Academic literature on the topic 'Sarco-endoplasmic calcium ATPase (SERCA)'
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Journal articles on the topic "Sarco-endoplasmic calcium ATPase (SERCA)"
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Boczek, Tomasz, Marta Sobolczyk, Joanna Mackiewicz, Malwina Lisek, Bozena Ferenc, Feng Guo, and Ludmila Zylinska. "Crosstalk among Calcium ATPases: PMCA, SERCA and SPCA in Mental Diseases." International Journal of Molecular Sciences 22, no. 6 (March 10, 2021): 2785. http://dx.doi.org/10.3390/ijms22062785.
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Calcium in mammalian neurons is essential for developmental processes, neurotransmitter release, apoptosis, and signal transduction. Incorrectly processed Ca2+ signal is well-known to trigger a cascade of events leading to altered response to variety of stimuli and persistent accumulation of pathological changes at the molecular level. To counterbalance potentially detrimental consequences of Ca2+, neurons are equipped with sophisticated mechanisms that function to keep its concentration in a tightly regulated range. Calcium pumps belonging to the P-type family of ATPases: plasma membrane Ca2+-ATPase (PMCA), sarco/endoplasmic Ca2+-ATPase (SERCA) and secretory pathway Ca2+-ATPase (SPCA) are considered efficient line of defense against abnormal Ca2+ rises. However, their role is not limited only to Ca2+ transport, as they present tissue-specific functionality and unique sensitive to the regulation by the main calcium signal decoding protein—calmodulin (CaM). Based on the available literature, in this review we analyze the contribution of these three types of Ca2+-ATPases to neuropathology, with a special emphasis on mental diseases.
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NEWTON, Thomas, John P. J. BLACK, John BUTLER, Anthony G. LEE, John CHAD, and J. Malcolm EAST. "Sarco/endoplasmic-reticulum calcium ATPase SERCA1 is maintained in the endoplasmic reticulum by a retrieval signal located between residues 1 and 211." Biochemical Journal 371, no. 3 (May 1, 2003): 775–82. http://dx.doi.org/10.1042/bj20021477.
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The location of sarco/endoplasmic-reticulum calcium ATPase (SERCA) retention/retrieval motifs in the sequence of the SERCA1 has been investigated by examining the subcellular location in COS-7 cells of enhanced-green-fluorescent-protein-tagged calcium-pump chimaeras. These chimaeras have been constructed from the fast-twitch SERCA1 and the plasma-membrane calcium ATPase PMCA3. The N-terminal, central and C-terminal segments of these calcium pumps were exchanged between SERCA1 and PMCA3. The segments exchanged correspond to residues 1–211, 212–711 and 712–994 of SERCA1, and residues 1–264, 265–788 and 789–1159 of PMCA3 respectively. Only chimaeras containing the N-terminal segment of SERCA1 were located in the endoplasmic reticulum (ER), whereas chimaeras containing the N-terminal segment from PMCA3 were able to escape from the ER and enter the endomembrane pathway en route for the plasma membrane. Co-localization of SERCA1 in COS-7 cells with the ER/Golgi-intermediate compartment marker ERGIC53 indicates that SERCA1 is maintained in the ER by a process of retrieval. These results indicate that the N-terminal region of SERCA1, containing transmembrane helices M1 and M2, contains an ER-retrieval signal.
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Li, Sen, Anant Chopra, Wendy Keung, Camie W. Y. Chan, Kevin D. Costa, Chi-Wing Kong, Roger J. Hajjar, Christopher S. Chen, and Ronald A. Li. "Sarco/endoplasmic reticulum Ca2+-ATPase is a more effective calcium remover than sodium-calcium exchanger in human embryonic stem cell-derived cardiomyocytes." American Journal of Physiology-Heart and Circulatory Physiology 317, no. 5 (November 1, 2019): H1105—H1115. http://dx.doi.org/10.1152/ajpheart.00540.2018.
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Human pluripotent stem cell (hPSCs)-derived ventricular (V) cardiomyocytes (CMs) display immature Ca2+–handing properties with smaller transient amplitudes and slower kinetics due to such differences in crucial Ca2+-handling proteins as the poor sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) pump but robust Na+-Ca2+ exchanger (NCX) activities in human embryonic stem cell (ESC)-derived VCMs compared with adult. Despite their fundamental importance in excitation-contraction coupling, the relative contribution of SERCA and NCX to Ca2+-handling of hPSC-VCMs remains unexplored. We systematically altered the activities of SERCA and NCX in human embryonic stem cell-derived ventricular cardiomyocytes (hESC-VCMs) and their engineered microtissues, followed by examining the resultant phenotypic consequences. SERCA overexpression in hESC-VCMs shortened the decay of Ca2+ transient at low frequencies (0.5 Hz) without affecting the amplitude, SR Ca2+ content and Ca2+ baseline. Interestingly, short hairpin RNA-based NCX suppression did not prolong the transient decay, indicating a compensatory response for Ca2+ removal. Although hESC-VCMs and their derived microtissues exhibited negative frequency-transient/force responses, SERCA overexpression rendered them less negative at high frequencies (>2 Hz) by accelerating Ca2+ sequestration. We conclude that for hESC-VCMs and their microtissues, SERCA, rather than NCX, is the main Ca2+ remover during diastole; poor SERCA expression is the leading cause for immature negative-frequency/force responses, which can be partially reverted by forced expression. Combinatorial approach to mature calcium handling in hESC-VCMs may help shed further mechanistic insights. NEW & NOTEWORTHY In this study of human pluripotent stem cell-derived cardiomyocytes, we studied the role of sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and Na+-Ca2+ exchanger (NCX) in Ca2+ handling. Our data support the notion that SERCA is more effective in cytosolic calcium removal than the NCX.
