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

FEBS Letters

Trueb, Beat¹  Zumbrunn, Jürg¹ 

[1] M.E. Müller-Institut für Biomechanik, Universität Bern, Postfach 30, CH-3010 Bern, Switzerland

关键词: Insulin-like growth factor;    Insulin-like growth factor binding protein;    Serine protease;    Subtractive cDNA cloning;    Transformation-sensitive protein;    Human fibroblast;    DFP;    diisopropul fluorophosphate;    IGF;    insulin-like growth factor;    IGFBP;    insulin-like growth factor binding protein;    RACE;    rapid amplification of cDNA ends;   

DOI  :  10.1016/S0014-5793(96)01229-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown