By Donald M. Bers PhD (auth.), Prof. Dr. G. Hasenfuss, Prof. Dr. H. Just (eds.)
Alteration of excitation-contraction coupling within the failing human center used to be deemed an engaging topic for a discussion among uncomplicated scientists and scientific researchers in continuation of past Gargellen meetings excited about the functionality of the conventional and failing human myocardium. In 1987 easy mechanisms and medical implications of then new insights into cardiac energetics used to be through a entire evaluation of inotropic stimulation and myocardial energetics in 1989. right here, we undertook a second look of the foundations of inotropic stimulation and of its power healing price, in accordance with new observa tions from experiments with human myocardium. In 1992 the danger as a result of myocardial phenotype swap due to model in middle failure used to be released. right here, adjustments of subcellular buildings and services as a result of continual center failure, summarized as phenotype switch, should be defined as a necessary attribute of the failing human myocardium. This subject used to be mentioned in better intensity within the quantity "Cellular and Molecular adjustments 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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Extra resources for Alterations of Excitation-Contraction Coupling in the Failing Human Heart
10). Measurements of developed left-ventricular pressure (DP), rate of left-ventricular pressure development (+dP/dt), and rate of pressure release (-dP/dt) were recorded as previously described (8, 10). M. under control conditions and at maximal isoproterenol stimulation, as previously described (8). The times to left-ventricular peak pressure development (TPP) and to half-relaxation of left ventricular pressure (RT llz ) were measured via digital micrometer and normalized to DP. M. under control conditions and during maximal isoproterenol stimulation, as previously described (8).
2-fold higher in the murine ventricle than in the murine atrium. 50 SERCA2 PLB ~ Q.. 00 ATRIUM VENTRICLE Fig. 3, Relative gene expression levcls of phospholamban and SERCA2 gene transcripts to cardiac a-MyHC in murine atrium and ventricle. 2-fold above that of ventricular muscle , while atrial phospholamban mRNA is three-fold below that of ventricular muscle. All mRNA levels were measured by phosphorimager analysis of hybridized RNA dot blots and reported relative to whole heart mRNA. Values represent the mean of six determinations.
Kranias, PhD Dept. of Pharmacology and Cell Biophysics University of Cincinnati College of Medicine 231 Bethesda Ave. Cincinnati, Ohio 45267-0575. USA 37 Phosphorylation and regulation of the Ca2+ -pumping ATPase in cardiac sarcoplasmic reticulum by calcium/calmodulindependent protein kinase N. Narayanan , A. Xu Department of Ph ysiology. Medical Sciences Building. University of Western Ontario. London. Canada Abstract In cardiac muscle, a membrane-associated Ca2 +/calmodulin-dependent protein kinase (CaM kinase) phosphorylates the Ca 2 +-pumping ATPase in addition to its previously characterized substrates, phospholamban and Ca 2 +-release channel (ryanodine receptor).
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.)