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Rathod, Nishadh, Jessi J. Bak, Joseph O. Primeau, M’Lynn E. Fisher, Lennane Michel Espinoza-Fonseca, Mary Joanne Lemieux, and Howard S. Young. "Nothing Regular about the Regulins: Distinct Functional Properties of SERCA Transmembrane Peptide Regulatory Subunits." International Journal of Molecular Sciences 22, no. 16 (August 18, 2021): 8891. http://dx.doi.org/10.3390/ijms22168891.
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The sarco-endoplasmic reticulum calcium ATPase (SERCA) is responsible for maintaining calcium homeostasis in all eukaryotic cells by actively transporting calcium from the cytosol into the sarco-endoplasmic reticulum (SR/ER) lumen. Calcium is an important signaling ion, and the activity of SERCA is critical for a variety of cellular processes such as muscle contraction, neuronal activity, and energy metabolism. SERCA is regulated by several small transmembrane peptide subunits that are collectively known as the “regulins”. Phospholamban (PLN) and sarcolipin (SLN) are the original and most extensively studied members of the regulin family. PLN and SLN inhibit the calcium transport properties of SERCA and they are required for the proper functioning of cardiac and skeletal muscles, respectively. Myoregulin (MLN), dwarf open reading frame (DWORF), endoregulin (ELN), and another-regulin (ALN) are newly discovered tissue-specific regulators of SERCA. Herein, we compare the functional properties of the regulin family of SERCA transmembrane peptide subunits and consider their regulatory mechanisms in the context of the physiological and pathophysiological roles of these peptides. We present new functional data for human MLN, ELN, and ALN, demonstrating that they are inhibitors of SERCA with distinct functional consequences. Molecular modeling and molecular dynamics simulations of SERCA in complex with the transmembrane domains of MLN and ALN provide insights into how differential binding to the so-called inhibitory groove of SERCA—formed by transmembrane helices M2, M6, and M9—can result in distinct functional outcomes.
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Kempton, Robert J., Taylor A. Kidd-Kautz, Soizic Laurenceau, and Stefan Paula. "Heck- and Suzuki-coupling approaches to novel hydroquinone inhibitors of calcium ATPase." Beilstein Journal of Organic Chemistry 15 (April 24, 2019): 971–75. http://dx.doi.org/10.3762/bjoc.15.94.
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In this study, we explored Heck- and Suzuki-coupling methodology to modify the template 2,5-di-tert-butylhydroquinone (BHQ, 2), an inhibitor of the enzyme sarco/endoplasmic reticulum calcium ATPase (SERCA). We found that by utilizing Suzuki coupling, we could successfully attach a six-carbon tether to BHQ that terminated in a leucine moiety to obtain target 14. Similar to related compounds based on the structure of the natural product thapsigargin, 14 displayed inhibitory potency against SERCA activity. This makes 14 a suitable candidate for the future attachment of a deactivating peptide to convey specificity for prostate cancer cells.
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Launay, Sophie, Maurizio Giannı̀, Tünde Kovàcs, Raymonde Bredoux, Arlette Bruel, Pascal Gélébart, Fabien Zassadowski, Christine Chomienne, Jocelyne Enouf, and Béla Papp. "Lineage-Specific Modulation of Calcium Pump Expression During Myeloid Differentiation." Blood 93, no. 12 (June 15, 1999): 4395–405. http://dx.doi.org/10.1182/blood.v93.12.4395.
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Abstract Calcium is accumulated from the cytosol into the endoplasmic reticulum by sarco-endoplasmic reticulum calcium transport ATPase (SERCA) enzymes. Because calcium stored in the endoplasmic reticulum is essential for cell growth, differentiation, calcium signaling, and apoptosis and because different SERCA enzymes possess distinct functional characteristics, in the present report we explored SERCA expression during in vitro differentiation of the human myeloid/promyelocytic cell lines HL-60 and NB4 and of freshly isolated acute promyelocytic leukemia cells. Two SERCA species have been found to be coexpressed in these cells: SERCA 2b and another isoform, SERCAPLIM, which is recognized by the PLIM430 monoclonal antibody. Induction of differentiation along the neutrophil granulocytic lineage by all-trans retinoic acid or cyclic AMP analogs led to an increased expression of SERCAPLIM, whereas the expression of the SERCA 2b isoform was decreased. The modulation of SERCA expression was manifest also on the mRNA level. Experiments with retinoic acid receptor isoform-specific retinoids indicated that SERCA expression is modulated by retinoic acid receptor -dependent signaling. SERCA expression of retinoic acid-resistant cell variants was refractory to treatment. Differentiation along the monocyte/macrophage lineage by phorbol ester resulted in an increased expression of both SERCA isoforms. In addition, when cells were treated by phorbol ester in the presence of the glucocorticoid dexamethasone, a known inhibitor of monocyte differentiation, a selective blockage of the induction of SERCAPLIM was observed. Altered SERCA expression modified the functional characteristics of calcium transport into the endoplasmic reticulum. These observations show for the first time that the modulation of calcium pump expression is an integral component of the differentiation program of myeloid precursors and indicate that a lineage-specific remodelling of the endoplasmic reticulum occurs during cell maturation. In addition, these data show that SERCA isoforms may serve as useful markers for the study of myeloid differentiation.
