Visualization of biphasic Ca2+diffusion from cytosol to nucleus in contracting adult rat cardiac myocytes with an ultra-fast confocal imaging system

Genka, Chokoh; Ishida, Hideyuki; Ichimori, Kohji; Hirota, Yuki; Tanaami, Takeo; Nakazawa, Hiroe

doi:10.1054/ceca.1999.0026

Cited by 51 publications

(45 citation statements)

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“…Similar results were obtained with cardiomyocytes [40] and coronary smooth muscle cells [41]. Therefore in the model, sarcoplasmic Ca 2+ removal (accounted for by a single time constant λ) was considered to be inhomogeneous, being highest just outside the nucleus.…”

Section: A 3-d Model For Amplitude Modulation Of Nuclear Ca 2+ Signalssupporting

confidence: 70%

“…Experimental data obtained with cardiac myocytes lead to the conclusion that Ca 2+ diffused freely through NPCs at low cytosolic Ca 2+ and that this diffusion was partially restricted at high cytosolic Ca 2+ [40]. Our experiments show that the maximal amplitude of [Ca 2+ ] S remained the same when changing from a single stimulus to a train of stimuli.…”

Section: A 3-d Model For Amplitude Modulation Of Nuclear Ca 2+ Signalssupporting

confidence: 54%

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Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

Koopman¹,

Willems²,

Oosterhof³

et al. 2005

Cell Calcium

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Video-rate confocal microscopy of Indo-1-loaded human skeletal myotubes was used to assess the relationship between the changes in sarcoplasmic ( [Ca 2+ ] N then increased to a maximum that was 2.3-fold higher than that of the single transient and equalled that of [Ca 2+ ] S . In the nucleus, and to a lesser extent in the sarcoplasm, [Ca 2+ ] decreased faster at the end of the stimulus train than after the preceding single stimulus (time constants of 3.3 and 2.1 s, respectively). To gain insight into the molecular principles underlying the shaping of the nuclear Ca 2+ signal, a 3-D mathematical model was constructed. Intriguingly, quantitative modelling required the inclusion of a satiable nuclear Ca 2+ buffer. Alterations in the concentration of this putative buffer had dramatic effects on the kinetics of the nuclear Ca 2+ signal. This finding unveils a possible mechanism by which the skeletal muscle can adapt to changes in physiological demand.

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Section: A 3-d Model For Amplitude Modulation Of Nuclear Ca 2+ Signalssupporting

confidence: 70%

Section: A 3-d Model For Amplitude Modulation Of Nuclear Ca 2+ Signalssupporting

confidence: 54%

Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

Koopman¹,

Willems²,

Oosterhof³

et al. 2005

Cell Calcium

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show abstract

“…The increases in cytosolic Ca 2ϩ were initially thought to be transmitted passively to the nucleus via Ca 2ϩ diffusion through nuclear pore complexes (31)(32)(33). More recent studies showed that cardiomyocytes contain a separate membrane source around and within the nucleus that is sensitive to IP 3 (2, 14, 22, 24, 25, 29).…”

Section: Discussionmentioning

confidence: 99%

Calsequestrin Accumulation in Rough Endoplasmic Reticulum Promotes Perinuclear Ca2+ Release

Guo

Cala

Song

2012

Journal of Biological Chemistry

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“…4). Due to a diffusional delay, the nuclear Ca 2+ transient lags behind the cytoplasmic Ca 2+ transient, as visualized by confocal Ca 2+ imaging [71,72,167]. Hormone-independent increases in cytoplasmic Ca 2+ transients (elicited by elevation of extracellular Ca 2+ ) are followed by increases in nuclear Ca 2+ transients of similar magnitude [72].…”

Section: Ip 3 Rs In Other Cardiac Cellsmentioning

confidence: 99%

Emerging roles of inositol 1,4,5-trisphosphate signaling in cardiac myocytes

Kockskämper

Zima

Roderick

et al. 2008

Journal of Molecular and Cellular Cardiology

172

149

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Inositol 1,4,5-trisphosphate (IP 3 ) is a ubiquitous intracellular messenger regulating diverse functions in almost all mammalian cell types. It is generated by membrane receptors that couple to phospholipase C (PLC), an enzyme which liberates IP 3 from phosphatidylinositol 4,5-bisphosphate (PIP 2 ). The major action of IP 3 , which is hydrophilic and thus translocates from the membrane into the cytoplasm, is to induce Ca 2+ release from endogenous stores through IP 3 receptors (IP 3 Rs). Cardiac excitation-contraction coupling relies largely on ryanodine receptor (RyR)-induced Ca 2+ release from the sarcoplasmic reticulum. Myocytes express a significantly larger number of RyRs compared to IP 3 Rs (∼100:1), and furthermore they experience substantial fluxes of Ca 2+ with each heartbeat. Therefore, the role of IP 3 and IP 3 -mediated Ca 2+ signaling in cardiac myocytes has long been enigmatic. Recent evidence, however, indicates that despite their paucity cardiac IP 3 Rs may play crucial roles in regulating diverse cardiac functions. Strategic localization of IP 3 Rs in cytoplasmic compartments and the nucleus enables them to participate in subsarcolemmal, bulk cytoplasmic and nuclear Ca 2+ signaling in embryonic stem cell-derived and neonatal cardiomyocytes, and in adult cardiac myocytes from the atria and ventricles. Intriguingly, expression of both IP 3 Rs and membrane receptors that couple to PLC/IP 3 signaling is altered in cardiac disease such as atrial fibrillation or heart failure, suggesting the involvement of IP 3 signaling in the pathology of these diseases. Thus, IP 3 exerts important physiological and pathological functions in the heart, ranging from the regulation of pacemaking, excitation-contraction and excitation-transcription coupling to the initiation and/or progression of arrhythmias, hypertrophy and heart failure. KeywordsInositol 1,4,5-trisphosphate; Cardiac myocyte; Calcium; Inotropy; Arrhythmias; Nucleus; Hypertrophy © 2008 Elsevier Inc. All rights reserved. * Corresponding author. E-mail address: jens.kockskaemper@meduni-graz.at (J. Kockskämper).. NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript The discovery of IP 3A quarter of a century ago it was shown that D-myo inositol 1,4,5-trisphosphate (IP 3 ) releases Ca 2+ from a non-mitochondrial internal Ca 2+ store [1]. Since this hallmark discovery, IP 3 has emerged as a ubiquitous intracellular messenger, releasing Ca 2+ from stores through activation of IP 3 receptors (IP 3 Rs) in almost all eukaryotic cells. The major IP 3 -sensitive intracellular Ca 2+ store is the endoplasmic reticulum. However, IP 3 has also been shown to release Ca 2+ stored in other compartments, such as the Golgi and the nuclear envelope [2]. In addition, IP 3 Rs are present on the plasma membrane of some cell types, where they can gate Ca 2+ influx [3]. A crucial role for IP 3 -dependent Ca 2+ release has been demonstrated in many mammalian cell types, ranging from tiny platelets, where it initiates blood clottin...

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Visualization of biphasic Ca2+diffusion from cytosol to nucleus in contracting adult rat cardiac myocytes with an ultra-fast confocal imaging system

Cited by 51 publications

References 0 publications

Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

Calsequestrin Accumulation in Rough Endoplasmic Reticulum Promotes Perinuclear Ca2+ Release

Emerging roles of inositol 1,4,5-trisphosphate signaling in cardiac myocytes

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