Matrix metalloproteinase 13 mediates nitric oxide activation of endothelial cell migration

Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3685-90. doi: 10.1073/pnas.0408217102. Epub 2005 Feb 22.

Abstract

To explore the mechanisms by which NO elicits endothelial cell (EC) migration we used murine and bovine aortic ECs in an in vitro wound-healing model. We found that exogenous or endogenous NO stimulated EC migration. Moreover, migration was significantly delayed in ECs derived from endothelial NO synthase-deficient mice compared with WT murine aortic EC. To assess the contribution of matrix metalloproteinase (MMP)-13 to NO-mediated EC migration, we used RNA interference to silence MMP-13 expression in ECs. Migration was delayed in cells in which MMP-13 was silenced. In untreated cells MMP-13 was localized to caveolae, forming a complex with caveolin-1. Stimulation with NO disrupted this complex and significantly increased extracellular MMP-13 abundance, leading to collagen breakdown. Our findings show that MMP-13 is an important effector of NO-activated endothelial migration.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Caveolin 1
  • Caveolins / physiology
  • Cell Movement*
  • Collagenases / physiology*
  • Endothelial Cells / cytology*
  • Matrix Metalloproteinase 13
  • Mice
  • Mice, Inbred C57BL
  • Nitric Oxide / physiology*
  • Nitric Oxide Synthase / physiology
  • Nitric Oxide Synthase Type II
  • Nitric Oxide Synthase Type III
  • Wound Healing*

Substances

  • Cav1 protein, mouse
  • Caveolin 1
  • Caveolins
  • Nitric Oxide
  • Nitric Oxide Synthase
  • Nitric Oxide Synthase Type II
  • Nitric Oxide Synthase Type III
  • Nos3 protein, mouse
  • Collagenases
  • Matrix Metalloproteinase 13
  • Mmp13 protein, mouse