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Launay, Sophie, Maurizio Giannı̀, Tünde Kovàcs, Raymonde Bredoux, Arlette Bruel, Pascal Gélébart, Fabien Zassadowski, Christine Chomienne, Jocelyne Enouf, and Béla Papp. "Lineage-Specific Modulation of Calcium Pump Expression During Myeloid Differentiation." Blood 93, no. 12 (June 15, 1999): 4395–405. http://dx.doi.org/10.1182/blood.v93.12.4395.412k06_4395_4405.
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Calcium is accumulated from the cytosol into the endoplasmic reticulum by sarco-endoplasmic reticulum calcium transport ATPase (SERCA) enzymes. Because calcium stored in the endoplasmic reticulum is essential for cell growth, differentiation, calcium signaling, and apoptosis and because different SERCA enzymes possess distinct functional characteristics, in the present report we explored SERCA expression during in vitro differentiation of the human myeloid/promyelocytic cell lines HL-60 and NB4 and of freshly isolated acute promyelocytic leukemia cells. Two SERCA species have been found to be coexpressed in these cells: SERCA 2b and another isoform, SERCAPLIM, which is recognized by the PLIM430 monoclonal antibody. Induction of differentiation along the neutrophil granulocytic lineage by all-trans retinoic acid or cyclic AMP analogs led to an increased expression of SERCAPLIM, whereas the expression of the SERCA 2b isoform was decreased. The modulation of SERCA expression was manifest also on the mRNA level. Experiments with retinoic acid receptor isoform-specific retinoids indicated that SERCA expression is modulated by retinoic acid receptor -dependent signaling. SERCA expression of retinoic acid-resistant cell variants was refractory to treatment. Differentiation along the monocyte/macrophage lineage by phorbol ester resulted in an increased expression of both SERCA isoforms. In addition, when cells were treated by phorbol ester in the presence of the glucocorticoid dexamethasone, a known inhibitor of monocyte differentiation, a selective blockage of the induction of SERCAPLIM was observed. Altered SERCA expression modified the functional characteristics of calcium transport into the endoplasmic reticulum. These observations show for the first time that the modulation of calcium pump expression is an integral component of the differentiation program of myeloid precursors and indicate that a lineage-specific remodelling of the endoplasmic reticulum occurs during cell maturation. In addition, these data show that SERCA isoforms may serve as useful markers for the study of myeloid differentiation.
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Aulestia, Francisco J., Pedro C. Redondo, Arancha Rodríguez-García, Juan A. Rosado, Ginés M. Salido, Maria Teresa Alonso, and Javier García-Sancho. "Two distinct calcium pools in the endoplasmic reticulum of HEK-293T cells." Biochemical Journal 435, no. 1 (March 15, 2011): 227–35. http://dx.doi.org/10.1042/bj20101427.
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Agonist-sensitive intracellular Ca2+ stores may be heterogeneous and exhibit distinct functional features. We have studied the properties of intracellular Ca2+ stores using targeted aequorins for selective measurements in different subcellular compartments. Both, HEK-293T [HEK (human embryonic kidney)-293 cells expressing the large T-antigen of SV40 (simian virus 40)] and HeLa cells accumulated Ca2+ into the ER (endoplasmic reticulum) to near millimolar concentrations and the IP3-generating agonists, carbachol and ATP, mobilized this Ca2+ pool. We find in HEK-293T, but not in HeLa cells, a distinct agonist-releasable Ca2+ pool insensitive to the SERCA (sarco/endoplasmic reticulum Ca2+ ATPase) inhibitor TBH [2,5-di-(t-butyl)-benzohydroquinone]. TG (thapsigargin) and CPA (cyclopiazonic acid) completely emptied this pool, whereas lysosomal disruption or manoeuvres collapsing endomembrane pH gradients did not. Our results indicate that SERCA3d is important for filling the TBH-resistant store as: (i) SERCA3d is more abundant in HEK-293T than in HeLa cells; (ii) the SERCA 3 ATPase activity of HEK-293T cells is not fully blocked by TBH; and (iii) the expression of SERCA3d in HeLa cells generated a TBH-resistant agonist-mobilizable compartment in the ER. Therefore the distribution of SERCA isoforms may originate the heterogeneity of the ER Ca2+ stores and this may be the basis for store specialization in diverse functions. This adds to recent evidence indicating that SERCA3 isoforms may subserve important physiological and pathophysiological mechanisms.
