Progelatinase B forms from human neutrophils. Complex formation of monomer/lipocalin with TIMP-1

被引：38

作者：

Kolkenbrock, H ^{[1
]}

HeckerKia, A ^{[1
]}

Orgel, D ^{[1
]}

Kinawi, A ^{[1
]}

Ulbrich, N ^{[1
]}

机构：

[1] FREE UNIV BERLIN,INST PHARM,D-14195 BERLIN,GERMANY

来源：

BIOLOGICAL CHEMISTRY | 1996年 / 377卷 / 7-8期

关键词：

progelatinase B; lipocalin complex; TIMP-1;

D O I：

10.1515/bchm3.1996.377.7-8.529

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：

The three forms of neutrophil gelatinase B - monomer, homodimer and monomer/lipocalin complex -, were isolated from phorbolester stimulated neutrophil granulocytes by chromatography on gelatin-Sepharose and heparin-Ultrogel. On average, about 50% of the monomer/lipocalin complex was found to be complexed with TIMP-1. After activation with trypsin monomer, homodimer and monomer/lipocalin complex displayed a specific activity of about 2000 mU/mg towards the substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg, whereas the monomer/lipocalin/TIMP-1 complex could be activated to a specific activity of only 200 mU/mg. The ternary monomer/lipocalin/TMP-1 complex behaves like the progelatinase A-TIMP-P complex and the progelatinase B-TIMP-1 complex in that it is an inhibitor for active metalloproteinases (MMPs) and, after activation, a gelatinase with a pronouncedly reduced activity. When the monomer/lipocalin/TIMP-1 complex inhibits an MMP, a quaternary complex monomer/lipocalin/TMP-1/MMP is generated which after activation shows a sixfold higher proteolytic activity than the active ternary complex.

引用

页码：529 / 533

页数：5

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