scholarly journals Differential effects of Pyk2 and FAK on the hypertrophic response of cardiac myocytes

2009 ◽  
Author(s):  
Emmanuel B. Menashi ◽  
Joseph C. Loftus
Keyword(s):  
Cardiac Myocytes ◽  
Differential Effects ◽  
Hypertrophic Response

scholarly journals Focal Adhesion Kinase Is Activated and Mediates the Early Hypertrophic Response to Stretch in Cardiac Myocytes

2003 ◽  
Vol 93 (2) ◽  
pp. 140-147 ◽  
Author(s):  
Adriana S. Torsoni ◽  
Sabata S. Constancio ◽  
Wilson Nadruz ◽  
Steven K. Hanks ◽  
Kleber G. Franchini
Keyword(s):  
Focal Adhesion Kinase ◽  
Cardiac Myocytes ◽  
Focal Adhesion ◽  
Hypertrophic Response

Striated muscle-specific β1D-integrin and FAK are involved in cardiac myocyte hypertrophic response pathway

2000 ◽  
Vol 279 (6) ◽  
pp. H2916-H2926 ◽  
Author(s):  
Can G. Pham ◽  
Alice E. Harpf ◽  
Rebecca S. Keller ◽  
Hoa T. Vu ◽  
Shaw-Yung Shai ◽  
...  
Keyword(s):  
Cardiac Myocytes ◽  
Cardiac Myocyte ◽  
Striated Muscle ◽  
Ventricular Myocytes ◽  
Adrenergic Stimulation ◽  
Hypertrophic Response ◽  
Protein Levels ◽  
Cell Matrix ◽  
Mediate Cell ◽  
Cell Matrix Adhesion

Alterations in the extracellular matrix occur during the cardiac hypertrophic process. Because integrins mediate cell-matrix adhesion and β1D-integrin (β1D) is expressed exclusively in cardiac and skeletal muscle, we hypothesized that β1D 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) β1D protein expression was upregulated perinatally; 2) α1-adrenergic stimulation of cardiac myocytes increased β1D protein levels 350% and altered its cellular distribution; 3) adenovirally mediated overexpression of β1D stimulated cellular reorganization, increased cell size by 250%, and induced molecular markers of the hypertrophic response; and 4) overexpression of free β1D cytoplasmic domains inhibited α1-adrenergic cellular organization and atrial natriuretic factor (ANF) expression. Additionally, FAK was linked to the hypertrophic response as follows: 1) coimmunoprecipitation of β1D and FAK was detected; 2) FAK overexpression induced ANF-luciferase; 3) rapid and sustained phosphorylation of FAK was induced by α1-adrenergic stimulation; and 4) blunting of the α1-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 β1D and FAK are both components of the hypertrophic response pathway of cardiac myocytes.

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