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Relevant bibliographies by topics / Sarcolemmal Calcium ATPase pump

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Academic literature on the topic 'Sarcolemmal Calcium ATPase pump'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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Journal articles on the topic "Sarcolemmal Calcium ATPase pump"

1

Chen, L. D., P. Kumar, R. J. Reiter, et al. "Melatonin prevents the suppression of cardiac Ca(2+)-stimulated ATPase activity induced by alloxan." American Journal of Physiology-Endocrinology and Metabolism 267, no. 1 (1994): E57—E62. http://dx.doi.org/10.1152/ajpendo.1994.267.1.e57.

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The effects of melatonin treatment on cardiac sarcolemmal membrane function were investigated in alloxan-injected rats. Ca(2+)-stimulated adenosine-triphosphatase (ATPase, Ca2+ pump) and Mg(2+)-ATPase activities were depressed significantly in sarcolemmal preparations from alloxan-injected rats compared with levels in control rats. These deficits were observed 2 days after alloxan injection, and they were accompanied by an increase in the density of voltage-sensitive calcium channels, as measured by the [3H]nitrendipine-binding assay. In a dose-dependent manner, treatment of rats with melatoni

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Qu, Yi, Joseph Torchia, and Amar Kumar Sen. "Protein kinase C mediated activation and phosphorylation of Ca2+ pump in cardiac sarcolemma." Canadian Journal of Physiology and Pharmacology 70, no. 9 (1992): 1230–35. http://dx.doi.org/10.1139/y92-171.

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The effects of purified protein kinase C (PKC) on the Ca2+-pumping ATPase of cardiac sarcolemma were investigated. The addition of PKC to sarcolemmal vesicles resulted in a significant increase in ATP-dependent Ca2+ uptake, by increasing the calcium affinity by 2.8-fold (Km 0.14 vs. 0.4 μM for control) and by increasing Vmax from 5 to 6.8 nmol∙mg protein−1∙min−1. The addition of PKC also stimulated Ca2+ ATPase activity in sarcolemmal preparations. This activity was increased further upon the addition of calmodulin. These results suggest that PKC stimulates Ca2+ ATPase through a kinase-directed

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Hanson, G. L., W. P. Schilling, and L. H. Michael. "Sodium-potassium pump and sodium-calcium exchange in adult and neonatal canine cardiac sarcolemma." American Journal of Physiology-Heart and Circulatory Physiology 264, no. 2 (1993): H320—H326. http://dx.doi.org/10.1152/ajpheart.1993.264.2.h320.

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The purpose of this study was to determine whether the Na(+)-K+ pump and the Na(+)-Ca2+ exchanger, two systems thought to be important in excitation-contraction coupling in the heart, change during postnatal development. In adult and neonatal canine cardiac sarcolemmal preparations, Na(+)-K(+)-adenosine-triphosphatase (ATPase) activity and specific [3H]ouabain binding were found to be higher in the adult compared with the neonate, although Na(+)-K(+)-ATPase turnover numbers were not significantly different. Furthermore, ouabain association and dissociation rate constants, examined under a vari

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Saini, Harjot K., and Naranjan S. Dhalla. "Modification of intracellular calcium concentration in cardiomyocytes by inhibition of sarcolemmal Na+/H+ exchanger." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 6 (2006): H2790—H2800. http://dx.doi.org/10.1152/ajpheart.00535.2006.

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Although the Na+/H+ exchanger (NHE) is considered to be involved in regulation of intracellular Ca2+ concentration ([Ca2+]i) through the Na+/Ca2+ exchanger, the exact mechanisms of its participation in Ca2+ handling by cardiomyocytes are not fully understood. Isolated rat cardiomyocytes were treated with or without agents that are known to modify Ca2+ movements in cardiomyocytes and exposed to an NHE inhibitor, 5-( N-methyl- N-isobutyl)amiloride (MIA). [Ca2+]i in cardiomyocytes was measured spectrofluorometrically with fura 2-AM in the absence or presence of KCl, a depolarizing agent. MIA incr

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Colston, J. T., P. Kumar, J. P. Chambers, and G. L. Freeman. "Altered sarcolemmal calcium channel density and Ca2+-pump ATPase activity in tachycardia heart failure." Cell Calcium 16, no. 5 (1994): 349–56. http://dx.doi.org/10.1016/0143-4160(94)90028-0.

