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Glycosylation-dependent binding of pancreatic type I phospholipase A2 to its specific receptor
H Fujita1, K Kawamoto, K Hanasaki
1Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Biochemical and Biophysical Research Communications
|April 6, 1995
Abstract:
Pancreatic group I phospholipase A2 (PLA2-I) elicits various biological responses via its specific receptor. The PLA2-I binding to its recombinant soluble receptor was considerably reduced after Peptide: N-glycosidase F treatment of the receptor. In cultured bovine smooth muscle cells, treatment with tunicamycin, a N-glycosylation inhibitor, resulted in a decrease in the number of PLA2-I receptor. In addition, the PLA2-I binding was blocked by the addition of a lectin, Wheat germ agglutinin. These results suggest an involvement of N-linked oligosaccharides of the PLA2-I receptor for its ligand recognition.