Decreased contraction of glycated collagen lattices coincides with impaired matrix metalloproteinase production

被引：57

作者：

Rittié, L ^{[1
]}

Berton, A ^{[1
]}

Monboisse, JC ^{[1
]}

Hornebeck, W ^{[1
]}

Gillery, P ^{[1
]}

机构：

[1] Univ Reims, Fac Med, IFR 53 Biomol, CNRS UPRESA 6021,Lab Biochem & Mol Biol, F-51095 Reims, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 264卷 / 02期

关键词：

D O I：

10.1006/bbrc.1999.1519

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：

Nonenzymatic glycation of extracellular matrix (ECM) proteins is increased in diabetes mellitus and aging and triggers cellular events leading to an imbalance in ECM homeostasis. We studied the influence of collagen glycation on matrix metalloproteinase production by dermal fibroblasts using the model of lattice cultures. Contraction of glycated collagen lattices was strongly reduced when compared to controls. Meanwhile, fibroblasts synthesized lower amounts of interstitial collagenase (MMP-1). Gelatinase A (MMP-2) production was not modified, but its activation was strongly inhibited. These effects were independent from the intensity of lattice contraction and from any simultaneous modification of tissue inhibitors of metalloproteinase (TLMP-1 and 2) production. These results demonstrate that the impaired ability of fibroblasts to remodel and contract a glycated extracellular matrix coincides with a decrease in MMP production. (C) 1999 Academic Press.

引用

页码：488 / 492

页数：5

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