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Journal articles on the topic 'NCX3'

Author: Grafiati

Published: 4 June 2021

Last updated: 3 February 2022

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1

Iwamoto, Takahiro, and Munekazu Shigekawa. "Differential inhibition of Na+/Ca2+exchanger isoforms by divalent cations and isothiourea derivative." American Journal of Physiology-Cell Physiology 275, no. 2 (August 1, 1998): C423—C430. http://dx.doi.org/10.1152/ajpcell.1998.275.2.c423.

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We compared the properties of three mammalian Na+/Ca2+exchanger isoforms, NCX1, NCX2, and NCX3, by analyzing the effects of Ni2+ and other cations as well as the recently identified inhibitor isothiourea derivatives on intracellular Na+-dependent45Ca2+uptake into CCL-39 (Dede) fibroblasts stably expressing each isoform. All these NCX isoforms had similar affinities for the extracellular transport substrates Ca2+ and Na+. Ni2+ inhibited45Ca2+uptake by competing with Ca2+ for the external transport site, with 10-fold less affinity in NCX3 than in NCX1 or NCX2. Ni2+ and Co2+ were most efficient i

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Boscia, Francesca, Rosaria Gala, Giuseppe Pignataro, Andrea de Bartolomeis, Maria Cicale, Alberto Ambesi-Impiombato, Gianfranco Di Renzo, and Lucio Annunziato. "Permanent Focal Brain Ischemia Induces Isoform-Dependent Changes in the Pattern of Na+/Ca2+ Exchanger Gene Expression in the Ischemic Core, Periinfarct Area, and Intact Brain Regions." Journal of Cerebral Blood Flow & Metabolism 26, no. 4 (August 17, 2005): 502–17. http://dx.doi.org/10.1038/sj.jcbfm.9600207.

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Dysregulation of sodium [Na+]i and calcium [Ca2+]i homeostasis plays a pivotal role in the pathophysiology of cerebral ischemia. Three gene products of the sodium–calcium exchanger family NCX1, NCX2, and NCX3 couple, in a bidirectional way, the movement of these ions across the cell membrane during cerebral ischemia. Each isoform displays a selective distribution in the rat brain. To determine whether NCX gene expression can be regulated after cerebral ischemia, we used NCX isoform-specific antisense radiolabeled probes to analyze, by radioactive in situ hybridization histochemistry, the patte

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3

Marshall, Christian R., Joanne A. Fox, Stefanie L. Butland, B. F. Francis Ouellette, Fiona S. L. Brinkman, and Glen F. Tibbits. "Phylogeny of Na+/Ca2+ exchanger (NCX) genes from genomic data identifies new gene duplications and a new family member in fish species." Physiological Genomics 21, no. 2 (April 14, 2005): 161–73. http://dx.doi.org/10.1152/physiolgenomics.00286.2004.

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The Na+/Ca2+ exchanger (NCX) is a member of the cation/Ca2+ antiporter (CaCA) family and plays a key role in maintaining cellular Ca2+ homeostasis in a variety of cell types. NCX is present in a diverse group of organisms and exhibits high overall identity across species. To date, three separate genes, i.e., NCX1, NCX2, and NCX3, have been identified in mammals. However, phylogenetic analysis of the exchanger has been hindered by the lack of nonmammalian NCX sequences. In this study, we expand and diversify the list of NCX sequences by identifying NCX homologs from whole-genome sequences acces

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4

Pignataro, Giuseppe, Elga Esposito, Ornella Cuomo, Rossana Sirabella, Francesca Boscia, Natascia Guida, Gianfranco Di Renzo, and Lucio Annunziato. "The NCX3 Isoform of the Na+/Ca2+ Exchanger Contributes to Neuroprotection Elicited by Ischemic Postconditioning." Journal of Cerebral Blood Flow & Metabolism 31, no. 1 (July 14, 2010): 362–70. http://dx.doi.org/10.1038/jcbfm.2010.100.

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It has been recently shown that a short sublethal brain ischemia subsequent to a prolonged harmful ischemic episode may confer ischemic neuroprotection, a phenomenon termed ischemic postconditioning. Na+/Ca2+ exchanger (NCX) isoforms, NCX1, NCX2, and NCX3, are plasma membrane ionic transporters widely distributed in the brain and involved in the control of Na+ and Ca2+ homeostasis and in the progression of stroke damage. The objective of this study was to evaluate the role of these three proteins in the postconditioning-induced neuroprotection. The NCX protein and mRNA expression was evaluated

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5

Quednau, B. D., D. A. Nicoll, and K. D. Philipson. "Tissue specificity and alternative splicing of the Na+/Ca2+ exchanger isoforms NCX1, NCX2, and NCX3 in rat." American Journal of Physiology-Cell Physiology 272, no. 4 (April 1, 1997): C1250—C1261. http://dx.doi.org/10.1152/ajpcell.1997.272.4.c1250.

