Synthetic peptides derived from the sequence around the plasmin cleavage site in vitronectin

FEBS Letters

Kreizman, Tamar¹  Gechtman, Zeev¹  Shaltiel, Shmuel¹  Fridkin, Mati²  Sharma, Raman¹ 

[1] Departments of Chemical Immunology, The Weizmann Institute of Science, Rehovot, 76100, Israel;Departments of Organic Chemistry, The Weizmann Institute of Science, Rehovot, 76100, Israel

关键词: PAI-1;    Peptides;    Plasmin;    Vitronectin;    BP;    basic peptide (for the amino acid sequence of individual peptides see Scheme 1);    ECM;    extracellular matrix;    ELISA;    enzyme-linked immunosorbent assay;    ONPG;    ortho-nitrophenyl-β-Dgalactopyranoside;    PAI-1;    plasminogen activator inhibitor - 1;    tPA;    tissue plasminogen activator;    Vn;    vitronectin.;   

DOI  :  10.1016/0014-5793(93)81181-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A series of 8 peptides derived from the amino acid sequence accommodating the plasmin cleavage site in vitronectin were synthesized and used to map its binding site for the type I plasminogen activator inhibitor (PAI-1). This mapping assigned the inhibitor binding site to the K³⁴⁸-R³⁷⁰ region with high affinity recognition elements within the K³⁴⁸-R³⁵⁷ sequence. These results account for our previous finding that cleavage of the R³⁶¹ -S³⁶² bond by plasmin significantly reduces the affinity between PAI-1 and vitronectin, since it splits the PAI-1 binding site in two. Furthermore, in the case of the two-chain form of vitronectin, this cleavage detaches the S³⁶²-R³⁷⁹ peptide which provides some of the affinity elements for the binding of PAI-1.

【 授权许可】

Unknown