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Papp, Bela, Sophie Launay, Pascal Gélébart, Atousa Arbabian, Agnes Enyedi, Jean-Philippe Brouland, Edgardo D. Carosella, and Homa Adle-Biassette. "Endoplasmic Reticulum Calcium Pumps and Tumor Cell Differentiation." International Journal of Molecular Sciences 21, no. 9 (May 9, 2020): 3351. http://dx.doi.org/10.3390/ijms21093351.
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Endoplasmic reticulum (ER) calcium homeostasis plays an essential role in cellular calcium signaling, intra-ER protein chaperoning and maturation, as well as in the interaction of the ER with other organelles. Calcium is accumulated in the ER by sarco/endoplasmic reticulum calcium ATPases (SERCA enzymes) that generate by active, ATP-dependent transport, a several thousand-fold calcium ion concentration gradient between the cytosol (low nanomolar) and the ER lumen (high micromolar). SERCA enzymes are coded by three genes that by alternative splicing give rise to several isoforms, which can display isoform-specific calcium transport characteristics. SERCA expression levels and isoenzyme composition vary according to cell type, and this constitutes a mechanism whereby ER calcium homeostasis is adapted to the signaling and metabolic needs of the cell, depending on its phenotype, its state of activation and differentiation. As reviewed here, in several normal epithelial cell types including bronchial, mammary, gastric, colonic and choroid plexus epithelium, as well as in mature cells of hematopoietic origin such as pumps are simultaneously expressed, whereas in corresponding tumors and leukemias SERCA3 expression is selectively down-regulated. SERCA3 expression is restored during the pharmacologically induced differentiation of various cancer and leukemia cell types. SERCA3 is a useful marker for the study of cell differentiation, and the loss of SERCA3 expression constitutes a previously unrecognized example of the remodeling of calcium homeostasis in tumors.
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Gilchrist, James S. C., Chris Palahniuk, Bernard Abrenica, Penelope Rampersad, Mark Mutawe, and Tom Cook. "RyR1/SERCA1 cross-talk regulation of calcium transport in heavy sarcoplasmic reticulum vesicles." Canadian Journal of Physiology and Pharmacology 81, no. 3 (March 1, 2003): 220–33. http://dx.doi.org/10.1139/y03-035.
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We investigated the functional interdependence of sarco-endoplasmic reticulum Ca2+ ATPase isoform 1 and ryanodine receptor isoform 1 in heavy sarcoplasmic reticulum membranes by synchronous fluorescence determination of extravesicular Ca2+ transients and catalytic activity. Under conditions of dynamic Ca2+ exchange ATPase catalytic activity was well coordinated to ryanodine receptor activation/inactivation states. Ryanodine-induced activation of Ca2+ release channel leaks also produced marked ATPase activation in the absence of measurable increases in bulk free extra vesicular Ca2+. This suggested that Ca2+ pumps are highly sensitive to Ca2+ release channel leak status and potently buffer Ca2+ ions exiting cytoplasmic openings of ryanodine receptors. Conversely, ryanodine receptor activation was dependent on Ca2+-ATPase pump activity. Ryanodine receptor activation by cytosolic Ca2+ was (i) inversely proportional to luminal Ca2+ load and (ii) dependent upon the rate of presentation of cytosolic Ca2+. Progressive Ca2+ filling coincided with progressive loss of Ca2+ sequestration rates and at a threshold loading, ryanodine-induced Ca2+ release produced small transient reversals of catalytic activity. These data indicate that attainment of threshold luminal Ca2+ loads coordinates sensitization of Ca2+ release channels with autogenic inhibition of Ca2+ pumping. This suggests that Ca2+-dependent control of Ca2+ release in intact heavy sarcoplasmic reticulum membranes involves a Ca2+- mediated "cross-talk" between sarco-endoplasmic reticulum Ca2+ ATPase isoform1 and ryanodine receptor isoform 1.Key words: Ca2+, sarcoplasmic reticulum, RyR, SERCA, calsequestrin, ryanodine.
Dissertations / Theses on the topic "Sarco-endoplasmic calcium ATPase (SERCA)"
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Shaikh, Sana Ashfaque. "Regulation of the Sarco-endoplasmic Reticulum Calcium ATPase by Sarcolipin." The Ohio State University, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=osu1429539826.
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Britzolaki, Aikaterini. "Investigating Novel Sarco/Endoplasmic Reticulum Calcium ATPase (SERCA)-Dependent Mechanisms Involved In Mouse Behavior." University of Dayton / OhioLINK, 2021. http://rave.ohiolink.edu/etdc/view?acc_num=dayton1620209352630612.
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Li, Sen, and 李森. "Intracellular alkalinization induces cytosolic Ca2+ increases by inhibiting sarco/endoplasmic reticulum Ca2+-ATPase (SERCA)." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2011. http://hub.hku.hk/bib/B46940546.
