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ATPase, Ca++ transporting, plasma membrane 4

The protein encoded by this gene belongs to the family of P-type primary ion transport ATPases characterized by the formation of an aspartyl phosphate intermediate during the reaction cycle. These enzymes remove bivalent calcium ions from eukaryotic cells against very large concentration gradients and play a critical role in intracellular calcium homeostasis. The mammalian plasma membrane calcium ATPase isoforms are encoded by at least four separate genes and the diversity of these enzymes is further increased by alternative splicing of transcripts. The expression of different isoforms and splice variants is regulated in a developmental, tissue- and cell type-specific manner, suggesting that these pumps are functionally adapted to the physiological needs of particular cells and tissues. This gene encodes the plasma membrane calcium ATPase isoform 4. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATPase, PMCA, PMCA1, PMCA2, PMCA3
Papers on PMCA4
Association of CD147 and Calcium Exporter PMCA4 Uncouples IL-2 Expression from Early TCR Signaling.
Stockinger et al., Vienna, Austria. In J Immunol, Feb 2016
Using affinity purification combined with mass spectrometry, we determined the domain specificity of CD147 interaction partners and identified the calcium exporter plasma membrane calcium ATPase isoform 4 (PMCA4) as the interaction partner of the immunosuppressive moieties of CD147.
An improved method for expression and purification of functional human Ca(2+) transporter PMCA4b in Saccharomyces cerevisiae.
Mata et al., Badajoz, Spain. In Protein Expr Purif, Jan 2016
Here, using the yeast Saccharomyces cerevisiae system, we show a new and enhanced method for the expression of the full-length human PMCA isoform 4b (hPMCA4b) and a truncated form lacking its auto-inhibitory domain.
Plasma membrane Ca2+-ATPase 4: interaction with constitutive nitric oxide synthases in human sperm and prostasomes which carry Ca2+/CaM-dependent serine kinase.
Martin-DeLeon et al., Newark, United States. In Mol Hum Reprod, Nov 2015
Deletion of the gene encoding the widely conserved plasma membrane calcium ATPase 4 (PMCA4), a major Ca(2+) efflux pump, leads to loss of sperm motility and male infertility in mice.
Ultrastructural and immunohistochemical localization of plasma membrane Ca2+-ATPase 4 in Ca2+-transporting epithelia.
Dimke et al., Edmonton, Canada. In Am J Physiol Renal Physiol, Nov 2015
The Pmca4 isoform is enriched in distal nephron isolates and decreased in mice lacking the epithelial transient receptor potential vanilloid 5 Ca(2+) channel.
Epididymosomes: transfer of fertility-modulating proteins to the sperm surface.
Martin-DeLeon, Newark, United States. In Asian J Androl, Sep 2015
More recently proteomic and hypothesis-driven studies have shown that EP from several mammals carry transmembrane (TM) proteins, including plasma membrane Ca 2 + -ATPase 4 (PMCA4).
Selective upregulation of the expression of plasma membrane calcium ATPase isoforms upon differentiation and 1,25(OH)2D3-vitamin treatment of colon cancer cells.
Kovács et al., Budapest, Hungary. In Biochem Biophys Res Commun, Sep 2015
We have previously presented co-expression of the plasma membrane calcium ATPase isoforms 4b (PMCA4b) and 1b (PMCA1b) in colon carcinoma cells, and selective upregulation of PMCA4b during differentiation initiated by short chain fatty acids or post-confluent growth.
Martin-DeLeon et al., Newark, United States. In J Biol Chem, Aug 2015
Oviductosomes ((OVS), exosomes/microvesicles), which deliver the Ca(2+) efflux pump, plasma membrane Ca(2+)ATPase 4 (PMCA4), to sperm are likely to play an important role in sperm fertilizing ability (Al-Dossary, A. A., Strehler, E. E., and Martin-DeLeon, P. A. (2013) PloS one 8, e80181).
Ethnic variability in the expression of hepatic drug transporters: absolute quantification by an optimized targeted quantitative proteomic approach.
