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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 in such discrimination of NCX isoforms, although their inhibitory potencies were less than those of La3+ and Cd2+. The monovalent cation Li+ stimulated45Ca2+uptake rate by all NCX isoforms similarly with low affinity, although the extent of stimulation was somewhat smaller in NCX1. On the other hand, the isothiourea derivative KB-R7943 was threefold more inhibitory to NCX3 than to NCX1 or NCX2. Thus distinct differences in the kinetic and pharmacological properties were detected between NCX3 and the other two isoforms.

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2

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 pattern of NCX1, NCX2, and NCX3 transcripts in the ischemic core, periinfarct area, as well as in nonischemic brain regions, after 6 and 24 h of permanent middle cerebral artery occlusion (pMCAO) in rats. We found that in the focal region, comprising divisions of the prefrontal, somatosensory, and insular cortices, all three NCX transcripts were downregulated. In the periinfarct area, comprising part of the motor cortex and the lateral compartments of the caudate-putamen, NCX2 messenger ribonucleic acid (mRNA) was downregulated, whereas NCX3 mRNA was significantly upregulated. In remote nonischemic brain regions such as the prelimbic and infralimbic cortices, and tenia tecta, both NCX1 and NCX3 transcripts were upregulated, whereas in the medial caudate-putamen only NCX3 transcripts increased. In all these intact regions, NCX2 signal strongly decreased. These results indicate that NCX gene expression is regulated after pMCAO in a differential manner, depending on the exchanger isoform and region involved in the insult. These data may provide a better understanding of each NCX subtype's pathophysiologic role and may allow researchers to design appropriate pharmacological strategies to treat brain ischemia.

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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 accessible through the Ensembl Genome Browser. We identified and annotated 13 new NCX sequences, including 4 from zebrafish, 4 from Japanese pufferfish, 2 from chicken, and 1 each from honeybee, mosquito, and chimpanzee. Examination of NCX gene structure, together with construction of phylogenetic trees, provided novel insights into the molecular evolution of NCX and allowed us to more accurately annotate NCX gene names. For the first time, we report the existence of NCX2 and NCX3 in organisms other than mammals, yielding the hypothesis that two serial NCX gene duplications occurred around the time vertebrates and invertebrates diverged. In addition, we have found a putative new NCX protein, named NCX4, that is related to NCX1 but has been observed only in fish species genomes. These findings present a stronger foundation for our understanding of the molecular evolution of the NCX gene family and provide a framework for further NCX phylogenetic and molecular studies.

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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 at different time points in the ischemic temporoparietal cortex of rats subjected to tMCAO alone or to tMCAO plus ischemic postconditioning. The results of this study showed that NCX3 protein and ncx3 mRNA were upregulated in those brain regions protected by postconditioning treatment. These changes in NCX3 expression were mediated by the phosphorylated form of the ubiquitously expressed serine/threonine protein kinase p-AKT, as the p-AKT inhibition prevented NCX3 upregulation. The relevant role of NCX3 during postconditioning was further confirmed by results showing that NCX3 silencing, induced by intracerebroventricular infusion of small interfering RNA (siRNA), partially reverted the postconditioning-induced neuroprotection. The results of this study support the idea that the enhancement of NCX3 expression and activity might represent a reasonable strategy to reduce the infarct extension after stroke.

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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 expressed in heart, brain, and skeletal muscle, whereas splicing variants with exon B are found in all rat tissues except heart. The second and third isoforms of the Na+/Ca2+ exchanger, NCX2 and NCX3, show a deletion of 37 amino acids in the intracellular loop corresponding to parts of the variable region of NCX1. We identified three splicing isoforms of NCX3 in brain and skeletal muscle by reverse transcriptase-polymerase chain reaction. These splice variants are generated by including either of two alternative exons equivalent to the NCX1 exon A or B and by including or excluding a sequence equivalent to the NCX1 exon C. We did not detect any alternative splicing of NCX2. We examined selected tissues from neonatal and adult rats and found developmental regulation for NCX1 and NCX3 splicing isoforms in skeletal muscle. Specific isoform patterns were also detected for NCX1 and NCX3 in cultured cortical neurons, astrocytes, and oligodendrocytes. We suggest a new terminology to distinguish the different splice variants of individual NCX isoforms.