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Campbell, Terry G. "Analysis of glycerol 3-phosphate dehydrogenase and sarco/endoplasmic reticulum calcium ion channel ATpase for use in deep metazoan phylogenetics." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002375.
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Ait, Ghezali Lamia. "Expression des pompes calcique de type SERCA dans l’épithélium du plexus choroïde normal et tumoral et au cours de la différenciation précoce des lymphocytes B." Thesis, Sorbonne Paris Cité, 2017. http://www.theses.fr/2017USPCD015/document.
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L’ion calcium est un second messager qui intervient dans de nombreux processuscellulaires dont la prolifération, la différenciation et l’apoptose. Ainsi, l’homéostasiecalcique constitue un point central de régulation de la signalisation cellulaire. En effet, laconcentration calcique cytosolique de calcium subit des oscillations, qui suivant leuramplitude ou leur fréquence, vont être capables d’activer spécifiquement certains facteursde transcription. La régulation de ces oscillations implique entre autres les ATPases de typeSERCA (Sarco/Endoplasmic Reticulum Calcium ATPase) qui accumulent le calcium dansle réticulum endoplasmique. L’objectif de ce travail de thèse a été l’étude des SERCAs aucours de la différenciation lymphocytaire B et dans l’épithélium du plexus choroïde ; ceci,afin de mieux comprendre le profil d’expression de ces pompes et les mécanismes derégulation impliqués.Au cours de la différenciation de lignées de leucémie aiguë lymphoblastique (LAL) nousavons observé que l’expression de l’isoforme SERCA2 restait stable ou augmentaitlégèrement alors que celle de l’isoforme SERCA3 était toujours fortement induite, pouvantatteindre des niveaux observés dans les cellules lymphoïdes matures. Nous avons égalementobservé que l’inhibition de l’activité des SERCAs altère la différenciation cellulaire qui estdépendante de la voie des PKC. Ces données indiquent que SERCA3 pourrait être utiliséecomme marqueur de la différenciation lymphocytaire B. Une régulation de l’expression desSERCAs a également été mise en évidence au cours de la différenciation de l’épithélium duplexus choroïde normal ou tumoral. SERCA3 est fortement exprimée dans l’épithéliumnormal, mais on retrouve une baisse ou une perte de son expression dans l’épithéliumtumoral, cette baisse est corrélée à la perte de la différenciation selon le grade des tumeurs.L’étude de l’expression des SERCAs dans les cellules primaires du plexus choroïde traitépar des agents cyto-différenciateurs (acides gras à chaîne courte), montre que ladifférenciation est associée à une surexpression de SERCA3. SERCA3 peut donc égalementêtre un marqueur de la différenciation de l’épithélium du plexus choroïde.L’ensemble de ce travail a montré que la différenciation cellulaire est associée à la régulationde protéines impliquées dans la régulation de l’homéostasie calcique : les SERCAs. On peutainsi proposer SERCA3 comme un nouveau marqueur phénotypique utile pour l’analyse dela différenciation du plexus choroïde normale et néoplasique, ainsi que pour celle de ladifférenciation lymphoïde pré-B leucémiqueCellular calcium is involved in a multitude of biological processes including thecontrol of cell proliferation, differentiation and programmed cell death, and constitutestherefore a keconcentration calcique cytosolique de calcium subit des oscillations, qui suivant leuramplitude ou leur fréquence, vont être capables d’activer spécifiquement certains facteursde transcription. La régulation de ces oscillations implique entre autres les ATPases de typeSERCA (Sarco/Endoplasmic Reticulum Calcium ATPase) qui accumulent le calcium dansle réticulum endoplasmique. L’objectif de ce travail de thèse a été l’étude des SERCAs aucours de la différenciation lymphocytaire B et dans l’épithélium du plexus choroïde ; ceci,afin de mieux comprendre le profil d’expression de ces pompes et les mécanismes derégulation impliqués.Au cours de la différenciation de lignées de leucémie aiguë lymphoblastique (LAL) nousavons observé que l’expression de l’isoforme SERCA2 restait stable ou augmentaitlégèrement alors que celle de l’isoforme SERCA3 était toujours fortement induite, pouvantatteindre des niveaux observés dans les cellules lymphoïdes matures. Nous avons égalementobservé que l’inhibition de l’activité des SERCAs altère la différenciation cellulaire qui estdépendante de la voie des PKC. Ces données indiquent que SERCA3 pourrait être utiliséey element in cell signaling. Calcium levels vary in a dynamic mannerdepending on the state of activation of the cell, and can display oscillations the amplitudeand frequency of which can convey specific signals to various transcription factors.Sarco/Endoplasmic Reticulum Calcium ATPases (SERCA enzymes) accumulate calciumfrom the cytosol into the endoplasmic reticulum (ER). By modulating the spatiotemporalcharacteristics of calcium signals and oscillations, SERCA pumps constitute an importantand unique point of control of calcium-dependent cell activation. In this work weinvestigated SERCA expression during early B lymphoid differentiation and in normal,tumoral and hyperplastic choroid plexus epithelial cells.We have shown that SERCA3 expression is markedly increased during thepharmacologically induced differentiation of immature B acute lymphoblastic leukemiacells, whereas the expression of the simultaneously expressed SERCA2 isoform is notmodified significantly. SERCA3 expression during this differentiation process can reachlevels observed in mature B lymphoid cells, and is dependent on the activation of proteinkinase C. Moreover, the direct pharmacological inhibition of SERCA-dependent calciumtransport interferes with the differentiation process.Our investigations on the choroid plexus show, that whereas SERCA3 is highly expressedin normal choroid plexus epithelium, expression is strongly decreased in benign choroidplexus tumors and is lost in carcinoma, whereas expression is retained in hyperplasia. Inaddition, treatment of primary normal choroid plexus epithelial cells by short chain fattyacid-type cell differentiation-inducing agents in vitro leads to the induction of SERCA3expression.Our observations when taken together indicate that ER calcium homeostasis is remodeledduring the differentiation of immature B lymphoid cells and in the choroid plexus due to theinduction of SERCA3 expression. We show that a cross-talk exists between SERCA functionand the control of differentiation in B cells, that SERCA3 constitutes a new phenotypicmarker for the study of early B cell differentiation, and that the lack of SERCA3 expressionmay be useful for the identification of choroid plexus tumors
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Ikeda, Yoshio. "A Calcium ATPase in Mosquito Larvae as a Putative Receptor for Cry Toxins." The Ohio State University, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=osu1367549657.
