THE PLASMINOGEN-ACTIVATOR INHIBITOR-1 BINDING-SITE IN THE KRINGLE-2 DOMAIN OF TISSUE-TYPE PLASMINOGEN-ACTIVATOR

被引：13

作者：

KANEKO, M ^{[1
]}

MIMURO, J ^{[1
]}

MATSUDA, M ^{[1
]}

SAKATA, Y ^{[1
]}

机构：

[1] JICHI MED SCH, INST HEMATOL, MINAMI KAWACHI, TOCHIGI 32904, JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 178卷 / 03期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0006-291X(91)91014-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 resides in the inner loop of the kringle-2 domain and is preferentially expressed in two chain tPA. © 1991.

引用

页码：1160 / 1166

页数：7

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