Cyclic strain-mediated regulation of endothelial matrix metalloproteinase-2 expression and activity

Cardiovasc Res. 2004 Sep 1;63(4):625-34. doi: 10.1016/j.cardiores.2004.05.008.

Abstract

Objective: To investigate the role of cyclic strain in controlling matrix metalloproteinase-2 (MMP-2) expression and activity in endothelial cells (ECs) in vitro.

Methods: A Flexercell Tension Plus FX-4000T system was used to apply a physiological level of equibiaxial cyclic strain (0-10% strain, 60 cycles/min, 0-24 h, cardiac waveform) to bovine aortic endothelial cells (BAECs). Cells and conditioned media were harvested for analysis of MMP-2/9 expression and activity (pro and active) using reverse-transcriptase polymerase chain reaction (RT-PCR), Western blotting and zymography techniques.

Results: Cyclic strain significantly increased MMP-2 expression and activity force- and time-dependently. Pretreatment with Gialpha-protein inhibitors, pertussis toxin (PTX) and NF023, transient expression of inhibitory mutants of Gialpha-subunits, or pretreatment with RGD peptides to block RGD-dependent integrin signaling failed to attenuate strain-induced increases in MMP-2 expression in BAECs. In contrast, inhibition of Gbetagamma-signaling with betaArk-ct or tyrosine kinase blockade with genistein reduced strain-induced MMP-2 expression while concomitantly inhibiting strain-induced p38 and ERK activity in these cells. Pretreatment with PD169316 and PD98059 to selectively inhibit p38 and ERK activity, respectively, also resulted in a significant inhibition of the strain-induced MMP-2 response. Finally, inhibition of the adaptor protein, Shc, (via Shc-SH2 transfection) resulted in a significant decrease in strain-induced MMP-2 activity concomitant with a reduction in ERK activity in BAECs.

Conclusion: Cyclic strain stimulates MMP-2 expression, in part, by stimulating both p38- and ERK-dependent pathways through activation of Gbetagamma and tyrosine kinase in BAECs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Aorta
  • Cattle
  • Cells, Cultured
  • Endothelial Cells / enzymology*
  • Endothelium, Vascular / enzymology*
  • GTP-Binding Proteins / metabolism
  • Glyceraldehyde-3-Phosphate Dehydrogenases / genetics
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
  • Matrix Metalloproteinase 2 / genetics
  • Matrix Metalloproteinase 2 / metabolism*
  • Mitogen-Activated Protein Kinases / metabolism
  • Pulsatile Flow
  • Reverse Transcriptase Polymerase Chain Reaction
  • Stress, Mechanical
  • p38 Mitogen-Activated Protein Kinases

Substances

  • Glyceraldehyde-3-Phosphate Dehydrogenases
  • Mitogen-Activated Protein Kinases
  • p38 Mitogen-Activated Protein Kinases
  • Matrix Metalloproteinase 2
  • GTP-Binding Proteins