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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 increase of NCX1 in cortical and hippocampal neurons. Interestingly, in cortex and hippocampus NCX1 overexpression increased, where NCX1 knock-out reduced, both exchanger activity and Akt1 phosphorylation, a neuronal survival signaling. More important, mice overexpressing NCX1 showed a reduced ischemic volume and an amelioration of focal and general deficits when subjected to transient middle cerebral artery occlusion. Conversely, NCX1-knock-out mice displayed a worsening of brain damage, focal and neurological deficits with a decrease in Akt phosphorylation. These results support the idea that NCX1 overexpression/activation may represent a feasible therapeutic opportunity in stroke intervention.

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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 of adult muscle. NCX3 appeared to be more uniformly distributed along the sarcolemma and inside myoplasm. In the adult, NCX1 was predominantly expressed in oxidative (type 1 and 2A) fibers of both slow- and fast-twitch muscles, whereas NCX3 was highly expressed in fast glycolytic (2B) fibers. NCX2 was expressed in rat brain but not in skeletal muscle. Developmental changes in NCX1 and NCX3 as well as the distribution of these isoforms at the cellular level and in different fiber types suggest that they may have different physiological roles.

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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 transported ions Na+ and Ca2+ were markedly similar for the three exchangers at both membrane surfaces. Likewise, generally similar responses to changes in pH, chymotrypsin treatment, and application of various inhibitors were obtained. Depletion of cellular ATP inhibited NCX1 and NCX2 but did not affect the activity of NCX3. Exchange activities of NCX1 and NCX3 were modestly increased by agents that activate protein kinases A and C. All exchangers were regulated by intracellular Ca2+. NCX1-induced exchange currents were especially large in excised patches and, like the native myocardial exchanger, were stimulated by ATP. Results may be influenced by our choice of expression system and specific splice variants, but, overall, the three exchangers appear to have very similar properties.

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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 proliferation of human gastrointestinal myofibroblasts, focusing on human gastric myofibroblasts (HGMs). We used microfluorometric measurements to investigate the intracellular Ca2+ and Na+ concentrations, PCR analysis and immunostaining to show the presence of the NCX, patch clamp for measuring NCX activity, and proliferation and migration assays to investigate the functional role of the exchanger. We showed that 53.0 ± 8.1% of the HGMs present Ca2+ oscillations, which depend on extracellular Ca2+ and Na+, and can be inhibited by NCX inhibitors. NCX1, NCX2, and NCX3 were expressed at both mRNA and protein levels in HGMs, and they contribute to the intracellular Ca2+ and Na+ homeostasis as well, regardless of the oscillatory activity. NCX inhibitors significantly blocked the basal and insulin-like growth factor II-stimulated migration and proliferation rates of HGMs. In conclusion, we showed that NCX plays a pivotal role in regulating the Ca2+ homeostasis, migration, and proliferation of HGMs. The inhibition of NCX activity may be a potential therapeutic target in hyperproliferative gastric diseases.

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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 cardiac myocytes. Site-directed mutagenesis of the GATA-4 site at −75 abolishes binding and reduces activity of the minimum and full-length promoters by >90 and ∼60%, respectively. Mutation of the GATA site at −145 reduces activity of the full-length promoter by ∼30%. Mutation of an E-box at −175 does not alter promoter activity.

