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

FEBS Lett. 2004 Apr 9;563(1-3):13-6. doi: 10.1016/S0014-5793(04)00233-9.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbamates / blood*
  • Carbamates / metabolism
  • Cell Adhesion
  • Cells, Cultured
  • Collagen Type I / isolation & purification
  • Collagen Type I / metabolism*
  • Collagen Type I / pharmacology
  • Enzyme Activation
  • Humans
  • Kinetics
  • Matrix Metalloproteinase 9 / biosynthesis*
  • Matrix Metalloproteinase 9 / drug effects
  • Matrix Metalloproteinase 9 / metabolism
  • Monocytes / cytology
  • Monocytes / drug effects
  • Monocytes / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Tissue Inhibitor of Metalloproteinase-1 / analysis

Substances

  • Carbamates
  • Collagen Type I
  • Tissue Inhibitor of Metalloproteinase-1
  • Matrix Metalloproteinase 9