Wang et al., Mozambique. In Drug Metab Dispos, Jul 2015
Using a targeted quantitative proteomic approach, we determined hepatic protein concentrations of OATP1B1, OATP1B3, OATP2B1, P-gp, and PMCA4 (a housekeeping protein) in a panel of human livers (n = 141) and compared protein expression across Caucasian, Asian, African-American, and unidentified donors.
Hetero-oligomeric Complex between the G Protein-coupled Estrogen Receptor 1 and the Plasma Membrane Ca2+-ATPase 4b.
Giles et al., Des Moines, United States. In J Biol Chem, Jun 2015
Heterologously expressed GPER/GPR30 in HEK 293 cells co-localizes with PMCA4b, the main endothelial PMCA isoform.
Identification of a receptor for extracellular renalase.
Desir et al., Shanghai, China. In Plos One, 2014
Using biotin transfer studies with RP-220 in the human proximal tubular cell line HK-2 and protein identification by mass spectrometry, we identified PMCA4b as a renalase binding protein.
Genome-wide association study indicates two novel resistance loci for severe malaria.
Horstmann et al., Hamburg, Germany. In Nature, 2012
Genome-wide association study for severe malaria identified a locus on chromosome 1q32 within the ATP2B4 gene, and another locus on chromosome 16q22.2, possibly linked to a neighbouring gene encoding the tight-junction protein MARVELD3
Alternative pathways for association and dissociation of the calmodulin-binding domain of plasma membrane Ca(2+)-ATPase isoform 4b (PMCA4b).
Strehler et al., Boston, United States. In J Biol Chem, 2012
Alternative pathways for association and dissociation of the calmodulin-binding domain of plasma membrane Ca(2+)-ATPase isoform 4b (PMCA4b).
CASK interacts with PMCA4b and JAM-A on the mouse sperm flagellum to regulate Ca2+ homeostasis and motility.
Martin-Deleon et al., Newark, United States. In J Cell Physiol, 2012
Ca(2+) homeostasis in sperm is maintained by the relative ratios of CASK-PMCA4b and CASK-JAM-A interactions
Plasma membrane calcium ATPase expression in human colon multistep carcinogenesis.
Wilhelm et al., Marburg an der Lahn, Germany. In Cancer Invest, 2012
The results of this study suggest posttranscriptional regulation of PMCA4 during carcinogenesis.
Plasma membrane calcium pump (PMCA) isoform 4 is targeted to the apical membrane by the w-splice insert from PMCA2.
Strehler et al., Budapest, Hungary. In Cell Calcium, 2012
Plasma membrane calcium pump (PMCA) isoform 4 is targeted to the apical membrane by the w-splice insert from PMCA2.
Ca2+ signalling in cardiovascular disease: the role of the plasma membrane calcium pumps.
Neyses et al., Manchester, United Kingdom. In Sci China Life Sci, 2011
This article focuses on the functions of PMCA, in particular isoform 4 (PMCA4), in the heart and vasculature and the reported links between PMCAs and contractile function, cardiac hypertrophy, cardiac rhythm and sudden cardiac death, and blood pressure control and hypertension.
The plasma membrane calcium pump in the hearing process: physiology and pathology.
Carafoli, Padova, Italy. In Sci China Life Sci, 2011
Two of them (PMCA1 and PMCA4) are expressed ubiquitously, and are considered housekeeping isoforms.
Impairment of the activity of the plasma membrane Ca²⁺-ATPase in Alzheimer's disease.
Sepúlveda et al., Spain. In Biochem Soc Trans, 2011
The peptide produces an inhibitory effect on the activity of PMCA which is isoform-specific, with the greatest inhibition of PMCA4.
Local signals with global impacts and clinical implications: lessons from the plasma membrane calcium pump (PMCA4).
Neyses et al., Manchester, United Kingdom. In Biochim Biophys Acta, 2011
The recently emerging role of the plasma membrane calcium/calmodulin dependent ATPase isoform 4 (PMCA4) in regulating calcium signalling, is reviewed.
CD22 attenuates calcium signaling by potentiating plasma membrane calcium-ATPase activity.
Wortis et al., Boston, United States. In Nat Immunol, 2004
Inhibition of plasma membrane calcium-ATPase (PMCA) attenuated these effects, as did disruption by homologous recombination of the gene encoding PMCA4a and PMCA4b.
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