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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+/Ca2+ exchangers may allow Ca2+ entry and may play more specialized roles in Ca2+ movement between compartments. The NCX (Na+/Ca2+ exchanger) [SLC (solute carrier) 8] branch of Na+/Ca2+ exchangers comprises three members: NCX1 has been most extensively studied, and is broadly expressed with particular abundance in heart, brain and kidney, NCX2 is expressed in brain, and NCX3 is expressed in brain and skeletal muscle. The NCX proteins subserve a variety of roles, depending upon the site of expression. These include cardiac excitation–contraction coupling, neuronal signalling and Ca2+ reabsorption in the kidney. The NCKX (Na2+/Ca2+–K+ exchanger) (SLC24) branch of Na+/Ca2+ exchangers transport K+ and Ca2+ in exchange for Na+, and comprises five members: NCKX1 is expressed in retinal rod photoreceptors, NCKX2 is expressed in cone photoreceptors and in neurons throughout the brain, NCKX3 and NCKX4 are abundant in brain, but have a broader tissue distribution, and NCKX5 is expressed in skin, retinal epithelium and brain. The NCKX proteins probably play a particularly prominent role in regulating Ca2+ flux in environments which experience wide and frequent fluctuations in Na+ concentration. Until recently, the range of functions that NCKX proteins play was generally underappreciated. This situation is now changing rapidly as evidence emerges for roles including photoreceptor adaptation, synaptic plasticity and skin pigmentation. The CCX (Ca2+/cation exchanger) branch has only one mammalian member, NCKX6 or NCLX (Na+/Ca2+–Li+ exchanger), whose physiological function remains unclear, despite a broad pattern of expression.

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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 prevented HDAC4 and HDAC5 recruitment to the ncx3 promoter. Importantly, DREAM, HDAC4, and HDAC5 recruitment to the ncx3 gene was increased in the temporoparietal cortex of rats subjected to transient middle cerebral artery occlusion (tMCAO), with a consequent histone-deacetylation of ncx3 promoter. Conversely, the tMCAO-induced NCX3 reduction was prevented by intracerebroventricular injection of siDREAM, siHDAC4, and siHDAC5. Notably, MC1568 prevented oxygen glucose deprivation plus reoxygenation and tMCAO-induced neuronal damage, whereas its neuroprotective effect was abolished by ncx3 knockdown. Collectively, we found that: (1) DREAM/HDAC4/HDAC5 complex epigenetically down-regulates ncx3 gene transcription after stroke, and (2) pharmacological inhibition of class IIa HDACs reduces stroke-induced neurodetrimental effects.

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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 control denuded oocytes are consistent with this view: (i) reverse transcription-PCR revealed that the oocyte expresses two transcripts for the NCX1 and NCX3 isoforms; (ii) immunofluorescence experiments showed that native NCX1 and InsP3Rs are largely codistributed in discrete areas of the plasma membrane in close apposition to the cortical endoplasmic reticulum shell; (iii) when stimulated by rabbit serum, which elevates intracellular Ca2+mediated by InsP3, voltage-clamped oocytes display a large and transient inward Ca2+-activated chloride current, ICl(Ca), as a result of the Ca2+rise at the inner surface membrane; (iv) this current is significantly enhanced by KB-R7943 and by an extracellular sodium-depleted medium, two maneuvers that prevent “Ca2+extrusion” via NCX; and (v) blocking NCX enhanced the ICl(Ca)elicited by InsP3but not by Ca2+photolysis in oocytes injected with the respective caged compounds. Moreover, overexpression of cardiac NCX1, confirmed by confocal microscopy, has functional consequences for the “Ca2+influx” but not for the serum-elicited “Ca2+efflux” mode of basal exchange activity and does not alter the number of endogenous NCX/InsP3Rs colocalization sites. Our results suggest that native NCX, because of its strategic position, may regulate InsP3-mediated Ca2+signaling during the early phases of oocyte maturation and/or fertilization, and furthermore foreign cardiac protein is excluded from the Ca2+microdomains surrounding the native NCX/InsP3Rs complex in the oocyte.

