Sarco/endoplasmic reticulum Ca2+(SERCA)-pumps: link to heart beats and calcium waves

Misquitta, Christine; Mack, Douglas P.; Grover, Ashok K.

doi:10.1054/ceca.1999.0032

Cited by 126 publications

(81 citation statements)

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“…SERCA2a is expressed in cardiac muscle, whereas SERCA2b is expressed ubiquitously. A third non-muscle SERCA cDNA, SERCA3a, has also been described, and the very recent cloning of the human gene provided evidence for at least three distinct mRNAs, SERCA3a, 3b and 3c [8], that differ in their 3h ends due to alternative splicing.…”

Section: Three Types Of Inspmentioning

confidence: 99%

“…Among the better-known structures are Ca# + channels, namely inositol 1,4,5-trisphosphate receptors (InsP $ -Rs) [5,6] and Ca# + pumps or sarco\endoplasmic reticulum Ca# + -ATPases (SERCAs) [7,8], which co-ordinate opposite Ca# + ion fluxes. InsP $ -Rs induce an increase in cytosolic Ca# + concentration as a result of Ca# + release from ER through the binding of InsP $ on InsP $ -Rs, whereas SERCAs are responsible for a decrease in cytosolic Ca# + concentration due to Ca# + resequestration in the ER Ca# + stores.…”

Section: Introductionmentioning

confidence: 99%

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Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Lacabaratz-Porret

Launay

Corvazier

et al. 2000

Biochemical Journal

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The endoplasmic reticulum (ER) plays a key role in Ca# + signalling through Ca# + release via inositol 1,4,5-trisphosphate receptors (InsP $ -Rs) and Ca# + uptake by sarco\endoplasmic reticulum Ca# + -ATPases (SERCAs). Here, we investigated the organization of platelet ER and its biogenesis during megakaryocytopoiesis. First, erythro\megakaryoblastic MEG 01, UT7, M-O7e and CHRF 288-11 cell lines, platelets and thrombopoietininduced UT7-Mpl cells were selected for the study of SERCA2b and SERCA3 proteins by Western blotting using the antibodies IID8 and PL\IM430, respectively. As judged by platelet glycoprotein IIIa (GPIIIa) expression, an increase in SERCA3 proteins was observed while that of SERCA2b remained unchanged throughout maturation. Second, these studies were extended to the newly described alternatively spliced SERCA3a-c RNAs and InsP $ -Rs using the in itro model of PMA-induced differentiation of MEG 01 cells. Time-course and dose-response studies showed a maximal approx. 4-fold up-regulation of SERCA3 proteins using 10 −) M PMA for 3 days, which paralleled induction of GPIIIa expression. SERCA3 induction was found to occur at the level of mRNA. The modulation of the different SERCA3 species (i.e. 3a, 3b and 3c) was isoform-specific : while

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Section: Three Types Of Inspmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Lacabaratz-Porret

Launay

Corvazier

et al. 2000

Biochemical Journal

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“…sarco(endo)plasmic reticulum Ca 2ϩ -ATPase; glucose oxidation; fatty acid oxidation; phosphocreatine-to-ATP ratio; myocardial energy potential THE CHANGES in intracellular Ca 2ϩ handling reported for the failing myocardium have been linked to sarco(endo)plasmic reticulum Ca 2ϩ -ATPase (SERCA). Calcium uptake into the sarcoplasmic reticulum (SR) by SERCA determines the rate of calcium removal for relaxation, the SR calcium content, and calcium released for contractions (33,45). In the failing heart, it has been proposed that SERCA contributes to reduced contractility and relaxation as the activity and number of these calcium transporters are reduced and calcium transients are blunted and slow to decay (1,3,12).…”

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confidence: 99%

Limited functional and metabolic improvements in hypertrophic and healthy rat heart overexpressing the skeletal muscle isoform of SERCA1 by adenoviral gene transfer in vivo