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The gene coding for the Na+/Ca2+ exchanger NCX1 is characterized by a cluster of six exons (A, B, C, D, E, and F) coding for a variable region in the COOH terminus of the large intracellular loop of the protein. Alternative splicing of these exons generates multiple tissue-specific variants of NCX1. Using reverse transcriptase-polymerase chain reaction, we analyzed eight previously described and four new splicing isoforms of NCX1 in a wide variety of tissues and cells. Exons A and B are mutually exclusive, as shown in earlier studies, and splicing isoforms containing exon A are preferentially

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6

Molinaro, Pasquale, Rossana Sirabella, Giuseppe Pignataro, Tiziana Petrozziello, Agnese Secondo, Francesca Boscia, Antonio Vinciguerra, et al. "Neuronal NCX1 overexpression induces stroke resistance while knockout induces vulnerability via Akt." Journal of Cerebral Blood Flow & Metabolism 36, no. 10 (July 22, 2016): 1790–803. http://dx.doi.org/10.1177/0271678x15611913.

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Three different Na+/Ca2+ exchanger (NCX) isoforms, NCX1, NCX2, and NCX3, are expressed in brain where they play a relevant role in maintaining Na+ and Ca2+ homeostasis. Although the neuroprotective roles of NCX2 and NCX3 in stroke have been elucidated, the relevance of NCX1 is still unknown because of embryonic lethality of its knocking-out, heart dysfunctions when it is overexpressed, and the lack of selectivity in currently available drugs. To overcome these limitations we generated two conditional genetically modified mice that upon tamoxifen administration showed a selective decrease or in

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7

Fraysse, Bodvaël, Thierry Rouaud, Marie Millour, Josiane Fontaine-Pérus, Marie-France Gardahaut, and Dmitri O. Levitsky. "Expression of the Na+/Ca2+exchanger in skeletal muscle." American Journal of Physiology-Cell Physiology 280, no. 1 (January 1, 2001): C146—C154. http://dx.doi.org/10.1152/ajpcell.2001.280.1.c146.

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The expression of the Na+/Ca2+ exchanger was studied in differentiating muscle fibers in rats. NCX1 and NCX3 isoform (Na+/Ca2+ exchanger isoform) expression was found to be developmentally regulated. NCX1 mRNA and protein levels peaked shortly after birth. Conversely, NCX3 isoform expression was very low in muscles of newborn rats but increased dramatically during the first 2 wk of postnatal life. Immunocytochemical analysis showed that NCX1 was uniformly distributed along the sarcolemmal membrane of undifferentiated rat muscle fibers but formed clusters in T-tubular membranes and sarcolemma o

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8

Linck, Bettina, Zhiyong Qiu, Zhaoping He, Qiusheng Tong, Donald W. Hilgemann, and Kenneth D. Philipson. "Functional comparison of the three isoforms of the Na+/Ca2+ exchanger (NCX1, NCX2, NCX3)." American Journal of Physiology-Cell Physiology 274, no. 2 (February 1, 1998): C415—C423. http://dx.doi.org/10.1152/ajpcell.1998.274.2.c415.

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Three distinct mammalian Na+/Ca2+exchangers have been cloned: NCX1, NCX2, and NCX3. We have undertaken a detailed functional comparison of these three exchangers. Each exchanger was stably expressed at high levels in the plasma membranes of BHK cells. Na+/Ca2+exchange activity was assessed using three different complementary techniques: Na+ gradient-dependent45Ca2+uptake into intact cells, Na+gradient-dependent45Ca2+uptake into membrane vesicles isolated from the transfected cells, and exchange currents measured using giant patches of excised cell membrane. Apparent affinities for the transpor

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9

Iwamoto, Takahiro, Tomoe Nishitani, and Munekazu Shigekawa. "Pharmacological characterization of Na+/Ca2+ exchanger isoforms (NCX1, NCX2, NCX3)." Japanese Journal of Pharmacology 76 (1998): 110. http://dx.doi.org/10.1016/s0021-5198(19)40559-3.