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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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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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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. Methods: In therapy sensitive D283 and therapy resistant UW228-3 medulloblastoma cells transcript levels were estimated by RT-PCR, protein abundance by Western blotting, cytosolic Ca2+-activity ([Ca2+]i) from Fura-2-fluorescence, Na+/ Ca2+-exchanger activity from the increase of [Ca2+]i (Δ[Ca2+]i) and from whole cell current (Ica) following abrupt replacement of Na+ containing (130 mM) and Ca2+ free by Na+ free and Ca2+ containing (2 mM) extracellular perfusate as well as cell death from PI -staining and annexin-V binding in flow cytometry. Results: The transcript levels of NCX3, NCKX2, and NCKX5, protein abundance of NCX3, slope and peak of Δ[Ca2+]i as well as Ica were significantly lower in therapy sensitive D283 than in therapy resistant UW228-3 medulloblastoma cells. The Na+/Ca2+-exchanger inhibitor KB-R7943 (10 µM) significantly blunted Δ[Ca2+]i, and augmented the ionizing radiation-induced apoptosis but did not significantly modify clonogenicity of medulloblastoma cells. Apoptosis was further enhanced by NCX3 silencing. Conclusions: Na+/Ca2+-exchanger activity significantly counteracts apoptosis but does not significantly affect clonogenicity after radiation of medulloblastoma cells.

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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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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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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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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 before LPS treatment. Dexamethasone did not affect the Ca2+content of intracellular stores, sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)2 and SERCA3 expression, ryanodine receptor (RyR)1 expression, or Ca2+entry through store-operated Ca2+channels. In contrast, dexamethasone increased the transcript level and the membrane protein abundance of the Na+/Ca2+exchanger NCX3. The activity of Na+/Ca2+exchangers was assessed by removal of extracellular Na+in the presence of external Ca2+, a maneuver triggering the Ca2+influx mode. Indeed, Na+removal resulted in a rapid transient increase of [Ca2+]iand induced an outwardly directed current as measured in whole cell patch-clamp experiments. Dexamethasone significantly augmented the increase of [Ca2+]iand the outward current following removal of extracellular Na+. The NCX blocker KB-R7943 reversed the inhibitory effect of dexamethasone on LPS-induced increase in [Ca2+]i. Dexamethasone blunted LPS-induced stimulation of CD86 expression and TNF-α production, an effect significantly less pronounced in the presence of NCX blocker KB-R7943. In conclusion, our results show that glucocorticoid treatment blunts LPS-induced increase in [Ca2+]iin DCs by increasing expression and activity of Na+/Ca2+exchanger NCX3. The effect contributes to the inhibitory effect of the glucocorticoid on DC maturation.

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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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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 transported in the same direction as Ca2+, with a coupling ratio of four Na+to one Ca2+plus one K+. The exchanger kinetics are affected by nontransported Ca2+, Na+, protons, ATP, and diverse other modulators. Five genes that code for the exchangers have been identified in mammals: three in the Na+/Ca2+exchanger family ( NCX1, NCX2, and NCX3) and two in the Na+/Ca2+plus K+family ( NCKX1 and NCKX2). Genes homologous to NCX1 have been identified in frog, squid, lobster, and Drosophila. In mammals, alternatively spliced variants of NCX1 have been identified; dominant expression of these variants is cell type specific, which suggests that the variations are involved in targeting and/or functional differences. In cardiac myocytes, and probably other cell types, the exchanger serves a housekeeping role by maintaining a low intracellular Ca2+concentration; its possible role in cardiac excitation-contraction coupling is controversial. Cellular increases in Na+concentration lead to increases in Ca2+concentration mediated by the Na+/Ca2+exchanger; this is important in the therapeutic action of cardiotonic steroids like digitalis. Similarly, alterations of Na+and Ca2+apparently modulate basolateral K+conductance in some epithelia, signaling in some special sense organs (e.g., photoreceptors and olfactory receptors) and Ca2+-dependent secretion in neurons and in many secretory cells. The juxtaposition of PM and sarco(endo)plasmic reticulum membranes may permit the PM Na+/Ca2+exchanger to regulate sarco(endo)plasmic reticulum Ca2+stores and influence cellular Ca2+signaling.

