Primary structure of a putative serine protease specific for IGF-binding proteins

被引：180

作者：

Zumbrunn, J ^{[1
]}

Trueb, B ^{[1
]}

机构：

[1] UNIV BERN,ME MULLER INST BIOMECH,CH-3010 BERN,SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 398卷 / 2-3期

关键词：

insulin-like growth factor; insulin-like growth factor binding protein; serine protease; subtractive cDNA cloning; transformation-sensitive protein; human fibroblast;

D O I：

10.1016/S0014-5793(96)01229-X

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：

From a subtracted cDNA library we have isolated a cDNA clone coding for a novel transformation-sensitive protein which is expressed by human fibroblasts, but not by their matched SV40 transformed counterparts, This protein has a molecular mass of 51 kDa and is highly related to the HtrA family of serine proteases from bacteria, At the N-terminal end, it contains an IGF-binding domain which may modulate the activity of the associated serine protease, Our data are consistent with the assumption that the novel protein represents one of the proteases that regulate the availability of IGFs by cleaving IGF-binding proteins.

引用

页码：187 / 192

页数：6

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