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10

POLUMURI, S. K., A. RUKNUDIN, MARGARET M. McCARTHY, TARA S. PERROT-SINAL, and D. H. SCHULZE. "Sodium-Calcium Exchanger NCX1, NCX2, and NCX3 Transcripts in Developing Rat Brain." Annals of the New York Academy of Sciences 976, no. 1 (January 24, 2006): 60–63. http://dx.doi.org/10.1111/j.1749-6632.2002.tb04714.x.

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11

Kemény, Lajos V., Andrea Schnúr, Mátyás Czepán, Zoltán Rakonczay, Eleonóra Gál, János Lonovics, György Lázár, et al. "Na+/Ca2+ exchangers regulate the migration and proliferation of human gastric myofibroblasts." American Journal of Physiology-Gastrointestinal and Liver Physiology 305, no. 8 (October 15, 2013): G552—G563. http://dx.doi.org/10.1152/ajpgi.00394.2012.

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Gastrointestinal myofibroblasts are contractile, electrically nonexcitable, transitional cells that play a role in extracellular matrix production, in ulcer healing, and in pathophysiological conditions they contribute to chronic inflammation and tumor development. Na+/Ca2+ exchangers (NCX) are known to have a crucial role in Ca2+ homeostasis of contractile cells, however, no information is available concerning the role of NCX in the proliferation and migration of gastrointestinal myofibroblasts. In this study, our aim was to investigate the role of NCX in the Ca2+ homeostasis, migration, and

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12

Nicholas, Susanne B., and Kenneth D. Philipson. "Cardiac expression of the Na+/Ca2+exchanger NCX1 is GATA factor dependent." American Journal of Physiology-Heart and Circulatory Physiology 277, no. 1 (July 1, 1999): H324—H330. http://dx.doi.org/10.1152/ajpheart.1999.277.1.h324.

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The cardiac sarcolemmal Na+/Ca2+exchanger plays a primary role in Ca2+ efflux and is important in regulating intracellular Ca2+ and beat-to-beat contractility. Of the three Na+/Ca2+exchanger genes cloned (NCX1, NCX2, and NCX3), only NCX1 is expressed in cardiac myocytes. NCX1 has alternative promoters for heart, kidney, and brain tissue-specific transcripts. Analysis of the cardiac NCX1 promoter (at −336 bp) identified a cardiac-specific minimum promoter (at −137) and two GATA sites (at −75 and −145). In this study, gel shift and supershift analyses identified GATA-4 in primary neonatal cardia

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13

Secondo, Agnese, Pasquale Molinaro, Anna Pannaccione, Alba Esposito, Maria Cantile, Pellegrino Lippiello, Rossana Sirabella, Takahiro Iwamoto, Gianfranco Di Renzo, and Lucio Annunziato. "Nitric Oxide Stimulates NCX1 and NCX2 but Inhibits NCX3 Isoform by Three Distinct Molecular Determinants." Molecular Pharmacology 79, no. 3 (December 15, 2010): 558–68. http://dx.doi.org/10.1124/mol.110.069658.

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14

ANNUNZIATO, L., G. PIGNATARO, F. BOSCIA, R. SIRABELLA, L. FORMISANO, M. SAGGESE, O. CUOMO, et al. "ncx1, ncx2, and ncx3 Gene Product Expression and Function in Neuronal Anoxia and Brain Ischemia." Annals of the New York Academy of Sciences 1099, no. 1 (February 15, 2007): 413–26. http://dx.doi.org/10.1196/annals.1387.050.

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15

Lytton, Jonathan. "Na+/Ca2+ exchangers: three mammalian gene families control Ca2+ transport." Biochemical Journal 406, no. 3 (August 29, 2007): 365–82. http://dx.doi.org/10.1042/bj20070619.

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Mammalian Na+/Ca2+ exchangers are members of three branches of a much larger family of transport proteins [the CaCA (Ca2+/cation antiporter) superfamily] whose main role is to provide control of Ca2+ flux across the plasma membranes or intracellular compartments. Since cytosolic levels of Ca2+ are much lower than those found extracellularly or in sequestered stores, the major function of Na+/Ca2+ exchangers is to extrude Ca2+ from the cytoplasm. The exchangers are, however, fully reversible and thus, under special conditions of subcellular localization and compartmentalized ion gradients, Na+/

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16

Formisano, Luigi, Giusy Laudati, Natascia Guida, Luigi Mascolo, Angelo Serani, Ornella Cuomo, Maria Cantile, et al. "HDAC4 and HDAC5 form a complex with DREAM that epigenetically down-regulates NCX3 gene and its pharmacological inhibition reduces neuronal stroke damage." Journal of Cerebral Blood Flow & Metabolism 40, no. 10 (November 7, 2019): 2081–97. http://dx.doi.org/10.1177/0271678x19884742.

