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이병현,배종섭,박낭운,김정은,박재용,김인산 생화학분자생물학회 2006 Experimental and molecular medicine Vol.38 No.2
Adhesion and migration of vascular smooth muscle cells (VSMCs) play an important role in the pathogenesis of atherosclerosis. These processes involve the interaction of VSMCs with extracellular matrix proteins. Here, we investigated integrin isoforms and signaling pathways mediating the adhesion and migration of VSMCs on β ig-h3, a transforming growth factor (TGF)-β -inducible extra-cellular matrix protein that is elevated in ather-osclerotic plaques. Adhesion assays showed that the α v β 5 integrin is a functional receptor for the adhesion of aortic VSMCs to β ig-h3. An YH18 motif containing amino acids between 563 and 580 of β ig-h3 was an essential motif for the adhesion and growth of VSMCs. Interaction between the YH18 motif and the α v β 5 integrin was responsible for the migration of VSMCs on β ig-h3. Inhibitors of pho-sphatidylinositide 3-kinase, extracellular signal-regulated kinase (ERK), and Src kinase reduced the adhesion and migration of VSMCs on β ig-h3. β ig-h3 triggered phosphorylation and activation of AKT, ERK, focal adhesion kinase, and paxillin mediating the adhesion and migration of VSMCs. Taken together, these results suggest that β ig-h3 and α v β 5 integrin play a role in the adhesion and migration of VSMCs during the pathogenesis of atherosclerosis.