Original Article

Integrin-linked kinase (ILK) is a widely expressed protein that contributes to cytoskeletal anchoring and macromolec-ular organization.1 In the heart, ILK promotes cardiomyocyte actin-cytoskeleton linkage to the plasma membrane at costa-meres.2 By binding to the cytoplasmic tail of β-integrins and scaffolding/recruiting multiprotein complexes, ILK contrib-utes to the adaptation of cellular processes (growth, prolifera-tion, survival, and differentiation) in response to mechanical forces applied to the extracellular matrix.1,3 ILK upregulates in human pressure-load cardiac hypertro-phy, and seems central to the adaptive hypertrophic response.4 Adenovirus-mediated ILK gene transfer attenuates adverse left ventricular remodeling postmyocardial infarction5 and enhances functional preservation/survival in rats with doxo-rubicin-induced dilated cardiomyopathy (DCM).6 A focal adhesion complex, including ILK, particularly interesting Cys-His-rich protein 1 (PINCH-1), and α-parvin promotes cell survival and is a critical target for thymosin β-4 treatment post-MI.7 We previously demonstrated that cardiac-directed knock-out of ILK causes a severe cardiomyopathy and premature death in mice.8 Subsequently, ILK mutation was demonstrated to cause DCM in man.9 Most of the deaths in ILK-deleted mice are sudden, presumably because of an acute arrhythmic cause.8 However, the functional, electrophysiological, an