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Hadri, Lahouaria. "Régulation de l'expression et rôle de l'isoforme Ca 2+ -ATPase du réticulum sarco/endoplasmique de type 3, SERCA 3, dans les cellules endothéliales." Paris 11, 2005. http://www.theses.fr/2005PA114804.
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Nous avons analysé les mécanismes de régulation de la transcription du gène SERCA3 et sa modulation par le calcium, dans les cellules endothéliales. Nos résultats montrent que les facteurs de transcription Ets-1 et Sp1 sont indispensables à l'activation du gène et que son expression est modulée par l'histamine et donc par l'augmentation de la [Ca2+]i via son récepteur H1 et la voie de la calcineurine/NFAT. Le gène SERCA3 code par épissage alternatif en 3' six isoformes : SERCA3a, 3b. . . 3f. Dans les cellules endothéliales EA. Hy 926, SERCA3a, -3b et -3f sont exprimées mais elles ne sont pas colocalisées avec l'isoforme ubiquitaire SERCA2b. En effet, SERCA3a, l'isoforme majoritaire, est distribué dans tout le cytosol et au niveau des invaginations membranaires, alors que que SERCA2b et les autres isoformes ont une localisation plutôt périnucléaire. Des expériences d'immunoprécipitation montrent que SERCA3a est liée au complexe cavéoline-eNOS, dans la cellule endothéliale.
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Newton, Tom. "Targeting of the sarco endoplasmic reticulum calcium ATPase." Thesis, University of Southampton, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.274568.
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Lansdale, Nicholas. "Investigating the role of Sarco-Endoplasmic Reticulum Ca2+-ATPase (SERCA) in airway development." Thesis, University of Liverpool, 2013. http://livrepository.liverpool.ac.uk/12693/.
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Background: Disorders of lung development cause death and disability in the young and old: novel insights into developmental regulators can aid therapeutic strategies. The Ca2+ATPase SERCA, already implicated in asthma and cystic fibrosis, appears to play a key role in lung development. SERCA inhibition with cyclopiazonic acid (CPA) in vitro, reduces both airway branching and peristalsis reversibly and dose dependently, whilst also halting myogenesis. It is unclear however, whether changes in branching are mediated via SERCA dependent contractility, or whether SERCA is a direct regulator of airway branching. Aims: (i) to further explore the CPA-induced embryonic lung phenotype by assaying gene expression and cell proliferation; and (ii) to determine effects of genetic perturbation of SERCA function in vivo on airway branching morphogenesis, in the absence of contractility (using a Drosophila model). Methods: Embryonic mouse (E11.5) lung explants were cultured +/- CPA at an air/fluid interface. Standard techniques were used to rear Drosophila and SERCA expression manipulated using conditional, heat-sensitive mutants and RNAi targeted to the trachea. Positively labelled, loss-of-function ‘flip-out’ RNAi and mutant clones were produced using heat-shock induced FLP-recombinase. Gene expression was assayed using real-time RT-PCR and SERCA function assessed using calcium dyes and genetic indicators. Embryonic and larval fly airways were imaged using fluorescent proteins and immunostaining, with live or fixed-sample confocal microscopy. Immunofluorescent staining was used to assess protein expression and cell proliferation. Results: SERCA inhibition with CPA significantly up or down regulated mRNA levels of key genes involved in lung branching morphogenesis, myogenesis and angiogenesis in vitro. CPA treatment also reduced cell proliferation dose-dependently in the lung epithelium and mesenchyme. In the fly embryo, neither conditional SERCA mutants nor targeted RNAi significantly affected tracheal morphology. However, residual SERCA mRNA and protein function was evident at this stage of development. Tracheal maturation, in the form of gas filling was significantly impaired though, in embryos expressing a conditional SERCA mutation. In larvae, development of the dorsal air sac primordium (ASP) was severely disrupted by targeted SERCA RNAi and this phenotype could be reproduced when sufficient numbers of loss-of–function clones were present. SERCA inhibition reduced the number of mitotic cells in the ASP and correspondingly, SERCA deficient clones comprised fewer cells than control counterparts: SERCA regulation of airway cell proliferation was therefore evident across species. Fewer SERCA deficient cells reached the tip of the ASP during morphogenesis compared to controls, whereas a greater proportion remained in the stalk, findings that indicate a cell-autonomous defect in cell migration. Changes in morphology were independent of changes in expression of the key ASP signalling pathways MAP kinase and Notch. Expression of the ASP tip-cell marker escargot was expanded in SERCA deficient larvae, with a number of positive cells being abnormally present in the stalk. This finding could be explained by a failure of these cells to migrate to the tip, alternatively by changes in cell fate. Given key roles of tip cells in morphogenetic signalling, escargot may play a role in SERCA inhibition-induced dysmorphogenesis. Conclusions: SERCA has an essential, conserved role in airway branching morphogenesis across species: this role appears independent of contractility. SERCA regulates cell migration and proliferation processes in the airway, findings that may have wider relevance, e.g. in proliferative disease, metastasis and tissue regeneration. Given evidence in plants and fungi of Ca2+ cycling regulating budding, findings here may indicate a role for SERCA as a generic regulator of iterative branching across biology, with clear implications for further research.
