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1D-integrin and FAK
are involved in cardiac myocyte hypertrophic response
pathway
1 Departments of Physiology and Medicine and Cardiovascular Research Laboratories, University of California School of Medicine, Los Angeles, California 90095; and 2 Mayo Clinic Scottsdale, Scottsdale, Arizona 85259
Alterations in the extracellular matrix occur during the cardiac
hypertrophic process. Because integrins mediate cell-matrix adhesion
and 
1D-integrin (1D) is expressed exclusively in
cardiac and skeletal muscle, we hypothesized that 1D and focal
adhesion kinase (FAK), a proximal integrin-signaling molecule, are
involved in cardiac growth. With the use of cultured ventricular
myocytes and myocardial tissue, we found the following: 1)
1D protein expression was upregulated perinatally; 2)
1-adrenergic stimulation of cardiac myocytes increased
1D protein levels 350% and altered its cellular distribution;
3) adenovirally mediated overexpression of 1D stimulated
cellular reorganization, increased cell size by 250%, and induced
molecular markers of the hypertrophic response; and 4)
overexpression of free 1D cytoplasmic domains inhibited 1-adrenergic cellular organization and atrial
natriuretic factor (ANF) expression. Additionally, FAK was linked to
the hypertrophic response as follows: 1)
coimmunoprecipitation of 1D and FAK was detected; 2) FAK
overexpression induced ANF-luciferase; 3) rapid and
sustained phosphorylation of FAK was induced by
1-adrenergic stimulation; and 4) blunting of
the 1-adrenergically modulated hypertrophic response was
caused by FAK mutants, which alter Grb2 or Src binding, as well as by
FAK-related nonkinase, a dominant interfering FAK mutant. We conclude
that 1D and FAK are both components of the hypertrophic response
pathway of cardiac myocytes.
neonatal rat ventricular myocytes; heart; cell signaling; extracellular matrix; focal adhesion kinase
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