Enhanced activation of and increased production of matrix metalloproteinase‐9 by human blood monocytes upon adhering to carbamylated collagen

FEBS Letters

Garnotel, Roselyne¹  Jaisson, Stéphane¹  Sabbah, Nadia¹  Gillery, Philippe¹ 

[1] Laboratory of Biochemistry and Molecular Biology, CNRS UMR 6198, IFR 53-Biomolecules, Faculty of Medicine, University of Reims Champagne-Ardenne, 51 Rue Cognacq Jay, 51095 Reims Cedex, France

关键词: Collagen;    Monocyte;    Carbamylation;    Matrix metalloproteinase-9;    Atherosclerosis;    Tissue inhibitor of metalloproteinase-1;    ECM;    extracellular matrix;    MMP;    matrix metalloproteinase;    TIMP;    tissue inhibitor of metalloproteinase;   

DOI  :  10.1016/S0014-5793(04)00233-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Carbamylation refers to chemical modification of protein side chains by cyanate derived e.g. from urea. It alters their structural and functional properties. We have studied the influence of the carbamylation of type I collagen in vitro on its interactions with elutriated human monocytes, and its potential role in atherosclerosis. Adhesion of monocytes onto carbamylated collagen was significantly enhanced compared to native collagen. There was no change in superoxide anion production. On the other hand, there was an increase in the production and the activation of matrix metalloproteinase-9. No effect was found on tissue inhibitor of metalloproteinase-1 production. Thus, the presence of carbamylated collagen may stimulate the remodelling of extracellular matrix mediated by activated monocytes. Such alterations may contribute to enhanced atherosclerosis in renal insufficiency, a pathological condition associated with elevated levels of carbamylation.

【 授权许可】

Unknown