GLYCOSYLATION-DEPENDENT BINDING OF PANCREATIC TYPE-I PHOSPHOLIPASE A(2) TO ITS SPECIFIC RECEPTOR

被引:13
作者
FUJITA, H [1 ]
KAWAMOTO, K [1 ]
HANASAKI, K [1 ]
ARITA, H [1 ]
机构
[1] SHIONOGI & CO LTD,SHIONOGI RES LABS,FUKUSHIMA KU,OSAKA 553,JAPAN
关键词
D O I
10.1006/bbrc.1995.1502
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:293 / 299
页数:7
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