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Piuhola, Jarkko, Annette Hammes, Kai Schuh, Ludwig Neyses, Olli Vuolteenaho, and Heikki Ruskoaho. "Overexpression of sarcolemmal calcium pump attenuates induction of cardiac gene expression in response to ET-1." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 281, no. 3 (2001): R699—R705. http://dx.doi.org/10.1152/ajpregu.2001.281.3.r699.

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The function of the plasma membrane calmodulin-dependent calcium ATPase (PMCA) in myocardium is unknown. PMCA is localized in caveolae, 50- to 100-nm membrane invaginations, which also contain receptors for endothelin-1 (ET-1) and various other ligands. PMCA has been suggested to play a role in regulation of caveolar signal transduction. We studied the effects of the hypertrophic agonist ET-1 and increased coronary perfusion pressure on cardiac synthesis of B-type natriuretic peptide (BNP) in transgenic rats overexpressing the human PMCA 4CI in isolated perfused heart preparation. ET-1 infusio

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Kaminishi, T., T. Matsuoka, T. Yanagishita, and K. J. Kako. "Increase vs. decrease of calcium uptake by isolated heart cells induced by H2O2 vs. HOCl." American Journal of Physiology-Cell Physiology 256, no. 3 (1989): C598—C607. http://dx.doi.org/10.1152/ajpcell.1989.256.3.c598.

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Adult rat heart myocytes were labeled rapidly with exogenous [45Ca2+]. Addition of 2.5 mM H2O2 to the heart cell suspension raised the content of rapidly exchangeable intracellular Ca2+ twofold, whereas addition of 1-30 mM HOCl decreased the Ca2+ content. The H2O2-induced increase in Ca2+ content was dependent on the medium Na+, pH, and temperature but was not significantly affected by addition of verapamil, diltiazem, amiloride, or 3-aminobenzamide. The [3H]ouabain binding to myocytes was suppressed by H2O2, whereas the Ca2+ efflux from myocytes was not influenced. An uncoupler, carbonyl cyan

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DOWLING, Paul, Philip DORAN, and Kay OHLENDIECK. "Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy." Biochemical Journal 379, no. 2 (2004): 479–88. http://dx.doi.org/10.1042/bj20031311.

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Although the primary abnormality in dystrophin is the underlying cause for mdx (X-chromosome-linked muscular dystrophy), abnormal Ca2+ handling after sarcolemmal microrupturing appears to be the pathophysiological mechanism leading to muscle weakness. To develop novel pharmacological strategies for eliminating Ca2+-dependent proteolysis, it is crucial to determine the fate of Ca2+-handling proteins in dystrophin-deficient fibres. In the present study, we show that a key luminal Ca2+-binding protein SAR (sarcalumenin) is affected in mdx skeletal-muscle fibres. One- and two-dimensional immunoblo

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Li, Li, Guoxiang Chu, Evangelia G. Kranias, and Donald M. Bers. "Cardiac myocyte calcium transport in phospholamban knockout mouse: relaxation and endogenous CaMKII effects." American Journal of Physiology-Heart and Circulatory Physiology 274, no. 4 (1998): H1335—H1347. http://dx.doi.org/10.1152/ajpheart.1998.274.4.h1335.

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Increases in heart rate are accompanied by acceleration of relaxation. This effect is apparent at the single myocyte level and depends on sarcoplasmic reticulum (SR) Ca transport and Ca/calmodulin dependent protein kinase [CaMKII; see R. A. Bassani, A. Mattiazzi, and D. M. Bers. Am. J. Physiol. 268 ( Heart Circ. Physiol. 37): H703–H712, 1995]. Because phosphorylation of phospholamban (PLB) by CaMKII can stimulate SR Ca transport, it is a plausible candidate mechanism. We examined this issue using ventricular myocytes isolated from wild-type (WT) mice and those in which the PLB gene was ablated

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Liu, Jie, Syevda Sirenko, Magdalena Juhaszova, et al. "Age-associated abnormalities of intrinsic automaticity of sinoatrial nodal cells are linked to deficient cAMP-PKA-Ca2+signaling." American Journal of Physiology-Heart and Circulatory Physiology 306, no. 10 (2014): H1385—H1397. http://dx.doi.org/10.1152/ajpheart.00088.2014.