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Djillani, Alaeddine. "Caractérisation des canaux calciques dans les polynucléaires neutrophiles : rôle dans la phagocytose et la production des radicaux libres oxygénés." Phd thesis, Université Paris Sud - Paris XI, 2013. http://tel.archives-ouvertes.fr/tel-01069097.
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Les polynucléaires neutrophiles représentent 50-70% des leucocytes sanguins et possèdent un rôle majeur dans la défense de l'organisme contre les pathogènes. Le Ca2+ est un second messager qui joue un rôle primordial dans le chimiotactisme, la phagocytose, la dégranulation et la production de formes réactives de l'oxygène (FRO) afin de neutraliser l'agent pathogène. Dans ces cellules, l'influx calcique de type SOCE est essentiel pour l'homéostasie calcique. Il est peu étudié en raison du manque d'outils pharmacologiques spécifiques d'où l'importance dans un premier temps de chercher de nouvelles molécules. Les cellules T Jurkat dont le SOCE est largement caractérisé servent de modèle pour la caractérisation initiale de ces molécules. Le 2-APB est parmi les molécules les plus largement utilisées dans la caractérisation du SOCE en raison de sa double activité sur le SOCE avec une potentialisation à [1-10 μM] et une inhibition à [> 20 μM]. En revanche, ce produit manque de spécificité et agit sur d'autres cibles cellulaires comme les récepteurs à l'inositol (1,4,5)-trisphosphate (InsP3Rs). La 1ère étape est de sélectionner à partir d'analogues commerciaux du 2-APB (Methoxy-APB, Dimethoxy-APB, Cyclic-APB, Benzothienyl-APB, Thienyl-APB et MDEB), des composés plus spécifiques et également plus efficaces que la molécule mère. Deux molécules se sont distinguées : le MDEB comme uniquement potentialisant du SOCE et le Benzothienyl-APB comme un puissant inhibiteur. En revanche, tous les analogues du 2-APB inhibent les InsP3Rs à l'exception du MDEB qui semble plus spécifique du SOCE. L'effet du MDEB sur le courant calcique, ICRAC, a été étudié grâce à la technique du patch-clamp. Il augmente d'environ 4 fois l'amplitude de ICRAC par rapport à celle enregistrée dans les cellules contrôle. Par ailleurs, le MDEB ralentie l'inactivation rapide de ICRAC due au Ca2+. Sur le plan physiologique, le MDEB à des concentrations croissantes inhibe la synthèse de l'IL-2 dans les cellules Jurkat stimulées et ceci malgré son effet potentialisant du SOCE. Cette activité est liée à son effet pro-apoptotique dans les cellules Jurkat stimulées. Le MDEB et le Benzothienyl-APB caractérisés dans la 1ère partie nous ont servi d'outils potentiels afin d'étudier le SOCE des cellules PLB-985 différenciées en cellules proches de neutrophiles. Le SOCE a été induit soit par un traitement des cellules avec la thapsigargine (Tg) soit de manière physiologique avec les peptides fMLF et le WKYMVm deux chimioattractants, ligands des récepteurs aux peptides formylés FPR et FPRL1 respectivement. En plus, le SOCE induit par la Tg est modulable par le 2-APB, potentialisé par le MDEB et inhibé par le Benzothienyl-APB. La phagocytose des levures par les cellules PLB-985 différenciées ainsi que la production de FRO intraphagosomales ont été inhibées par le MDEB et le Benzothienyl-APB. Les FRO extracellulaires ont été également inhibées par Benzothienyl-APB en revanche à cause de la forte interférence du MDEB avec la technique de mesure nous n'avons pas pu étudier ses activités. En conclusion, le MDEB et le Benzothienyl-APB sont de nouveaux outils pharmacologiques potentialisant ou inhibant le SOCE des leucocytes, qui nous permettront dans l'avenir une meilleure compréhension de l'entrée calcique et ses rôles dans ces cellules.
