CHANGES IN BINDING-ACTIVITY OF LUTEINIZING-HORMONE RECEPTORS BY SITE DIRECTED MUTAGENESIS OF POTENTIAL GLYCOSYLATION SITES

被引：35

作者：

ZHANG, R ^{[1
]}

TSAIMORRIS, CH ^{[1
]}

KITAMURA, M ^{[1
]}

BUCZKO, E ^{[1
]}

DUFAU, ML ^{[1
]}

机构：

[1] NICHHD,ENDOCRINOL & REPROD RES BRANCH,MOLEC ENDOCRINOL SECT,BETHESDA,MD 20892

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 181卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91261-A

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：

Site directed mutagenesis of the rat ovarian luteinizing hormone (LH) receptor cDNA was performed at each of the six potential N-linked glycosylation sites to determine the effect of putative carbohydrate chains on the activity of the membrane receptor. The conversion of Asn173 to Gln resulted in the total loss of hormone binding to the surface of the transfected cell. Mutant receptors synthesized with substitutions at the remaining potential N-linked glycosylation positions of 77, 152, 269, 277 and 291 revealed no significant change in the hormone affinity. However Asn77Gln and Asn152Gln exhibited significant decreases (∼ 80%) in the number of high affinity hormone binding sites. The changes in hormone binding activity upon elimination of the potential glycosylation sites at 77, 152 and 173 indicate the presence of functional carbohydrate chains at these positions in the rat ovarian LH hCG receptor. © 1991.

引用

页码：804 / 808

页数：5

共 17 条

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