Synthetic peptides derived from the sequence around the plasmin cleavage site in vitronectin. Use in mapping the PAI-1 binding site.
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.
Gechtman
Z
Z
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Sharma
R
R
Kreizman
T
T
Fridkin
M
M
Shaltiel
S
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D005341:Fibrinolysin / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000378:metabolism; D010449:Peptide Mapping; D017395:Plasminogen Activator Inhibitor 1 / Q000378:metabolism*; D019096:Vitronectin
D006023:Glycoproteins; D010446:Peptide Fragments; D017395:Plasminogen Activator Inhibitor 1; D019096:Vitronectin; D005341:Fibrinolysin