GP-3, a newly characterized glycoprotein on the inner surface of the zymogen granule membrane, undergoes regulated secretion.

摘要: We have recently reported the cloning of rat zymogen granule membrane glycoprotein GP-3 and related pancreatic secretory lipase (Wishart, M. J., Andrews, P. C., Nichols, R., Blevins, G. T., Logsdon, C.D., Williams, J. A. (1993) Biol. Chem. 268, 10303-10311). Specific antipeptide antibodies were generated against both used for biochemical physiological characterization GP-3. Western blotting confirmed that was found exclusively in membranes absent from content which contains majority lipase. Extraction with Triton X-114 showed to be significantly more hydrophobic than The amino acid sequence one potential N-linked glycosylation site at Asn-336. loss concanavalin A labeling after chemical deglycosylation trifluoromethanesulfonic enzymatic N-glycanase possess a small oligosaccharide side chain. Digestion intact permeabilized granules nonspecific protease Pronase localized inner surface membranes. Since is resident on membrane, it should appear outer cellular exocytosis. Although attachment resistant treatment phosphatidylinositol-specific phospholipase C, we observed released into juice secretion greatly enhanced by cholecystokinin.