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Gene Review

ATP2B1  -  ATPase, Ca++ transporting, plasma membrane 1

Homo sapiens

Synonyms: PMCA1, PMCA1kb, Plasma membrane calcium ATPase isoform 1, Plasma membrane calcium pump isoform 1, Plasma membrane calcium-transporting ATPase 1
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Disease relevance of ATP2B1


Psychiatry related information on ATP2B1

  • This review summarizes the results of recent analysis of the PMCA dysregulation in diseased cells or model systems of pathological conditions, including both acute disorders like hypoxia/ischemia and seizure, and slowly progressing dysfunctions like Alzheimer's disease, hypertension, diabetes and aging [6].

High impact information on ATP2B1

  • During mouse embryonic development, PMCA1 is ubiquitously detected from the earliest time points, and all isoforms show spatially overlapping but distinct expression patterns with dynamic temporal changes occurring during late fetal development [3].
  • The PMCA concept has been proved on the amplification of prions implicated in the pathogenesis of transmissible spongiform encephalopathies [7].
  • Immunofluorescence experiments demonstrated an asymmetric localization of plasma membrane Ca(2+) ATPase (PMCA), which appeared to be partially co-localized with CaR and the gastric H(+)/K(+)-ATPase in the apical membrane of the acid-secreting cells [8].
  • Here we demonstrate that PMCA 4b is a negative regulator of nitric oxide synthase I (NOS-I, nNOS) in HEK293 embryonic kidney and neuro-2a neuroblastoma cell models [9].
  • Effects of PMCA and SERCA pump overexpression on the kinetics of cell Ca(2+) signalling [10].

Chemical compound and disease context of ATP2B1


Biological context of ATP2B1


Anatomical context of ATP2B1


Associations of ATP2B1 with chemical compounds

  • We showed that both PMCA1 and SERCA3 isoform protein and mRNA are upregulated two- to three-fold in thapsigargin-treated HLE B-3 cells in a time and dose-dependent manner [14].
  • Plasma membrane Ca(2+)-ATPases (PMCAs) are involved in local Ca(2+) signaling and in the spatial control of Ca(2+) extrusion, but how different PMCA isoforms are targeted to specific membrane domains is unknown [18].
  • A 1.4-fold- and 2.0-fold-higher protein synthesis peak was seen in PMCA-overexpressing cardiomyocytes after stimulation with isoproterenol for 12 hours and 24 hours, respectively [19].
  • PMCA associates much more strongly with phosphatidylcholine containing disordered hydrocarbon chains than ordered hydrocarbon chains [20].
  • These findings suggest a role for phosphoinositide 3-kinase in regulating PMCA expression, which may be important in the control of Ca(2+)-sensitive VSMC functions [21].

Regulatory relationships of ATP2B1


Other interactions of ATP2B1


Analytical, diagnostic and therapeutic context of ATP2B1

  • METHODS: PMCA mRNA expression was examined by RT-PCR analysis of total RNA from native hCE using PMCA gene specific primers [16].
  • PMCA isoform expression at the protein level in native hCE was examined by immunoblotting using isoform specific antibodies (Abs) and a panPMCA Ab that recognizes all PMCAs [16].
  • Specific probes detect major mRNA species of 5.6 kilobases for hPMCA1, and of 7.5 kilobases for hPMCA3, on Northern blots of human K562 erythroleukemic cell RNA [26].
  • In situ hybridization was employed to determine the expression pattern of the four human PMCA isoforms in the human hippocampus [27].
  • PURPOSE: To compare the effect of 20 cm SDS-PAGE electrophoresis, which is most widely used in proteomic research, in identifying human lens epithelium B3 (HLE B3) cells plasma membrane calcium ATPase (PMCA) isoform's apparent molecular weight (MW), with that of 8 cm SDS-PAGE electrophoresis [28].


