Advanced glycation end products inhibit production and activity of matrix metalloproteinase-2 in human umbilical vein endothelial cells

J Int Med Res. 2007 Sep-Oct;35(5):709-15. doi: 10.1177/147323000703500517.

Abstract

The aim of this study was to investigate the effects of advanced glycation end products (AGEs) on the expression and activity of matrix metalloproteinases-2 (MMP-2) in human umbilical vein endothelial cells (HUVECs). Cultured HUVECs were incubated with various concentrations of AGEs-modified albumin or unmodified albumin for different time periods. Protein and gene expression of MMP-2 and the receptor for AGEs (RAGE) were measured by Western blot and reverse transcription-polymerase chain reaction, respectively. The activity of MMP-2 in the conditioned medium was measured by gelatin zymography. The AGE-modified albumin inhibited MMP-2 but increased RAGE protein and gene expression in HUVECs in a concentration- and time-dependent manner. An inhibition of MMP-2 activity was also detected in the conditioned medium of HUVECs incubated with AGEs-modified albumin. In conclusion, AGEs inhibited the expression and activity of MMP-2 in HUVECs; this may be mediated through upregulation of RAGE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cells, Cultured
  • Culture Media, Conditioned
  • DNA Primers
  • Endothelium, Vascular / cytology
  • Endothelium, Vascular / enzymology*
  • Endothelium, Vascular / metabolism
  • Enzyme Induction
  • Glycation End Products, Advanced / blood*
  • Humans
  • Matrix Metalloproteinase 2 / biosynthesis*
  • Matrix Metalloproteinase 2 / genetics
  • Matrix Metalloproteinase 2 / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction

Substances

  • Culture Media, Conditioned
  • DNA Primers
  • Glycation End Products, Advanced
  • Matrix Metalloproteinase 2