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The histone deacetylases (HDACs)-dependent mechanisms regulating gene transcription of the Na+/Ca+ exchanger isoform 3 ( ncx3) after stroke are still unknown. Overexpression or knocking-down of HDAC4/HDAC5 down-regulates or increases, respectively, NCX3 mRNA and protein. Likewise, MC1568 (class IIa HDACs inhibitor), but not MS-275 (class I HDACs inhibitor) increased NCX3 promoter activity, gene and protein expression. Furthermore, HDAC4 and HDAC5 physically interacted with the transcription factor downstream regulatory element antagonist modulator (DREAM). As MC1568, DREAM knocking-down preven

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17

Thurneysen, Thomas, Debora A. Nicoll, Kenneth D. Philipson, and Hartmut Porzig. "Sodium/calcium exchanger subtypes NCX1, NCX2 and NCX3 show cell-specific expression in rat hippocampus cultures." Molecular Brain Research 107, no. 2 (November 2002): 145–56. http://dx.doi.org/10.1016/s0169-328x(02)00461-8.

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18

Solís-Garrido, Luisa M., Antonio J. Pintado, Eva Andrés-Mateos, María Figueroa, Carlos Matute, and Carmen Montiel. "Cross-talk between Native Plasmalemmal Na+/Ca2+Exchanger and Inositol 1,4,5-Trisphosphate-sensitive Ca2+Internal Store inXenopusOocytes." Journal of Biological Chemistry 279, no. 50 (September 16, 2004): 52414–24. http://dx.doi.org/10.1074/jbc.m408872200.

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Because the presence of a native plasmalemmal Na+/Ca2+exchange (NCX) activity inXenopus laevisoocytes remains controversial, its possible functional role in these cells is poorly understood. Here, in experiments on control oocytes and oocytes overexpressing a cloned NCX1 cardiac protein, confocal microscopy combined with electrophysiological techniques reveal that these cells express an endogenous NCX protein forming a functional microdomain with inositol 1,4,5-trisphosphate receptors (InsP3R) that controls intracellular Ca2+in a restricted subplasmalemmal space. The following data obtained in

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19

Lu, Jing, Xiao-Yong Tong, and Xiao-Liang Wang. "Altered gene expression of Na+/Ca2+ exchanger isoforms NCX1, NCX2 and NCX3 in chronic ischemic rat brain." Neuroscience Letters 332, no. 1 (October 2002): 21–24. http://dx.doi.org/10.1016/s0304-3940(02)00905-9.

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20

Formisano, Luigi, Natascia Guida, Luigi Mascolo, Angelo Serani, Giusy Laudati, Vincenzo Pizzorusso, and Lucio Annunziato. "Transcriptional and epigenetic regulation of ncx1 and ncx3 in the brain." Cell Calcium 87 (May 2020): 102194. http://dx.doi.org/10.1016/j.ceca.2020.102194.

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21

Pignataro, Giuseppe, Francesca Boscia, Elga Esposito, Rossana Sirabella, Ornella Cuomo, Antonio Vinciguerra, Gianfranco Di Renzo, and Lucio Annunziato. "NCX1 and NCX3: Two new effectors of delayed preconditioning in brain ischemia." Neurobiology of Disease 45, no. 1 (January 2012): 616–23. http://dx.doi.org/10.1016/j.nbd.2011.10.007.

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22

Pelzl, Lisann, Zohreh Hosseinzadeh, Tamer al-Maghout, Yogesh Singh, Itishri Sahu, Rosi Bissinger, Sebastian Schmidt, et al. "Role of Na+/Ca2+ Exchangers in Therapy Resistance of Medulloblastoma Cells." Cellular Physiology and Biochemistry 42, no. 3 (2017): 1240–51. http://dx.doi.org/10.1159/000478953.

