Glycosylation-dependent binding of pancreatic type I phospholipase A2 to its specific receptor.

Pancreatic group I phospholipase A(2) (PLA(2)-I) elicits various biological responses via its specific receptor. The PLA(2)-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 PLA(2)-I receptor. In addition, the PLA(2)-I binding was blocked by the addition of a lectin, Wheat germ agglutinin. These results suggest an involvement of N-linked oligosaccharides of the PLA(2)-I receptor for its ligand recognition. (C) 1995 Academic Press, Inc.