  1. Expression of plasma membrane calcium pump isoform mRNAs in breast cancer cell lines. Lee, W.J., Roberts-Thomson, S.J., Holman, N.A., May, F.J., Lehrbach, G.M., Monteith, G.R. Cell. Signal. (2002) [Pubmed]
  2. Differentiation induces up-regulation of plasma membrane Ca(2+)-ATPase and concomitant increase in Ca(2+) efflux in human neuroblastoma cell line IMR-32. Usachev, Y.M., Toutenhoofd, S.L., Goellner, G.M., Strehler, E.E., Thayer, S.A. J. Neurochem. (2001) [Pubmed]
  3. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Strehler, E.E., Zacharias, D.A. Physiol. Rev. (2001) [Pubmed]
  4. Expression and functional characterization of isoforms 4 of the plasma membrane calcium pump. Preianò, B.S., Guerini, D., Carafoli, E. Biochemistry (1996) [Pubmed]
  5. Distribution of plasma membrane Ca2+ pump (PMCA) isoforms in the gerbil brain: effect of ischemia-reperfusion injury. Lehotský, J., Kaplán, P., Racay, P., Mézesová, V., Raeymaekers, L. Neurochem. Int. (1999) [Pubmed]
  6. The role of plasma membrane Ca2+ pumps (PMCAs) in pathologies of mammalian cells. Lehotsky, J., Kaplán, P., Murín, R., Raeymaekers, L. Front. Biosci. (2002) [Pubmed]
  7. Cyclic amplification of protein misfolding: application to prion-related disorders and beyond. Soto, C., Saborio, G.P., Anderes, L. Trends Neurosci. (2002) [Pubmed]
  8. Asymmetrical, agonist-induced fluctuations in local extracellular [Ca(2+)] in intact polarized epithelia. Caroppo, R., Gerbino, A., Debellis, L., Kifor, O., Soybel, D.I., Brown, E.M., Hofer, A.M., Curci, S. EMBO J. (2001) [Pubmed]
  9. The plasmamembrane calmodulin-dependent calcium pump: a major regulator of nitric oxide synthase I. Schuh, K., Uldrijan, S., Telkamp, M., Rothlein, N., Neyses, L. J. Cell Biol. (2001) [Pubmed]
  10. Effects of PMCA and SERCA pump overexpression on the kinetics of cell Ca(2+) signalling. Brini, M., Bano, D., Manni, S., Rizzuto, R., Carafoli, E. EMBO J. (2000) [Pubmed]
  11. Ca(2+)-Mg (2+)-dependent ATP-ase activity and calcium homeostasis in children with chronic kidney disease. Polak-Jonkisz, D., Zwolińska, D., Purzyc, L., Musiał, K. Pediatr. Nephrol. (2007) [Pubmed]
  12. Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. Stauffer, T.P., Hilfiker, H., Carafoli, E., Strehler, E.E. J. Biol. Chem. (1993) [Pubmed]
  13. Structure of the gene encoding the human plasma membrane calcium pump isoform 1. Hilfiker, H., Strehler-Page, M.A., Stauffer, T.P., Carafoli, E., Strehler, E.E. J. Biol. Chem. (1993) [Pubmed]
  14. Regulation of sarco/endoplasmic and plasma membrane calcium ATPase gene expression by calcium in cultured human lens epithelial cells. Marian, M.J., Mukhopadhyay, P., Borchman, D., Tang, D., Paterson, C.A. Cell Calcium (2007) [Pubmed]
  15. Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23. Olson, S., Wang, M.G., Carafoli, E., Strehler, E.E., McBride, O.W. Genomics (1991) [Pubmed]
  16. Expression and immunolocalization of plasma membrane calcium ATPase isoforms in human corneal epithelium. Talarico, E.F., Kennedy, B.G., Marfurt, C.F., Loeffler, K.U., Mangini, N.J. Mol. Vis. (2005) [Pubmed]
  17. Analysis of mRNA expression and cloning of a novel plasma membrane Ca(2+)-ATPase splice variant in human heart. Santiago-García, J., Mas-Oliva, J., Saavedra, D., Zarain-Herzberg, A. Mol. Cell. Biochem. (1996) [Pubmed]
  18. Alternative splicing of the first intracellular loop of plasma membrane Ca2+-ATPase isoform 2 alters its membrane targeting. Chicka, M.C., Strehler, E.E. J. Biol. Chem. (2003) [Pubmed]
  19. Overexpression of the sarcolemmal calcium pump in the myocardium of transgenic rats. Hammes, A., Oberdorf-Maass, S., Rother, T., Nething, K., Gollnick, F., Linz, K.W., Meyer, R., Hu, K., Han, H., Gaudron, P., Ertl, G., Hoffmann, S., Ganten, U., Vetter, R., Schuh, K., Benkwitz, C., Zimmer, H.G., Neyses, L. Circ. Res. (1998) [Pubmed]
  20. The influence of membrane lipid structure on plasma membrane Ca2+ -ATPase activity. Tang, D., Dean, W.L., Borchman, D., Paterson, C.A. Cell Calcium (2006) [Pubmed]
  21. Expression of plasma membrane calcium ATPases in phenotypically distinct canine vascular smooth muscle cells. Abramowitz, J., Aydemir-Koksoy, A., Helgason, T., Jemelka, S., Odebunmi, T., Seidel, C.L., Allen, J.C. J. Mol. Cell. Cardiol. (2000) [Pubmed]
  22. Plasma membrane calcium-ATPase 2 and 4 in human breast cancer cell lines. Lee, W.J., Roberts-Thomson, S.J., Monteith, G.R. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  23. Expression, purification, and characterization of isoform 1 of the plasma membrane Ca2+ pump: focus on calpain sensitivity. Guerini, D., Pan, B., Carafoli, E. J. Biol. Chem. (2003) [Pubmed]
  24. Calcium transport in human salivary glands: a proposed model of calcium secretion into saliva. Homann, V., Kinne-Saffran, E., Arnold, W.H., Gaengler, P., Kinne, R.K. Histochem. Cell Biol. (2006) [Pubmed]
  25. Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels. Brandt, P., Neve, R.L., Kammesheidt, A., Rhoads, R.E., Vanaman, T.C. J. Biol. Chem. (1992) [Pubmed]
  26. Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. Strehler, E.E., James, P., Fischer, R., Heim, R., Vorherr, T., Filoteo, A.G., Penniston, J.T., Carafoli, E. J. Biol. Chem. (1990) [Pubmed]
  27. mRNA expression of the four isoforms of the human plasma membrane Ca(2+)-ATPase in the human hippocampus. Zacharias, D.A., DeMarco, S.J., Strehler, E.E. Brain Res. Mol. Brain Res. (1997) [Pubmed]
  28. Detection of molecular weight of PMCA isoform with 20 cm SDS PAGE electrophoresis: compared with 8 cm SDS PAGE. Yang, H., Zeng, J. Yan ke xue bao = Eye science / "Yan ke xue bao" bian ji bu (2005) [Pubmed]
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