Alterations of Excitation-Contraction Coupling in the by Donald M. Bers PhD (auth.), Prof. Dr. G. Hasenfuss, Prof. PDF

By Donald M. Bers PhD (auth.), Prof. Dr. G. Hasenfuss, Prof. Dr. H. Just (eds.)

ISBN-10: 3642486703

ISBN-13: 9783642486708

ISBN-10: 364248672X

ISBN-13: 9783642486722

Alteration of excitation-contraction coupling within the failing human center was once deemed an attractive topic for a discussion among easy scientists and medical researchers in continuation of past Gargellen meetings taken with the functionality of the traditional and failing human myocardium. In 1987 uncomplicated mechanisms and scientific implications of then new insights into cardiac energetics was once by way of a finished overview of inotropic stimulation and myocardial energetics in 1989. right here, we undertook a re-examination of the rules of inotropic stimulation and of its strength healing worth, in keeping with new observa­ tions from experiments with human myocardium. In 1992 the danger because of myocardial phenotype swap on account of edition in middle failure was once released. right here, changes of subcellular constructions and features on account of power middle failure, summarized as phenotype swap, should be defined as an important attribute of the failing human myocardium. This subject used to be mentioned in better intensity within the quantity "Cellular and Molecular changes within the Failing Human Heart", contemplating either the sarcolemma and the phosphodiesterases, in addition to excitation-contraction coupling and contractile proteins, extracellular matrix, and mitrochondrial function.

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At lit • ATRIUM VENTRICLE Fig. 4. Average rates of atrial and ventricular force development (+dF/dt) and relaxation of tension ( - dF/dt). The rate of ventricular contraction (+dF/dt) is approx. three-fold slower than the rate of contraction for atrial muscle. Similarly, the rate of ventricular relaxation is nearly three times slower than the rate of atrial relaxation . M. forfive to six individual muscles, recorded at maximal length-tension , which provided for normalization of the load on the muscles.

Microsomes containing the SERCA2 enzyme were harvested from these cells and subjected to phosphorylation by exogenous a-CaM kinase II. The phosphorylated and unphosphorylated (control) microsomes were then assayed for Ca2 + uptake activity at varying free ea2 + concentrations as indicated. The Ca 2+ uptake rate (nmoUminlmg of microsomal protein) of phosphorylated microsomes was normalized to the activity of control microsomes and is shown as a percentage of the control Ca2+ uptake rate . In these experiments phosporylation of SERCA 2 by CaM kinase was localized to Se~8 .

Consistent with these observations on the critical role of the phospholamban: SERCA2 ratio in contractility, recent studies in our laboratory indicated that phospholamban over-expression in the murine heart results in an increased phospholamban: SERCA2 ratio and decreses in the contractile parameters (unpublished observations). Furthermore, it is interesting to note that hearts from phospholamban knock-out mice were refractory to the inotropic effects of isoproterenol, which was effective in stimulating wild-type hearts (8, 9).

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Alterations of Excitation-Contraction Coupling in the Failing Human Heart by Donald M. Bers PhD (auth.), Prof. Dr. G. Hasenfuss, Prof. Dr. H. Just (eds.)

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