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Background/Aims: Alterations of cytosolic Ca2+-activity ([Ca2+]i) are decisive in the regulation of tumor cell proliferation, migration and survival. Transport processes participating in the regulation of [Ca2+]i include Ca2+ extrusion through K+-independent (NCX) and/or K+-dependent (NCKX) Na+/Ca2+-exchangers. The present study thus explored whether medulloblastoma cells express Na+/Ca2+-exchangers, whether expression differs between therapy sensitive D283 and therapy resistant UW228-3 medulloblastoma cells, and whether Na+/Ca2+-exchangers participate in the regulation of cell survival. Metho

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23

CANITANO, ADRIANA, MICHELE PAPA, FRANCESCA BOSCIA, PASQUALINA CASTALDO, STEFANIA SELLITTI, MAURIZIO TAGLIALATELA, and LUCIO ANNUNZIATO. "Brain Distribution of the Na+/Ca2+ Exchanger-Encoding Genes NCX1, NCX2, and NCX3 and Their Related Proteins in the Central Nervous System." Annals of the New York Academy of Sciences 976, no. 1 (January 24, 2006): 394–404. http://dx.doi.org/10.1111/j.1749-6632.2002.tb04766.x.

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24

Minelli, Andrea, Pasqualina Castaldo, Pietro Gobbi, Sara Salucci, Simona Magi, and Salvatore Amoroso. "Cellular and subcellular localization of Na+–Ca2+ exchanger protein isoforms, NCX1, NCX2, and NCX3 in cerebral cortex and hippocampus of adult rat." Cell Calcium 41, no. 3 (March 2007): 221–34. http://dx.doi.org/10.1016/j.ceca.2006.06.004.

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25

Sokolow, Sophie, Sanh H. Luu, Alison J. Headley, Alecia Y. Hanson, Taeree Kim, Carol A. Miller, Harry V. Vinters, and Karen H. Gylys. "High levels of synaptosomal Na+–Ca2+ exchangers (NCX1, NCX2, NCX3) co-localized with amyloid-beta in human cerebral cortex affected by Alzheimer's disease." Cell Calcium 49, no. 4 (April 2011): 208–16. http://dx.doi.org/10.1016/j.ceca.2010.12.008.

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26

Heise, Nicole, Ekaterina Shumilina, Meerim K. Nurbaeva, Evi Schmid, Kalina Szteyn, Wenting Yang, Nguyen Thi Xuan, et al. "Effect of dexamethasone on Na+/Ca2+exchanger in dendritic cells." American Journal of Physiology-Cell Physiology 300, no. 6 (June 2011): C1306—C1313. http://dx.doi.org/10.1152/ajpcell.00396.2010.

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Ca+-dependent signaling regulates the function of dendritic cells (DCs), antigen-presenting cells linking innate and adaptive immunity. The activity of DCs is suppressed by glucocorticoids, potent immunosuppressive hormones. The present study explored whether the glucocorticoid dexamethasone influences the cytosolic Ca2+concentration ([Ca2+]i) in DCs. To this end, DCs were isolated from mouse bone marrow. According to fura-2 fluorescence, exposure of DCs to lipopolysaccharide (LPS, 100 ng/ml) increased [Ca2+]i, an effect significantly blunted by overnight incubation with 10 nM dexamethasone be

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27

Bojarski, Christina, Bruno P. Meloni, Stephen R. Moore, Bernadette T. Majda, and Neville W. Knuckey. "Na+/Ca2+ exchanger subtype (NCX1, NCX2, NCX3) protein expression in the rat hippocampus following 3 min and 8 min durations of global cerebral ischemia." Brain Research 1189 (January 2008): 198–202. http://dx.doi.org/10.1016/j.brainres.2007.10.065.

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28

Blaustein, Mordecai P., and W. Jonathan Lederer. "Sodium/Calcium Exchange: Its Physiological Implications." Physiological Reviews 79, no. 3 (July 1, 1999): 763–854. http://dx.doi.org/10.1152/physrev.1999.79.3.763.

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The Na+/Ca2+exchanger, an ion transport protein, is expressed in the plasma membrane (PM) of virtually all animal cells. It extrudes Ca2+in parallel with the PM ATP-driven Ca2+pump. As a reversible transporter, it also mediates Ca2+entry in parallel with various ion channels. The energy for net Ca2+transport by the Na+/Ca2+exchanger and its direction depend on the Na+, Ca2+, and K+gradients across the PM, the membrane potential, and the transport stoichiometry. In most cells, three Na+are exchanged for one Ca2+. In vertebrate photoreceptors, some neurons, and certain other cells, K+is transpor

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29

Stains, Joseph P., Janet A. Weber, and Carol V. Gay. "Expression of Na+/Ca2+ exchanger isoforms (NCX1 and NCX3) and plasma membrane Ca2+ ATPase during osteoblast differentiation." Journal of Cellular Biochemistry 84, no. 3 (2002): 625–35. http://dx.doi.org/10.1002/jcb.10050.

