Open Access
Article
Integrins and proximal signaling mechanisms in cardiovascular disease
Hind Lal1,Suresh K Verma1,Donald M Foster1,Honey B Golden1,John C Reneau1,Linley E Watson1,Hitesh Singh1,David E Dostal1
1
Division of Molecular Cardiology, Cardiovascular Research Institute, The Texas AandM University System Health Science Center, College of Medicine, Baylor College of Dentistry, The Texas A and M Health Science Center, Dallas, TX, USA
DOI: 10.2741/3381 Volume 14 Issue 6, pp.2307-2334
Published: 01 January 2009
(This article belongs to the Special Issue Advances in systemic inflammatory response)
Abstract

Integrins are heterodimeric cell-surface molecules, which act as the principle mediators of molecular dialog between a cell and its extracellular matrix environment. In addition to their structural functions, integrins mediate signaling from the extracellular space into the cell through integrin-associated signaling and adaptor molecules such as FAK (focal adhesion kinase), ILK (integrin-linked kinase), PINCH (particularly interesting new cysteine-histidine rich protein) and Nck2 (non-catalytic (region of) tyrosine kinase adaptor protein-2). Via these molecules, integrin signaling tightly and cooperatively interacts with receptor tyrosine kinases (RTKs) signaling to regulate survival, proliferation and cell shape as well as polarity, adhesion, migration and differentiation. In the heart and blood vessels, the function and regulation of these molecules can be partially disturbed and thus contribute to cardiovascular diseases such as cardiac hypertrophy and atherosclerosis. In this review, we discuss the primary mechanisms of action and signaling of integrins in the cardiac and vascular system in normal and pathological states, as well as therapeutic strategies for targeting these systems (1).

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Hind Lal, Suresh K Verma, Donald M Foster, Honey B Golden, John C Reneau, Linley E Watson, Hitesh Singh, David E Dostal. Integrins and proximal signaling mechanisms in cardiovascular disease. Frontiers in Bioscience-Landmark. 2009. 14(6); 2307-2334.