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A reduced sinoatrial node (SAN) functional reserve underlies the age-associated decline in heart rate acceleration in response to stress. SAN cell function involves an oscillatory coupled-clock system: the sarcoplasmic reticulum (SR), a Ca2+clock, and the electrogenic-sarcolemmal membrane clock. Ca2+-activated-calmodulin-adenylyl cyclase/CaMKII-cAMP/PKA-Ca2+signaling regulated by phosphodiesterase activity drives SAN cells automaticity. SR-generated local calcium releases (LCRs) activate Na+/Ca2+exchanger in the membrane clock, which initiates the action potential (AP). We hypothesize that SAN

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Dissertations / Theses on the topic "Sarcolemmal Calcium ATPase pump"

1

Zhang, Jing. "Sarcoplasmic reticulum ATPase and sarcolemmal calcium(2+)-ATPase messenger RNA expression during in vitro skeletal muscle cell differentiation." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp01/MQ32292.pdf.

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Lockyer, Peter John. "Cloning, expression and inhibitor studies of organellar Ca'2'+-ATPase." Thesis, University of Southampton, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.242292.

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Bhupathy, Poornima. "Sarcolipin a novel regulator of the cardiac sarcoplasmic reticulum calcium ATPase." Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1202404580.

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James, Andrew. "Metabolic regulation of the plasma membrane calcium pump in pancreatic ductal adenocarcinoma." Thesis, University of Manchester, 2015. https://www.research.manchester.ac.uk/portal/en/theses/metabolic-regulation-of-the-plasma-membrane-calcium-pump-in-pancreatic-ductal-adenocarcinoma(0533b59c-e6ee-41fb-ad32-cb4784eadfa1).html.

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Pancreatic ductal adenocarcinoma (PDAC) is an aggressive form of cancer with poor prognosis and limited treatment options. Since many patients present with metastatic disease and are thus ineligible for surgical resection, PDAC is almost ubiquitously fatal; new treatment options are therefore needed to combat this disease. A key hallmark of many cancers, including PDAC, is metabolic reprogramming and a shift towards a high glycolytic rate, known as the Warburg effect. This allows cancer cells to generate ATP in the face of hypoxia and to meet the increased metabolic requirements associated wit

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Pavoine, Catherine. "La pompe à calcium de la membrane plasmique de l'hépatocyte." Paris 6, 1986. http://www.theses.fr/1986PA066424.

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Zhang, Jing. "Sarcoplasmic reticulum ATPase and sarcolemmal calcium(2+)-ATPase messenger RNA expression during in vitro skeletal muscle cell differentiation." 1997. http://hdl.handle.net/1993/1381.

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Three genes coding sarcoplasmic reticulum Ca$\sp{2+}$-ATPases (SERCA) and at least four genes coding sarcolemmal Ca$\sp{2+}$-ATPase (PMCA) have been isolated and characterized. The objective of this work was to study the mRNA expression for Ca$\sp{2+}$-ATPase isoforms during in vitro differentiation of skeletal muscle cell lines. To analyze the mRNA expression pattern of the SERCA and PMCA isoforms, three skeletal muscle cell lines (L6, C2C12, Sol8) were used as models. The mRNAs of these Ca$\sp{2+}$-ATPase gene were detected by a semi-quantitatively RT-PCR technique. It is generally regarded

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Akin, Brandy Lee. "Investigating the molecular mechanism of phospholamban regulation of the Ca²-pump of cardiac sarcoplasmic reticulum." Thesis, 2011. http://hdl.handle.net/1805/2516.

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Indiana University-Purdue University Indianapolis (IUPUI)<br>The Ca2+ pump or Ca2+-ATPase of cardiac sarcoplasmic reticulum, SERCA2a, is regulated by phospholamban (PLB), a small inhibitory phosphoprotein that decreases the apparent Ca2+ affinity of the enzyme. We propose that PLB decreases Ca2+ affinity by stabilizing the Ca2+-free, E2·ATP state of the enzyme, thus blocking the transition to E1, the high Ca2+ affinity state required for Ca2+ binding and ATP hydrolysis. The purpose of this dissertation research is to critically evaluate this idea using series of cross-linkable PLB mutants of

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Book chapters on the topic "Sarcolemmal Calcium ATPase pump"

1

Imai, Shoichi, Yutaka Yoshida, and Hsiao-Tung Sun. "Sarcolemmal (Ca2+ + Mg2+)-ATPase of Vascular Smooth Muscle." In Calcium Protein Signaling. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5679-0_10.

