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Synthetic peptides derived from the sequence around the plasmin cleavage site in vitronectin
Author(s) -
Gechtman Zeev,
Sharma Raman,
Kreizman Tamar,
Fridkin Mati,
Shaltiel Shmuel
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81181-x
Subject(s) - vitronectin , plasmin , cleavage (geology) , binding site , chemistry , peptide , peptide sequence , plasminogen activator , stereochemistry , biochemistry , biology , integrin , enzyme , receptor , genetics , paleontology , fracture (geology) , gene
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 K 348 ‐R 370 region with high affinity recognition elements within the K 348 ‐R 357 sequence. These results account for our previous finding that cleavage of the R 361 ‐S 362 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 S 362 ‐R 379 peptide which provides some of the affinity elements for the binding of PAI‐1.