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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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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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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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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 amplitude of 0 Na+-induced [Ca2+]i increase was larger during the day than at night, with no difference between dorsal and ventral SCN neurons. Ca2+ extrusion via forward NCX was studied by determining the effect of Na+ removal on Ca2+ clearance after high-K+-induced Ca2+ loads. The clearance of Ca2+ proceeded with two exponential decay phases, with the fast decay having total signal amplitude of ∼85% and a time constant of ∼7 s. Na+-free solution slowed the fast decay rate threefold, whereas mitochondrial protonophore prolonged mostly the slow decay. In contrast, blockade of plasmalemmal and sarco(endo)plasmic reticulum Ca2+ pumps had little effect on the kinetics of Ca2+ clearance. RT-PCR indicated the expression of NCX1 and NCX2 mRNAs. Immunohistochemical staining showed the presence of NCX1 immunoreactivity in the whole SCN but restricted distribution of NCX2 immunoreactivity in the ventrolateral SCN. Together our results demonstrate an important role of NCX, most likely NCX1, as well as mitochondrial Ca2+ uptake in clearing somatic Ca2+ after depolarization-induced Ca2+ influx in SCN neurons.

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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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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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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 expressed in stomach, the former was expressed strongly in antrum, whereas the latter displayed greater expression in fundus. Isolated plasma membrane fractions derived from gastric fundus smooth muscle were also investigated to clarify the relationship between NCX protein expression and function. Na+-dependent Ca2+ uptake increased directly with Ca2+ concentration. Ca2+ uptake in Na+-loaded vesicles was markedly elevated in comparison with K+-loaded vesicles. Additionally, Ca2+ uptake by the Na+- or K+-loaded vesicles was substantially higher in the presence of A23187 than in its absence. The result can be explained based on the assumption that Na+ gradients facilitate downhill movement of Ca2+. Na+-dependent Ca2+ uptake was abolished by the monovalent cationic ionophore, monensin. NaCl enhanced Ca2+ efflux from vesicles, and this efflux was significantly inhibited by gramicidin. Results documented evidence that NCX2 isoform functionally contributes to Ca2+ extrusion and maintenance of contraction-relaxation cycle in gastric fundus smooth muscle.Key words: stomach, smooth muscle, Na+/Ca2+ exchanger (NCX), NCX2.

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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-related proteins, NCXs, calbindin, calcium pumping proteins (TRPV5-6, PMCA1b), transcripts are abundant in the smooth muscle, uterus, aorta, and intestine. The expressions of calcium-related proteins in the kidney, duodenum, and placenta after hypoxic stress in rats at gestation Day 19.5 (GD 19.5) were examined by real-time PCR and Western blot analysis. Hypoxic condition did not change fetal weight; however, it significantly increased the weight of placenta compared to normoxic condition. In GD 19.5, renal NCKX3 and TRPV6 expressions were increased, whereas the levels of NCX1 were decreased in hypoxic rats compared with normoxic pregnant rats. The expressions of CaBP-9k, TRPV5, and PMCA1b were not altered in normoxic or hypoxic rat tissues. Duodenal expressions of CaBP-9k, TRPV5-6, and PMCA1 were decreased in hypoxic rats, whereas NCXs were not changed. The transcripts of NCKX3, TRPV5-6, and PMCA1b were highly expressed in the placenta of hypoxic rat. Taken together, the expressions of renal, duodenal, and placental calcium-related proteins appear to be modulated by hypoxia-induced oxidative stress, implying that calcium-related proteins may be involved in preeclamptic oxidative stress.