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30

Secondo, Agnese, Rosaria Ilaria Staiano, Antonella Scorziello, Rossana Sirabella, Francesca Boscia, Annagrazia Adornetto, Valeria Valsecchi, et al. "BHK cells transfected with NCX3 are more resistant to hypoxia followed by reoxygenation than those transfected with NCX1 and NCX2: Possible relationship with mitochondrial membrane potential." Cell Calcium 42, no. 6 (December 2007): 521–35. http://dx.doi.org/10.1016/j.ceca.2007.01.006.

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31

Nicoll, Debora A., Beate D. Quednau, Zhiyong Qui, Yu-Rong Xia, Aldons J. Lusis, and Kenneth D. Philipson. "Cloning of a Third Mammalian Na+-Ca2+Exchanger, NCX3." Journal of Biological Chemistry 271, no. 40 (October 4, 1996): 24914–21. http://dx.doi.org/10.1074/jbc.271.40.24914.

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32

Wang, Yi-Chi, Ya-Shuan Chen, Ruo-Ciao Cheng, and Rong-Chi Huang. "Role of Na+/Ca2+ exchanger in Ca2+ homeostasis in rat suprachiasmatic nucleus neurons." Journal of Neurophysiology 113, no. 7 (April 2015): 2114–26. http://dx.doi.org/10.1152/jn.00404.2014.

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Intracellular Ca2+ is critical to the central clock of the suprachiasmatic nucleus (SCN). However, the role of Na+/Ca2+ exchanger (NCX) in intracellular Ca2+ concentration ([Ca2+]i) homeostasis in the SCN is unknown. Here we show that NCX is an important mechanism for somatic Ca2+ clearance in SCN neurons. In control conditions Na+-free solution lowered [Ca2+]i by inhibiting TTX-sensitive as well as nimodipine-sensitive Ca2+ influx. With use of the Na+ ionophore monensin to raise intracellular Na+ concentration ([Na+]i), Na+-free solution provoked rapid Ca2+ uptake via reverse NCX. The peak am

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33

Sirabella, Rossana, Agnese Secondo, Anna Pannaccione, Pasquale Molinaro, Luigi Formisano, Natascia Guida, Gianfranco Di Renzo, Lucio Annunziato, and Mauro Cataldi. "ERK1/2, p38, and JNK regulate the expression and the activity of the three isoforms of the Na+/Ca2+exchanger, NCX1, NCX2, and NCX3, in neuronal PC12 cells." Journal of Neurochemistry 122, no. 5 (July 11, 2012): 911–22. http://dx.doi.org/10.1111/j.1471-4159.2012.07838.x.

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34

Iwamoto, Takahiro, Yan Pan, Tomoe Y. Nakamura, Shigeo Wakabayashi, and Munekazu Shigekawa. "Protein Kinase C-Dependent Regulation of Na+/Ca2+Exchanger Isoforms NCX1 and NCX3 Does Not Require Their Direct Phosphorylation†." Biochemistry 37, no. 49 (December 1998): 17230–38. http://dx.doi.org/10.1021/bi981521q.

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35

Lariccia, Vincenzo, and Salvatore Amoroso. "Calcium- and ATP-dependent regulation of Na/Ca exchange function in BHK cells: Comparison of NCX1 and NCX3 exchangers." Cell Calcium 73 (July 2018): 95–103. http://dx.doi.org/10.1016/j.ceca.2018.04.007.

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36

Pignataro, Giuseppe, Francesca Boscia, Elga Esposito, Rossana Sirabella, Ornella Cuomo, Antonio Vinciguerra, Gianfranco Di Renzo, and Lucio Annunziato. "Corrigendum to “NCX1 and NCX3: Two new effectors of delayed preconditioning in brain ischemia” [Neurobiol. Dis. 45 (2012) 616–623]." Neurobiology of Disease 98 (February 2017): 160–61. http://dx.doi.org/10.1016/j.nbd.2016.12.002.

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37

Cross, Jane L., Bruno P. Meloni, Anthony J. Bakker, Sophie Sokolow, André Herchuelz, Stéphane Schurmans, and Neville W. Knuckey. "Neuronal injury in NCX3 knockout mice following permanent focal cerebral ischemia and in NCX3 knockout cortical neuronal cultures following oxygen-glucose deprivation and glutamate exposure." Journal of Experimental Stroke and Translational Medicine 2, no. 1 (January 2009): 3–9. http://dx.doi.org/10.6030/1939-067x-2.1.3.

