FEBS Letters | |
Synthetic peptides derived from the sequence around the plasmin cleavage site in vitronectin | |
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
【 预 览 】
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RO201912020297346ZK.pdf | 551KB | download |