Kaneko M, Mimuro J, Matsuda M, Sakata Y
Institute of Hematology, Jichi Medical School, Tochigi-Ken, Japan.
Biochem Biophys Res Commun. 1991 Aug 15;178(3):1160-6. doi: 10.1016/0006-291x(91)91014-4.
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.
我们已经表明，含有天冬酰胺-精氨酸-精氨酸-亮氨酸氨基酸序列的合成肽，该序列源自组织型纤溶酶原激活剂（tPA）kringle-2结构域内环的氨基酸序列，通过与纤溶酶原激活剂抑制剂-1（PAI-1）结合，抑制双链tPA与PAI-1之间的复合物形成。这种结合是可逆的，不仅受到tPA的抑制，而且还受到无酶活性的tPA的抑制。对PAI-1与含有天冬酰胺-精氨酸-精氨酸-亮氨酸序列的肽之间相互作用的定量分析表明，kringle-2结构域内环中的PAI-1结合位点残基，并且在双链tPA中优先表达。
