Protein kinase a (PKA)-dependent troponin-I phosphorylation and PKA regulatory subunits are decreased in human dilated cardiomyopathy

Most studies indicate that failing human hearts have greater baseline myofibrillar Ca2+ sensitivity of tension development than nonfailing hearts. Phosphorylation of cardiac troponin I (TnI) by cAMP-dependent protein kinase (PKA) decreases the affinity of the troponin complex for Ca2+, thus altering...

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Veröffentlicht in:	Circulation (New York, N.Y.) N.Y.), 1999-02, Vol.99 (4), p.505-510
Hauptverfasser:	ZAKHARY, D. R, MORAVEC, C. S, STEWART, R. W, BOND, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Adult Autoradiography Biological and medical sciences Cardiology. Vascular system Cardiomyopathy, Dilated - metabolism Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - metabolism Enzyme-Linked Immunosorbent Assay Female Heart Humans Male Medical sciences Middle Aged Myocarditis. Cardiomyopathies Myofibrils - metabolism Phosphorylation Troponin I - metabolism
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Zusammenfassung:	Most studies indicate that failing human hearts have greater baseline myofibrillar Ca2+ sensitivity of tension development than nonfailing hearts. Phosphorylation of cardiac troponin I (TnI) by cAMP-dependent protein kinase (PKA) decreases the affinity of the troponin complex for Ca2+, thus altering the Ca2+ sensitivity of force production. We tested the hypothesis that PKA-dependent TnI phosphorylation is altered in the failing human heart and investigated changes in PKA regulatory subunits as a potential mechanism. Using in vitro back-phosphorylation with [gamma-32P]ATP, we demonstrated a significant (P
ISSN:	0009-7322 1524-4539
DOI:	10.1161/01.cir.99.4.505