The plasminogen activator inhibitor-1 binding site in the kringle-2 domain of tissue-type plasminogen activator.
We have shown that synthetic peptides containing the amino acid sequence Asn-Arg-Arg-Leu, derived from the amino acid sequence of the inner loop of the kringle-2 domain of tissue-type plasminogen activator (tPA), inhibited complex formation between two chain tPA and plasminogen activator inhibitor-1 (PAI-1) by binding to PAI-1. This binding was reversible and was inhibited by not only tPA but also by enzymatically inactive tPA. Quantitative analyses of the interaction of PAI-1 with the peptide containing the Asn-Arg-Arg-Leu sequence indicated that the PAI-1 binding site residues in the inner loop of the kringle-2 domain and is preferentially expressed in two chain tPA.
Kaneko
M
M
Institute of Hematology, Jichi Medical School, Tochigi-Ken, Japan.
Mimuro
J
J
Matsuda
M
M
Sakata
Y
Y
D000595:Amino Acid Sequence; D001665:Binding Sites; D001667:Binding, Competitive; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism; D015849:Plasminogen Inactivators / Q000378:metabolism*; D010959:Tissue Plasminogen Activator / Q000138:chemical synthesis / Q000378:metabolism*
D010455:Peptides; D015849:Plasminogen Inactivators; D010959:Tissue Plasminogen Activator