Glycosylation-dependent binding of pancreatic type I phospholipase A2 to its specific receptor.
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.
Fujita
H
H
Shionogi Research Laboratories, Shionogi & Co., Ltd., Osaka, Japan.
Kawamoto
K
K
Hanasaki
K
K
Arita
H
H
D000818:Animals; D001011:Aorta / Q000166:cytology / Q000378:metabolism; D002417:Cattle; D002478:Cells, Cultured; D006031:Glycosylation; D037102:Lectins / Q000378:metabolism; D009131:Muscle, Smooth, Vascular / Q000166:cytology / Q000378:metabolism; D010179:Pancreas / Q000201:enzymology*; D010741:Phospholipases A / Q000378:metabolism*; D054467:Phospholipases A2; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000378:metabolism*; D054507:Receptors, Phospholipase A2; D013379:Substrate Specificity; D014415:Tunicamycin / Q000494:pharmacology
D037102:Lectins; D011956:Receptors, Cell Surface; D054507:Receptors, Phospholipase A2; D014415:Tunicamycin; D010741:Phospholipases A; D054467:Phospholipases A2