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38

Sakai, Yasushi, Hiroki Kinoshita, Keiichirou Saitou, Ikuo Homma, Koji Nobe, and Takahiro Iwamoto. "Functional differences of Na+/Ca2+ exchanger expression in Ca2+ transport system of smooth muscle of guinea pig stomach." Canadian Journal of Physiology and Pharmacology 83, no. 8-9 (August 1, 2005): 791–97. http://dx.doi.org/10.1139/y05-079.

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The plasma membrane ATP-dependent Ca2+ pump and the Na+/Ca2+ exchanger (NCX) are the major means of Ca2+ extrusion in smooth muscle. However, little is known regarding distribution and function of the NCX in guinea pig gastric smooth muscle. The expression pattern and distribution of NCX isoforms suggest a role as a regulator of Ca2+ transport in cells. Na+ pump inhibition and the consequent to removal of K+ caused gradual contraction in fundus. In contrast, the response was significantly less in antrum. Western blotting analysis revealed that NCX1 and NCX2 are the predominant NCX isoforms exp

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39

Yang, H., and E. B. Jeung. "99 THE DIFFERENTIAL EXPRESSION OF CALCIUM-RELATED PROTEINS BY HYPOXIC STRESS IN THE DUODENUM, KIDNEY, AND PLACENTA OF PREGNANT RATS." Reproduction, Fertility and Development 25, no. 1 (2013): 197. http://dx.doi.org/10.1071/rdv25n1ab99.

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Preeclampsia is a pregnancy-specific disease characterized by the de novo development of concurrent hypertension, proteinuria, and oxidative stress in placenta. Hypoxia occurs during the development of placenta in the first trimester and is implicated in trophoblast differentiation. Oxidative stress, resulting from deficient remodeling of spiral arteries, is an important inducer of preeclampsia. The potassium-dependent sodium/calcium exchangers including NCKX3 and NCX1 play critical roles in the transport of intracellular calcium that is exchanged with extracellular sodium ions. Calcium-relate

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Iwamoto, Takahiro, Akira Uehara, Tomoe Y. Nakamura, Issei Imanaga, and Munekazu Shigekawa. "Chimeric Analysis of Na+/Ca2+Exchangers NCX1 and NCX3 Reveals Structural Domains Important for Differential Sensitivity to External Ni2+or Li+." Journal of Biological Chemistry 274, no. 33 (August 13, 1999): 23094–102. http://dx.doi.org/10.1074/jbc.274.33.23094.

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Pignataro, Giuseppe, Rosaria Gala, Ornella Cuomo, Anna Tortiglione, Lucia Giaccio, Pasqualina Castaldo, Rossana Sirabella, et al. "Two Sodium/Calcium Exchanger Gene Products, NCX1 and NCX3, Play a Major Role in the Development of Permanent Focal Cerebral Ischemia." Stroke 35, no. 11 (November 2004): 2566–70. http://dx.doi.org/10.1161/01.str.0000143730.29964.93.

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Sisalli, M. J., A. Secondo, A. Esposito, V. Valsecchi, C. Savoia, G. F. Di Renzo, L. Annunziato, and A. Scorziello. "Endoplasmic reticulum refilling and mitochondrial calcium extrusion promoted in neurons by NCX1 and NCX3 in ischemic preconditioning are determinant for neuroprotection." Cell Death & Differentiation 21, no. 7 (March 14, 2014): 1142–49. http://dx.doi.org/10.1038/cdd.2014.32.

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Khaksar, Sepideh, and Mohammad Reza Bigdeli. "Anti-excitotoxic effects of cannabidiol are partly mediated by enhancement of NCX2 and NCX3 expression in animal model of cerebral ischemia." European Journal of Pharmacology 794 (January 2017): 270–79. http://dx.doi.org/10.1016/j.ejphar.2016.11.011.

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SECONDO, A., I. R. STAIANO, A. SCORZIELLO, R. SIRABELLA, F. BOSCIA, A. ADORNETTO, L. M. T. CANZONIERO, G. DI RENZO, and L. ANNUNZIATO. "The Na+/Ca2+ Exchanger Isoform 3 (NCX3) but Not Isoform 2 (NCX2) and 1 (NCX1) Singly Transfected in BHK Cells Plays a Protective Role in a Model of in Vitro Hypoxia." Annals of the New York Academy of Sciences 1099, no. 1 (February 15, 2007): 481–85. http://dx.doi.org/10.1196/annals.1387.052.

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Dong, Hui, Yanfen Jiang, Chris R. Triggle, Xiaofang Li, and Jonathan Lytton. "Novel role for K+-dependent Na+/Ca2+ exchangers in regulation of cytoplasmic free Ca2+ and contractility in arterial smooth muscle." American Journal of Physiology-Heart and Circulatory Physiology 291, no. 3 (September 2006): H1226—H1235. http://dx.doi.org/10.1152/ajpheart.00196.2006.

