Document Detail

betaig-h3 triggers signaling pathways mediating adhesion and migration of vascular smooth muscle cells through alphavbeta5 integrin.
MedLine Citation:
PMID:  16672769     Owner:  NLM     Status:  MEDLINE    
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 betaig-h3, a transforming growth factor (TGF)-beta-inducible extracellular matrix protein that is elevated in atherosclerotic plaques. Adhesion assays showed that the alphavbeta5 integrin is a functional receptor for the adhesion of aortic VSMCs to betaig-h3. An YH18 motif containing amino acids between 563 and 580 of betaig-h3 was an essential motif for the adhesion and growth of VSMCs. Interaction between the YH18 motif and the alphavbeta5 integrin was responsible for the migration of VSMCs on betaig-h3. Inhibitors of phosphatidylinositide 3-kinase, extracellular signal-regulated kinase (ERK), and Src kinase reduced the adhesion and migration of VSMCs on betaig-h3. betaig-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 betaig-h3 and alphavbeta5 integrin play a role in the adhesion and migration of VSMCs during the pathogenesis of atherosclerosis.
Byung Heon Lee; Jong Sup Bae; Rang Woon Park; Jung Eun Kim; Jae Yong Park; In San Kim
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Experimental & molecular medicine     Volume:  38     ISSN:  1226-3613     ISO Abbreviation:  Exp. Mol. Med.     Publication Date:  2006 Apr 
Date Detail:
Created Date:  2006-05-04     Completed Date:  2006-07-25     Revised Date:  2013-06-03    
Medline Journal Info:
Nlm Unique ID:  9607880     Medline TA:  Exp Mol Med     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  153-61     Citation Subset:  IM    
Department of Biochemistry and Cell and Matrix Biology Research Institute, School of Medicine, Kyungpook National University, Daegu 700-422, Korea.
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MeSH Terms
Amino Acid Motifs / genetics
Amino Acid Sequence
Cell Adhesion / physiology
Cell Movement / physiology*
Cells, Cultured
Chromones / pharmacology
Enzyme Inhibitors / pharmacology
Extracellular Matrix Proteins / genetics,  physiology*
Extracellular Signal-Regulated MAP Kinases / antagonists & inhibitors
Flavonoids / pharmacology
Integrins / genetics,  physiology*
Molecular Sequence Data
Morpholines / pharmacology
Muscle, Smooth, Vascular / cytology,  drug effects,  metabolism*
Myocytes, Smooth Muscle / drug effects,  metabolism
Paxillin / metabolism
Phosphatidylinositol 3-Kinases / antagonists & inhibitors
Protein-Tyrosine Kinases / antagonists & inhibitors
Receptors, Vitronectin / genetics,  physiology*
Signal Transduction / physiology*
Transforming Growth Factor beta / genetics,  physiology*
src-Family Kinases / antagonists & inhibitors
Reg. No./Substance:
0/2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one; 0/Chromones; 0/Enzyme Inhibitors; 0/Extracellular Matrix Proteins; 0/Flavonoids; 0/Integrins; 0/Morpholines; 0/Paxillin; 0/Receptors, Vitronectin; 0/Transforming Growth Factor beta; 0/integrin alphaVbeta5; 148710-76-3/betaIG-H3 protein; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC Kinases; EC Kinases; EC Signal-Regulated MAP Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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