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

Abstract：

: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 (TIMP-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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Rittié L,Berton A,Monboisse JC,Hornebeck W,Gillery P

doi

10.1006/bbrc.1999.1519

subject

Has Abstract

pub_date

1999-10-22 00:00:00

pages

488-92

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91519-X

journal_volume

264

pub_type

杂志文章

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