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Cytoplasmic free Ca2+ ([Ca2+]cyt) is essential for the contraction and relaxation of blood vessels. The role of plasma membrane Na+/Ca2+ exchange (NCX) activity in the regulation of vascular Ca2+ homeostasis was previously ascribed to the NCX1 protein. However, recent studies suggest that a relatively newly discovered K+-dependent Na+/Ca2+ exchanger, NCKX (gene family SLC24), is also present in vascular smooth muscle. The purpose of the present study was to identify the expression and function of NCKX in arteries. mRNA encoding NCKX3 and NCKX4 was demonstrated by RT-PCR and Northern blot in bo

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Di Martino, Rossana, Maria Sisalli, Rossana Sirabella, Salvatore Della Notte, Domenica Borzacchiello, Antonio Feliciello, Lucio Annunziato та Antonella Scorziello. "Ncx3-Induced Mitochondrial Dysfunction in Midbrain Leads to Neuroinflammation in Striatum of A53t-α-Synuclein Transgenic Old Mice". International Journal of Molecular Sciences 22, № 15 (30 липня 2021): 8177. http://dx.doi.org/10.3390/ijms22158177.

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The exact mechanism underlying selective dopaminergic neurodegeneration is not completely understood. The complex interplay among toxic alpha-synuclein aggregates, oxidative stress, altered intracellular Ca2+-homeostasis, mitochondrial dysfunction and disruption of mitochondrial integrity is considered among the pathogenic mechanisms leading to dopaminergic neuronal loss. We herein investigated the molecular mechanisms leading to mitochondrial dysfunction and its relationship with activation of the neuroinflammatory process occurring in Parkinson’s disease. To address these issues, experiments

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Sosnoski, Donna M., and Carol V. Gay. "NCX3 is a major functional isoform of the sodium–calcium exchanger in osteoblasts." Journal of Cellular Biochemistry 103, no. 4 (2008): 1101–10. http://dx.doi.org/10.1002/jcb.21483.

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Boscia, F., C. D'Avanzo, A. Pannaccione, A. Secondo, A. Casamassa, L. Formisano, N. Guida, and L. Annunziato. "Silencing or knocking out the Na+/Ca2+ exchanger-3 (NCX3) impairs oligodendrocyte differentiation." Cell Death & Differentiation 19, no. 4 (September 30, 2011): 562–72. http://dx.doi.org/10.1038/cdd.2011.125.

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Jeung, E. B. "189 THE CALCIUM EXCHANGERS NCKX3 AND NCX1 ARE DISTINCTLY EXPRESSED AND REGULATED BY STEROIDS IN THE HUMAN ENDOMETRIUM DURING THE MENSTRUAL CYCLE." Reproduction, Fertility and Development 23, no. 1 (2011): 195. http://dx.doi.org/10.1071/rdv23n1ab189.

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Plasma membrane sodium–calcium exchangers are an important component of intracellular calcium homeostasis and electrical conduction. The potassium-dependent or sodium–calcium exchangers NCKX3 (gene SLC24A3) and NCX1 (gene SLC8A1) play a critical role in the transport of intracellular calcium across the cell membrane in exchange for extracellular sodium ions. The transcripts SLC24A3 and SLC8A1 are most abundant in the brain and smooth muscle, but many other tissues, particularly the uterus, aorta, and intestine, also express this gene at lower levels. However, the expression and physiological r

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Venn, Neil, Lee P. Haynes, and Robert D. Burgoyne. "Specific effects of KChIP3/calsenilin/DREAM, but not KChIPs 1, 2 and 4, on calcium signalling and regulated secretion in PC12 cells." Biochemical Journal 413, no. 1 (June 12, 2008): 71–80. http://dx.doi.org/10.1042/bj20080441.

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The KChIPs (K+ channel-interacting proteins) are members of the NCS (neuronal calcium sensor) protein family of Ca2+-binding proteins. It is unclear to what extent the KChIPs have distinct functions although they all interact with Kv4 K+ channels. KChIP3 has also been shown to repress transcription of specific genes via binding to DRE (downstream regulatory element) motifs and all KChIPs may share this function. In the present study, we have compared the function of isoforms of the four KChIPs. KChIPs 1–4 were found to stimulate the traffic of Kv4.2 channels to the plasma membrane. KChIP3 expr

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