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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 both rat mesenteric and aortic smooth muscle. NCXK3 and NCKX4 proteins were also demonstrated by immunoblot and immunofluorescence. After voltage-gated Ca2+ channels, store-operated Ca2+ channels, and Na+ pump were pharmacologically blocked, when the extracellular Na+ was replaced with Li+ (0 Na+) to induce reverse mode (Ca2+ entry) activity of Na+/Ca2+ exchangers, a large increase in [Ca2+]cyt signal was observed in primary cultured aortic smooth muscle cells. About one-half of this [Ca2+]cyt signal depended on the extracellular K+. In addition, after the activity of NCX was inhibited by KB-R7943, Na+ replacement-induced Ca2+ entry was absolutely dependent on extracellular K+. In arterial rings denuded of endothelium, a significant fraction of the phenylephrine-induced and nifedipine-resistant aortic or mesenteric contraction could be prevented by removal of extracellular K+. Taken together, these data provide strong evidence for the expression of NCKX proteins in the vascular smooth muscle and their novel role in mediating agonist-stimulated [Ca2+]cyt and thereby vascular tone.

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Di Martino, Rossana, Maria Sisalli, Rossana Sirabella, Salvatore Della Notte, Domenica Borzacchiello, Antonio Feliciello, Lucio Annunziato, and 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, no. 15 (July 30, 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 were performed in vitro and in vivo in mice carrying the human mutation of α-synuclein A53T under the prion murine promoter. In these models, the expression and activity of NCX isoforms, a family of important transporters regulating ionic homeostasis in mammalian cells working in a bidirectional way, were evaluated in neurons and glial cells. Mitochondrial function was monitored with confocal microscopy and fluorescent dyes to measure mitochondrial calcium content and mitochondrial membrane potential. Parallel experiments were performed in 4 and 16-month-old A53T-α-synuclein Tg mice to correlate the functional data obtained in vitro with mitochondrial dysfunction and neuroinflammation through biochemical analysis. The results obtained demonstrated: 1. in A53T mice mitochondrial dysfunction occurs early in midbrain and later in striatum; 2. mitochondrial dysfunction occurring in the midbrain is mediated by the impairment of NCX3 protein expression in neurons and astrocytes; 3. mitochondrial dysfunction occurring early in midbrain triggers neuroinflammation later into the striatum, thus contributing to PD progression during mice aging.

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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 roles of NCKX3 and NCX1 are largely unknown in the human endometrium during the menstrual cycle. Thus, we examined the endometrial expression of NCKX3 and NCX1 at the transcriptional and translational levels at different phases of the menstrual cycle. Our findings revealed that NCKX1 and NCKX3 were differentially expressed during the menstrual cycle. The endometrial expression of NCKX3 mRNA and protein was enhanced up to 1.5- to 2.5-fold at the early proliferative phase, midproliferative phase, and early secretory phase compared with other phases, whereas a significant alteration in NCX1 expression during the human menstrual cycle was not observed. Subsequent immunohistochemical analysis revealed a large number of uterine NCKX3 and NCX1 proteins in the cytoplasm of luminal and glandular epithelial cells throughout the menstrual cycle. Taken together, these results suggest that human endometrial NCKX3 is abundantly expressed in the endometrium and that NCKX3 may be involved in reproductive function during the menstrual cycle in the human endometrium.

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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 expression in PC12 cells resulted in an increase in exocytosis evoked by activation of purinergic receptors. In contrast, KChIPs 1, 2 and 4, although expressed to the same extent, had no effect on secretion. In addition, KChIP3 but not KChIPs 1, 2 and 4 modified the ATP-induced Ca2+ signal resulting in a delay in recovery after the peak Ca2+ elevation and also specifically resulted in down-regulation of the Na+/Ca2+ exchanger NCX3, which could explain the effects on the Ca2+ signal and secretion. Regulation of NCX3 by KChIP3 has been shown to occur via its DREAM (DRE antagonist modulator) function [Gomez-Villafuertes, Torres, Barrio, Savignac, Gabellini, Rizzato, Pintado, Gutierrez-Adan, Mellstrom, Carafoli and Naranjo (2005) J. Neurosci. 25, 10822–10830] suggesting that this activity might depend on the cellular context of expression of the various KChIPs. These results reveal a new role for KChIP3 in the regulation of Ca2+-regulated secretion and also suggest that the functions of each of the KChIPs may be more specialized than previously appreciated.

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