Literature DB >> 8567978

Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice.

V J Kadambi1, S Ponniah, J M Harrer, B D Hoit, G W Dorn, R A Walsh, E G Kranias.   

Abstract

Phospholamban is the regulator of the cardiac sarcoplasmic reticulum (SR) Ca(2+)-ATPase activity and an important modulator of basal contractility in the heart. To determine whether all the SR Ca(2+)-ATPase enzymes are subject to regulation by phospholamban in vivo, transgenic mice were generated which overexpressed phospholamban in the heart, driven by the cardiac-specific alpha-myosin heavy chain promoter. Quantitative immunoblotting revealed a twofold increase in the phospholamban protein levels in transgenic hearts compared to wild type littermate hearts. The transgenic mice showed no phenotypic alterations and no changes in heart/body weight, heart/lung weight, and cardiomyocyte size. Isolated unloaded cardiac myocytes from transgenic mice exhibited diminished shortening fraction (63%) and decreased rates of shortening (64%) and relengthening (55%) compared to wild type (100%) cardiomyocytes. The decreases in contractile parameters of transgenic cardiomyocytes reflected decreases in the amplitude (83%) of the Ca2+ signal and prolongation (131%) in the time for decay of the Ca2+ signal, which was associated with a decrease in the apparent affinity of the SR Ca(2+)-ATPase for Ca2+ (56%), compared to wild type (100%) cardiomyocytes. In vivo analysis of left ventricular systolic function using M mode and pulsed-wave Doppler echocardiography revealed decreases in fractional shortening (79%) and the normalized mean velocity of circumferential shortening (67%) in transgenic mice compared to wild type (100%) mice. The differences in contractile parameters and Ca2+ kinetics in transgenic cardiomyocytes and the depressed left ventricular systolic function in transgenic mice were abolished upon isoproterenol stimulation. These findings indicate that a fraction of the Ca(2+)-ATPases in native SR is not under regulation by phospholamban. Expression of additional phospholamban molecules results in: (a) inhibition of SR Ca2+ transport; (b) decreases in systolic Ca2+ levels and contractile parameters in ventricular myocytes; and (c) depression of basal left ventricular systolic function in vivo.

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Year:  1996        PMID: 8567978      PMCID: PMC507048          DOI: 10.1172/JCI118446

Source DB:  PubMed          Journal:  J Clin Invest        ISSN: 0021-9738            Impact factor:   14.808


  33 in total

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Journal:  Biochemistry       Date:  1979-11-13       Impact factor: 3.162

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Journal:  Circ Res       Date:  1979-03       Impact factor: 17.367

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Journal:  Biotechniques       Date:  1995-06       Impact factor: 1.993

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Journal:  Neurochem Res       Date:  1987-10       Impact factor: 3.996

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Journal:  J Biol Chem       Date:  1974-10-10       Impact factor: 5.157

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Journal:  Circ Res       Date:  1974-04       Impact factor: 17.367

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Authors:  E G Kranias; R J Solaro
Journal:  Nature       Date:  1982-07-08       Impact factor: 49.962

8.  In vivo echocardiographic detection of enhanced left ventricular function in gene-targeted mice with phospholamban deficiency.

Authors:  B D Hoit; S F Khoury; E G Kranias; N Ball; R A Walsh
Journal:  Circ Res       Date:  1995-09       Impact factor: 17.367

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Journal:  Biochem J       Date:  1988-02-01       Impact factor: 3.857

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Authors:  E G Kranias
Journal:  J Biol Chem       Date:  1985-09-15       Impact factor: 5.157

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  62 in total

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Authors:  J James; H Osinska; T E Hewett; T Kimball; R Klevitsky; S Witt; D G Hall; J Gulick; J Robbins
Journal:  Transgenic Res       Date:  1999-02       Impact factor: 2.788

2.  The Federation of European Physiological Societies (FEPS). Are physiologists ready for new physiology?

Authors:  B Swynghedauw
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Journal:  Mol Cell Biol       Date:  2002-06       Impact factor: 4.272

4.  Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17.

Authors:  Piero Pollesello; Arto Annila
Journal:  Biophys J       Date:  2002-07       Impact factor: 4.033

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Journal:  J Physiol       Date:  2003-01-01       Impact factor: 5.182

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Journal:  Proc Natl Acad Sci U S A       Date:  2004-06-16       Impact factor: 11.205

7.  Pathogenesis of dilated cardiomyopathy: molecular, structural, and population analyses in tropomodulin-overexpressing transgenic mice.

Authors:  M A Sussman; S Welch; N Gude; P R Khoury; S R Daniels; D Kirkpatrick; R A Walsh; R L Price; H W Lim; J D Molkentin
Journal:  Am J Pathol       Date:  1999-12       Impact factor: 4.307

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Journal:  Curr Mol Med       Date:  2012-02       Impact factor: 2.222

Review 9.  Alterations in adrenergic receptor signaling in heart failure.

Authors:  S Lamba; W T Abraham
Journal:  Heart Fail Rev       Date:  2000-03       Impact factor: 4.214

10.  Posttranslational modifications of calcium/calmodulin-dependent protein kinase IIδ and its downstream signaling in human failing hearts.

Authors:  Tomas Rajtik; Eva Goncalvesova; Zoltan V Varga; Przemyslaw Leszek; Mariusz Kusmierczyk; Michal Hulman; Jan Kyselovic; Peter Ferdinandy; Adriana Adameova
Journal:  Am J Transl Res       Date:  2017-08-15       Impact factor: 4.060

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