O’Donnell

Fields²,

Xu³

et al. 2008

American Journal of Physiology-Heart and Circulatory Physiology

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O'Donnell JM, Fields A, Xu X, Chowdhury SA, Geenen DL, Bi J. Limited functional and metabolic improvements in hypertrophic and healthy rat heart overexpressing the skeletal muscle isoform of SERCA1 by adenoviral gene transfer in vivo. Am J Physiol Heart Circ Physiol 295: H2483-H2494, 2008. First published October 24, 2008 doi:10.1152/ajpheart.01023.2008.-Adenoviral gene transfer of sarco(endo)plasmic reticulum Ca 2ϩ -ATPase (SERCA)2a to the hypertrophic heart in vivo has been consistently reported to lead to enhanced myocardial contractility. It is unknown if the faster skeletal muscle isoform, SERCA1, expressed in the whole heart in early failure, leads to similar improvements and whether metabolic requirements are maintained during an adrenergic challenge. In this study, Ad.cmv.SERCA1 was delivered in vivo to aortic banded and shamoperated Sprague-Dawley rat hearts. The total SERCA content increased 34%. At 48 -72 h posttransfer, echocardiograms were acquired, hearts were excised and retrograded perfused, and hemodynamics were measured parallel to NMR measures of the phosphocreatine (PCr)-to-ATP ratio (PCr/ATP) and energy substrate selection at basal and high workloads (isoproterenol). In the Langendorff mode, the rate-pressure product was enhanced 27% with SERCA1 in hypertrophic hearts and 10% in shams. The adrenergic response to isoproterenol was significantly potentiated in both groups with SERCA1.31 P NMR analysis of PCr/ATP revealed that the ratio remained low in the hypertrophic group with SERCA1 overexpression and was not further compromised with adrenergic challenge.13 C NMR analysis revealed fat and carbohydrate oxidation were unaffected at basal with SERCA1 expression; however, there was a shift from fats to carbohydrates at higher workloads with SERCA1 in both groups. Transport of NADH-reducing equivalents into the mitochondria via the ␣-ketoglutamate-malate transporter was not affected by either SERCA1 overexpression or adrenergic challenge in both groups. Echocardiograms revealed an important distinction between in vivo versus ex vivo data. In contrast to previous SERCA2a studies, the echocardiogram data revealed that SERCA1 expression compromised function (fractional shortening) in the hypertrophic group. Shams were unaffected. While our ex vivo findings support much of the earlier cardiomyocyte and transgenic data, the in vivo data challenge previous reports of improved cardiac function in heart failure models after SERCA intervention. sarco(endo)plasmic reticulum Ca 2ϩ -ATPase; glucose oxidation; fatty acid oxidation; phosphocreatine-to-ATP ratio; myocardial energy potential THE CHANGES in intracellular Ca 2ϩ handling reported for the failing myocardium have been linked to sarco(endo)plasmic reticulum Ca 2ϩ -ATPase (SERCA). Calcium uptake into the sarcoplasmic reticulum (SR) by SERCA determines the rate of calcium removal for relaxation, the SR calcium content, and calcium released for contractions (33,45). In the failing heart, it has been proposed that SERCA contributes to reduced contractil...

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“…This cytosolic calcium transient requires the rapid reuptake of calcium into the ER, which is usually accomplished by the sarco/endoplasmic reticulum calcium ATPase (SERCA) (reviewed in Ref. 17).…”

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confidence: 99%

Sarco/endoplasmic Reticulum Calcium ATPase-2 Expression Is Regulated by ATF6 during the Endoplasmic Reticulum Stress Response

Thuerauf

Hoover

Meller

et al. 2001

Journal of Biological Chemistry

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The recently described transcription factor, ATF6, mediates the expression of proteins that compensate for potentially stressful changes in the endoplasmic reticulum (ER), such as reduced ER calcium. In cardiac myocytes the maintenance of optimal calcium levels in the sarcoplasmic reticulum (SR), a specialized form of the ER, is required for proper contractility. The present study investigated the hypothesis that ATF6 serves as a regulator of the expression of sarco/endoplasmic reticulum calcium ATPase-2 (SERCA2), a protein that transports calcium into the SR from the cytoplasm. Depletion of SR calcium in cultured cardiac myocytes fostered the translocation of ATF6 from the ER to the nucleus, activated the promoter for rat SERCA2, and led to increased levels of SERCA2 protein. SERCA2 promoter induction by calcium depletion was partially blocked by dominant-negative ATF6, whereas constitutively activated ATF6 led to SERCA2 promoter activation. Mutation analyses identified a promoter-proximal ER stress-response element in the rat SERCA2 gene that was required for maximal induction by ATF6 and calcium depletion. Although this element was shown to be responsible for all of the effects of ATF6 on SERCA2 promoter activation, it was responsible for only a portion of the effects of calcium depletion. Thus, SERCA2 induction in response to calcium depletion appears to be a potentially physiologically important compensatory response to this stress that involves intracellular signaling pathways that are both dependent and independent of ATF6.

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Sarco/endoplasmic reticulum Ca2+(SERCA)-pumps: link to heart beats and calcium waves

Cited by 126 publications

References 0 publications

Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study

Limited functional and metabolic improvements in hypertrophic and healthy rat heart overexpressing the skeletal muscle isoform of SERCA1 by adenoviral gene transfer in vivo

Sarco/endoplasmic Reticulum Calcium ATPase-2 Expression Is Regulated by ATF6 during the Endoplasmic Reticulum Stress Response

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