Gliadin binding to rat and human enterocytes.
Binding of 125I-crude gluten digest (Frazer's fraction III. FF-III) and 125I-concanavalin A (Con A) to isolated rat enterocytes and of 125I-FF-III to human enterocytes was investigated. Specific binding of 125I-FF-III to rat enterocytes was observed but binding was not inhibited by any of a range of simple and complex saccharides. although casein and bovine serum albumin displaced FF-III at high concentrations. Con A also bound to enterocytes in a specific manner and was inhibited by alpha-methyl-D-mannoside, confirming a lectin-mediated interaction. 125I-FF-III exhibited quantitatively similar specific binding to both normal human and coeliac enterocytes. The primary interaction of gliadin peptides with the enterocyte surface membrane is not lectin-mediated and unlikely to be of fundamental importance in the pathogenesis of coeliac disease.
D000818:Animals; D002446:Celiac Disease / Q000378:metabolism* / Q000473:pathology; D002462:Cell Membrane / Q000378:metabolism; D003208:Concanavalin A / Q000378:metabolism; D005903:Gliadin / Q000378:metabolism*; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism* / Q000473:pathology; D008297:Male; D010940:Plant Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D010940:Plant Proteins; D003208:Concanavalin A; D005903:Gliadin