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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 209卷 / 01期

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

页码：293 / 299

页数：7

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