IMMUNOLOGICAL AND PARTIAL SEQUENCE IDENTITY OF MOUSE BM180 WITH WHEATALPHA-GLIADIN

BM180, a novel 180-kDa basement membrane protein enriched in guanidine -HCl extracts of lacrimal and parotid exocrine secretory glands, was i mmunopurified using the secretion inhibitory monoclonal antibody 3E12. The N-terminal amino acid sequence was found to be VRVPVPQLQPQNP. An identical sequence comprises the N-terminus of the wheat storage prote in alpha-gliadin. The presence of a gliadin-like protein in basement m embranes was confirmed using a monoclonal and several polyclonal anti- gliadin antibodies, the former of which detected a 180-kDa protein in basement membrane blots. A full-length alpha-gliadin cDNA was found to hybridize at high stringency with mouse and human genomic DNA; and in lacrimal gland Northern blots with a 2.3-kb message. Since BM180 appe ars to be required for stimulus-secretion coupling by lacrimal acinar cells, circulating anti-alpha-gliadin antibodies associated with Sjogr en's syndrome ('Dry Eye') and more commonly in Coeliac disease, may be secretion inhibitory. (C) 1995 Academic Press. Inc.