Functional communication between PKC-targeted cardiac troponin I phosphorylation sites
                    
                        
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                    چکیده
منابع مشابه
Structural consequences of cardiac troponin I phosphorylation.
beta-Adrenergic stimulation of the heart results in bisphosphorylation of the N-terminal extension of cardiac troponin I (TnI). Bisphosphorylation of TnI reduces the affinity of the regulatory site on troponin C (TnC) for Ca(2+) by increasing the rate of Ca(2+) dissociation. What remains unclear is how the phosphorylation signal is transmitted from one subunit of troponin to another. We have pr...
متن کاملTroponin I protein kinase C phosphorylation sites and ventricular function.
OBJECTIVE Cardiac Troponin I (cTnI) phosphorylation by protein kinase C (PKC) results in a reduction of maximal actomyosin ATPase activity, an effect that is more marked at higher levels of calcium (Ca2+) and is likely to reduce active force development. We postulated that there would be greater Ca2+-dependent changes in ventricular function in hearts of cTnI transgenic (TG) mice expressing mut...
متن کاملFunctional effects of rho-kinase-dependent phosphorylation of specific sites on cardiac troponin.
We tested the hypothesis that activation of Rho-A-dependent kinase (ROCK-II) alters cardiac myofilament response to Ca2+ by mechanisms involving phosphorylation of thin filament proteins. We determined effects of a constitutively active form of ROCK-II on ATPase activity and tension development in detergent-extracted (skinned) fiber bundles isolated from mouse left ventricular papillary muscles...
متن کاملDephosphorylation specificities of protein phosphatase for cardiac troponin I, troponin T, and sites within troponin T
Protein dephosphorylation by protein phosphatase 1 (PP1), acting in concert with protein kinase C (PKC) and protein kinase A (PKA), is a pivotal regulatory mechanism of protein phosphorylation. Isolated rat cardiac myofibrils phosphorylated by PKC/PKA and dephosphorylated by PP1 were used in determining dephosphorylation specificities, Ca(2+)-stimulated Mg(2+)ATPase activities, and Ca(2+) sensi...
متن کاملRegulation of cardiac contractile function by troponin I phosphorylation.
Cardiac troponin I (cTnI) is a key regulatory protein in cardiac muscle contraction and relaxation, linking Ca(2+)-troponin C binding with activation of crossbridge reactions with the thin filament. In recent years, it has become increasingly apparent that myofilament properties as well as changes in intracellular Ca(2+) have a major role in the dynamic modulation of contractile function. The p...
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ژورنال
عنوان ژورنال: Archives of Biochemistry and Biophysics
سال: 2017
ISSN: 0003-9861
DOI: 10.1016/j.abb.2017.05.019