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Publication : Immunological and partial sequence identity of mouse BM180 with wheat alpha-gliadin.

First Author  Laurie GW Year  1995
Journal  Biochem Biophys Res Commun Volume  217
Issue  1 Pages  10-5
PubMed ID  8526896 Mgi Jnum  J:30593
Mgi Id  MGI:78092 Doi  10.1006/bbrc.1995.2738
Citation  Laurie GW, et al. (1995) Immunological and partial sequence identity of mouse BM180 with wheat alpha-gliadin. Biochem Biophys Res Commun 217(1):10-5
abstractText  BM180, a novel 180-kDa basement membrane protein enriched in guanidine-HCl extracts of lacrimal and parotid exocrine secretory glands, was immunopurified 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 protein alpha-gliadin. The presence of a gliadin-like protein in basement membranes 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 appears to be required for stimulus-secretion coupling by lacrimal acinar cells, circulating anti-alpha-gliadin antibodies associated with Sjogren's syndrome ('Dry Eye') and more commonly in Coeliac disease, may be secretion inhibitory.
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