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Tsokos-Kuhn, Janice O., Helen Hughes, Charles V. Smith, and Jerry R. Mitchell. "Alkylating Toxins and the Liver Plasma Membrane Calcium Pump/Calcium ATPase." In Advances in Experimental Medicine and Biology. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4757-0007-7_17.

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3

Tada, Michihiko, Masaaki Kadoma, and Junichi Fujii. "Molecular Structure of Canine Cardiac Phospholamban, the Regulatory Protein of Ca Pump ATPase of Sarcoplasmic Reticulum." In Cell Calcium Metabolism. Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5598-4_11.

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4

Krain, B., A. Hammes, and L. Neyses. "Regulation of mRNA-expression of the sarcolemmal calmodulin-dependent calcium pump in cardiac hypertrophy." In Alterations of Excitation-Contraction Coupling in the Failing Human Heart. Steinkopff, 1998. http://dx.doi.org/10.1007/978-3-642-48670-8_9.

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Stafford, Nicholas, Ludwig Neyses, and Delvac Oceandy. "The Control of Sub-plasma Membrane Calcium Signalling by the Plasma Membrane Calcium ATPase Pump PMCA4." In Microdomains in the Cardiovascular System. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54579-0_16.

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Ziegelhöffer, Attila, Tatiana Ravingerová, Andrej Džurba, et al. "Prevention by 7-oxo-prostacyclin of the calcium paradox in rat heart: Role of the sarcolemmal (Na,K)-ATPase." In Biochemical Mechanisms in Heart Function. Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1279-6_33.

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Carafoli, Ernesto. "The Ca2+-Atpase of the Plasma Membrane." In Cellular Calcium. Oxford University PressOxford, 1991. http://dx.doi.org/10.1093/oso/9780199631315.003.0013.

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Abstract 1. Introduction The ejection of Ca2+ from cells is a necessity dictated by the existence in the plasma membrane of Ca channels which permit, albeit in a strictly controlled fashion, the penetration of Ca into the cell. Normally, Ca is about 10 000 times less concentrated in the cytosol than in the environment: therefore its ejection is an active process, and is indeed mediated by an ATP-powered pump. The pump was discovered by Schatzmann in 1966 in erythrocytes (1), and was subsequently found in a number of other eukaryotic plasma membranes (for reviews, see refs 2-5). The pump belong

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Celio, Marco R. "Ca2+ -ATPase (plasma membrane)." In Guidebook to the Calcium-binding Proteins. Oxford University PressOxford, 1996. http://dx.doi.org/10.1093/oso/9780198599517.003.0025.

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Abstract The plasma membrane Ca2+ ATPase (PMCA) or Ca2• pump is an integral membrane protein which is present in all mammalian cells. It belongs to the family of the P-type ATPases. The pump transports Ca2+ ions out of the cells, by using the energy stored in ATP and is essential in the control of the Ca2+ concentration in the cytosol.

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Garg, Dr Gopal. "Antiulcer Agents." In Edited Book of Pharmacology-III [According to Latest Syllabus of B. Pharm-VI Semester of Pharmacy Council of India]. Iterative International Publishers, Selfypage Developers Pvt Ltd, 2024. http://dx.doi.org/10.58532/nbennurphch2.

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Antiulcer agents are essential medications used to manage and treat conditions like peptic ulcers, gastroesophageal reflux disease (GERD), and other acid-related disorders of the gastrointestinal tract. These agents are classified into several categories based on their mechanisms of action: proton pump inhibitors (PPIs), H2-receptor antagonists (H2RAs), antacids, mucosal protective agents, antibiotics, and prostaglandin analogues. PPIs, such as omeprazole and lansoprazole, work by irreversibly inhibiting the hydrogen-potassium ATPase enzyme, significantly reducing gastric acid secretion. H2RAs

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