Download 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.)

Alteration of excitation-contraction coupling within the failing human center used to be deemed an engaging topic for a discussion among easy scientists and medical researchers in continuation of earlier Gargellen meetings curious about the functionality of the conventional and failing human myocardium. In 1987 uncomplicated mechanisms and scientific implications of then new insights into cardiac energetics was once by way of a entire assessment of inotropic stimulation and myocardial energetics in 1989. right here, we undertook a re-examination of the rules of inotropic stimulation and of its capability healing price, in line with new observa­ tions from experiments with human myocardium. In 1992 the chance as a result of myocardial phenotype switch by reason of variation in center failure used to be released. right here, adjustments of subcellular buildings and features due to power middle failure, summarized as phenotype swap, can be defined as a necessary attribute of the failing human myocardium. This subject was once mentioned in larger 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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Talosi L, Edes I, Kranias EG (1993) Intracellular mechanisms mediating the reversal of {3-adrenergic stimulation in intact beating hearts. Am 1 PhysioI264: H791-H797 8. Luo W, Grupp IL, Doetschman T, Ponniah S, Harrer 1, Zhou Z, Kranias EG (1994) Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of {3-agonist stimulation. Circ Res 75: 401-409 9. Luo W, Kiss E, Koss KL, Grupp IL, Harrer J, Edes I, lones WK, Kranias EG (1995) Cardiac remodeling by alterations in phospholamban protein levels.

W. "----- 1600 •0 - :: » -. c :~ tl :! -< ~ Phosphorylated con,,,,~ 1200 CI. ~ If e 800 ~c -< ... 116105-- 94- - 6743- ---0 e;§0 'C e - c to ::I (\I U "1 ~j ...... ~~ 400 r- ,. 7S M Jlu . • .... " o "-"' 1 .. 4- A B Fig. 4. Phosphorylation and stimulation of purified rabbit cardiac SR Ca 2 + -ATPase by cxogenous CaM kinase. Left panel: Phosphorylation of purificd cardiac SR Ca2 + -ATPase (Ca 2 + pump) by exogenous CaM kinase. A) Coomassie Bluc-stained polycarylamide gel. B) autoradiogram of the same gel.

5-fold above atrial mRNA in measurements which were not normalized to a cardiac muscle indicator such as a-MyHC. To determine whether SERCA2 is also differentially expressed between murine atrial and ventricular compartments, we similarly analyzed the transcript ratios of SERCA2 relative to a-MyHC mRNA, using dot blots of the same cardiac RNA samples used in the quantitation of phospholamban gene transcripts (Fig. 3). Blotted RNA was probed with a 60-bp oligonucleotide, antisense to a portion of the murine SERCA2 gene.

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