Literature DB >> 10425730

Intracellular Ca2+ storage sites in the carp heart: comparison with the rat heart.

A Chugun1, T Oyamada, K Temma, Y Hara, H Kondo.   

Abstract

The Ca(2+)-releasing mechanisms of the sarcoplasmic reticulum responsible for cardiac muscle contraction in carp were examined and compared with these mechanisms in rats. Morphologically, the ventricular muscles of the carp heart are composed of an outer compact and an inner spongy layer. In the present study, ventricular muscle preparations were obtained from the compact layer of the carp heart, because the spongy layer does not contribute significantly to the overall force of contraction. Electron microscopic observations showed that the sarcoplasmic reticulum in the carp ventricular muscle, compared to that in the rat ventricular muscle, was poorly developed. Consistent with this finding, specific [3H]ryanodine binding to partially purified sarcoplasmic reticulum preparations obtained from carp ventricular muscle as compared with the preparations isolated from the rat ventricular muscle showed a lower affinity and a smaller number of binding sites. Additionally, a higher Ca2+ concentration was required to cause a half maximal stimulation of [3H]ryanodine binding in the carp heart. In skinned ventricular muscle fibers isolated from carp hearts, the caffeine-induced contracture was significantly weaker than that observed in rat hearts. These results suggest that, in carp hearts, the sarcoplasmic reticulum has an important role as a supply source of Ca2+ for muscle contraction, though the storage capacity and/or amount of Ca2+ release in carp was significantly smaller than that in rats.

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Year:  1999        PMID: 10425730     DOI: 10.1016/s1095-6433(99)00040-9

Source DB:  PubMed          Journal:  Comp Biochem Physiol A Mol Integr Physiol        ISSN: 1095-6433            Impact factor:   2.320


  3 in total

1.  Ryanodine and dihydropyridine receptor binding in ventricular cardiac muscle of fish with different temperature preferences.

Authors:  V Tiitu; M Vornanen
Journal:  J Comp Physiol B       Date:  2003-03-08       Impact factor: 2.200

2.  Conformational changes of a Ca2+-binding domain of the Na+/Ca2+ exchanger monitored by FRET in transgenic zebrafish heart.

Authors:  Yi Xie; Michela Ottolia; Scott A John; Jau-Nian Chen; Kenneth D Philipson
Journal:  Am J Physiol Cell Physiol       Date:  2008-06-11       Impact factor: 4.249

Review 3.  Avian cardiomyocyte architecture and what it reveals about the evolution of the vertebrate heart.

Authors:  Holly A Shiels
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2022-10-03       Impact factor: 6.671

  3 in total

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