, previously shown to be a good indica tion of toxicity to in vitro intestinal bioptic specimens from coeliac patients. Subfraction 2R was still able to agglutinate K562(S) cells after digestion by morphologically normal small intestinal mucosa of c oeliacs in remission, but was inactivated after digestion by normal mu cosa. These results are consistent with the hypothesis that there is a mucosal defect in handling gliadin peptides in coeliac patients, and suggest that there is either a primary (or secondary) enzyme deficienc y, or some other mechanism, operating in the intestinal mucosa of coel iac patients in remission.