Book chapters on the topic "Sarco-endoplasmic calcium ATPase (SERCA)"
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Zanotti, Giuseppe. "The Ca2+ ATPase of the Sarco-/Endoplasmic Reticulum (SERCA): Structure and Control." In Regulation of Ca2+-ATPases,V-ATPases and F-ATPases, 137–51. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-24780-9_9.
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Fajmut, Aleš. "Molecular Mechanisms and Targets of Cyclic Guanosine Monophosphate (cGMP) in Vascular Smooth Muscles." In Muscle Cell and Tissue - Novel Molecular Targets and Current Advances [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97708.
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Molecular mechanisms and targets of cyclic guanosine monophosphate (cGMP) accounting for vascular smooth muscles (VSM) contractility are reviewed. Mathematical models of five published mechanisms are presented, and four novel mechanisms are proposed. cGMP, which is primarily produced by the nitric oxide (NO) dependent soluble guanylate cyclase (sGC), activates cGMP-dependent protein kinase (PKG). The NO/cGMP/PKG signaling pathway targets are the mechanisms that regulate cytosolic calcium ([Ca2+]i) signaling and those implicated in the Ca2+-desensitization of the contractile apparatus. In addition to previous mathematical models of cGMP-mediated molecular mechanisms targeting [Ca2+]i regulation, such as large-conductance Ca2+-activated K+ channels (BKCa), Ca2+-dependent Cl− channels (ClCa), Na+/Ca2+ exchanger (NCX), Na+/K+/Cl− cotransport (NKCC), and Na+/K+-ATPase (NKA), other four novel mechanisms are proposed here based on the existing but perhaps overlooked experimental results. These are the effects of cGMP on the sarco−/endo- plasmic reticulum Ca2+-ATPase (SERCA), the plasma membrane Ca2+-ATPase (PMCA), the inositol 1,4,5-trisphosphate (IP3) receptor channels type 1 (IP3R1), and on the myosin light chain phosphatase (MLCP), which is implicated in the Ca2+-desensitization. Different modeling approaches are presented and discussed, and novel model descriptions are proposed.
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Adachi, Takeshi. "Modulation of Vascular Sarco/Endoplasmic Reticulum Calcium ATPase in Cardiovascular Pathophysiology." In Cardiovascular Pharmacology - Heart and Circulation, 165–95. Elsevier, 2010. http://dx.doi.org/10.1016/s1054-3589(10)59006-9.
Full textConference papers on the topic "Sarco-endoplasmic calcium ATPase (SERCA)"
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Sheikh, Abdul Q., Jennifer R. Hurley, and Daria A. Narmoneva. "Diabetes Alters Intracellular Calcium Transients in Cardiac Endothelial Cells." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53797.
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Diabetic cardiomyopathy (DCM) is a serious diabetes-associated complication that results in myocardial dysfunction independent of other etiological factors [1]. Pathological alterations to the myocardium associated with DCM include circulatory defects, impaired heart muscle contraction, and abnormal calcium (Ca2+) homeostasis in cardiac cells[2]. In myocardium, endothelial cells play an essential role in maintaining intracellular Ca2+ hemostasis in response to stimuli and regulating cardiac function [3]. External stimulus may cause abrupt changes in Ca2+ balance, including Ca2+ release from sarco-endoplasmic reticulum (ER) [4]. Subsequent return of the Ca2+ level to basal levels occurs due to Ca2+ decay mechanism, which is mainly regulated by sarco-endoplasmic reticulum Ca2+ ATPase pumps (SERCA) present at ER membrane which are responsible for Ca2+ sequestration [5]. Studies have shown that the mechanisms by which Ca2+ homeostasis alters cardiac function in diabetic cardiomyocytes include reduced activity of the SERCA pumps [6]. However, no information is available regarding the effects of diabetes on Ca2+ hemostasis and the underlying Ca2+ sequestration mechanism in diabetic cardiac endothelial cells[7]. This study tested the hypothesis that diabetic endothelial cells will exhibit disruptions in Ca2+ decay kinetics via alterations in the sequestration mechanism.
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Hirst, Stuart J., Sarah Preston, Joanne L. Van Der Velden, Kenneth J. Snibson, Els N. Meeusen, and Robert J. Bischof. "Sarco/endoplasmic Reticulum Ca2+ ATPase (SERCA) Inhibition Prevents Airway Smooth Muscle Proliferation." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2300.
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Lansdale, Nick, Marilyn G. Connell, Neil C. Featherstone, Angela Midgley, and Edwin C. Jesudason. "Cyclopiazonic Acid (CPA) Inhibition Of Sarco-Endoplasmic Reticulum Ca2+-ATPase (SERCA) Reduces, With Similar Dose-dependency, Prenatal Airway Branching, Peristalsis And Cell Proliferation And Modulates Gene Expression Required For Lung Development." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a4140.
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