Matrix metalloproteinase 13 mediates nitric oxide activation of endothelial cell migration
| Autor: | José M. López-Novoa, Mónica Martínez-Moreno, Carlos Zaragoza, Alberto Álvarez-Barrientos, Esther López-Rivera, Santiago Lamas, Jose L. Rodrigo, Alicia Rodríguez-Barbero, Tania R. Lizarbe, Ana Patricia Fernández |
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| Rok vydání: | 2005 |
| Předmět: |
Nitric Oxide Synthase Type III
Caveolin 1 Nitric Oxide Synthase Type II Biology Matrix metalloproteinase Nitric Oxide Caveolins Mice Cell Movement Caveolae Matrix Metalloproteinase 13 Extracellular Animals Collagenases Wound Healing Multidisciplinary Endothelial Cells Biological Sciences Cell biology Mice Inbred C57BL Nitric oxide synthase Endothelial stem cell Biochemistry biology.protein Cattle Nitric Oxide Synthase Wound healing |
| Zdroj: | Proceedings of the National Academy of Sciences. 102:3685-3690 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0408217102 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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