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ATP2A3  -  ATPase, Ca++ transporting, ubiquitous

Homo sapiens

Synonyms: Calcium pump 3, SERCA3, SR Ca(2+)-ATPase 3, Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
 
 
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Disease relevance of ATP2A3

  • The presence of the D17S1828 genetic marker in the cosmid contig enabled us to map the SERCA3 gene (ATP2A3) 11 centimorgans from the top of the short arm p of chromosome 17, in the vicinity of the cystinosis gene locus [1].
  • Expression of endomembrane calcium pumps in colon and gastric cancer cells. Induction of SERCA3 expression during differentiation [2].
  • We report that SERCA3 expression is significantly reduced or lost in colon carcinomas when compared with normal colonic epithelial cells, which express this enzyme at a high level [2].
  • To better characterize the role of SERCA3 in colon carcinogenesis, its expression has been investigated in colonic epithelium, benign lesions, adenomas, and adenocarcinomas [3].
  • Inhibition of Sp1-like factor-dependent transcription blocked SERCA3 expression during cell differentiation, and SERCA3 expression was induced by the expression of dominant-negative TCF4 in colon cancer cells [3].
 

High impact information on ATP2A3

  • In conclusion, intracellular calcium homeostasis becomes progressively anomalous during colon carcinogenesis as reflected by deficient SERCA3 expression [3].
  • Using HEK293 cells to express human SERCA3a, we were able to measure both ATP-mediated, oxalate-dependent (45)Ca(2+) uptake and Ca(2+)-dependent ATP hydrolysis activities due exclusively to SERCA3 [4].
  • Treatment of the tumor cells with butyrate or other established differentiation inducing agents resulted in a marked and specific induction of the expression of SERCA3, whereas the expression of the ubiquitous SERCA2 enzymes did not change significantly or was reduced [2].
  • A similar marked increase in SERCA3 expression was found during spontaneous differentiation of post-confluent Caco-2 cells, and this closely correlated with the induction of other known markers of differentiation [2].
  • Three novel sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) 3 isoforms. Expression, regulation, and function of the membranes of the SERCA3 family [5].
 

Biological context of ATP2A3

 

Anatomical context of ATP2A3

 

Associations of ATP2A3 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 [11].
  • 2) An antiserum directed against an NH2-terminal SERCA3-specific peptide (N89) reacts with SERCA3 expressed in COS cells and with the 97-kDa protein in rat platelets and the corresponding protein in human platelets [9].
  • SERCA3 null mutants survive and appear healthy, but endothelium-dependent relaxation of vascular smooth muscle is impaired and Ca(2+) signaling is altered in pancreatic beta cells [12].
  • Finally, cells treated with histamine and loaded with fura 2 exhibited an improved capacity in eliminating high cytosolic Ca2+ concentrations, in accordance with an increase in activity of a low-affinity Ca2+-ATPase, like SERCA 3 [6].
  • The histamine-induced up-regulation of SERCA 3 was abolished by cyclosporin A and by VIVIT, a peptide that prevents calcineurin and NFAT (nuclear factor of activated T-cells) from interacting, indicating involvement of the calcineurin/NFAT pathway [6].
 

Physical interactions of ATP2A3

  • Studies using photoactivated cross-linker and chimeric Ca-ATPase between SERCA2 and nonmuscle Ca-ATPase (SERCA3) indicated that potential binding residues are located just downstream of the active ATPase site (Asp351) of SERCA2 [13].
 

Other interactions of ATP2A3

  • SERCA3 was not expressed in normal or DD epidermis, but was found in eccrine glands and blood vessels [10].
  • Coexpression of the transmembrane sequence of phospholamban (Met-PLN28-52) with SERCA1a, SERCA2a, and SERCA3 inhibited Ca2+ transport by lowering apparent Ca2+ affinity [14].
  • As judged by platelet glycoprotein IIIa (GPIIIa) expression, an increase in SERCA3 proteins was observed while that of SERCA2b remained unchanged throughout maturation [15].
 

Analytical, diagnostic and therapeutic context of ATP2A3

References

  1. Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene. Promoter analysis and alternative splicing of the SERCA3 pre-mRNA. Dode, L., De Greef, C., Mountian, I., Attard, M., Town, M.M., Casteels, R., Wuytack, F. J. Biol. Chem. (1998) [Pubmed]
  2. Expression of endomembrane calcium pumps in colon and gastric cancer cells. Induction of SERCA3 expression during differentiation. Gélébart, P., Kovács, T., Brouland, J.P., van Gorp, R., Grossmann, J., Rivard, N., Panis, Y., Martin, V., Bredoux, R., Enouf, J., Papp, B. J. Biol. Chem. (2002) [Pubmed]
  3. The loss of sarco/endoplasmic reticulum calcium transport ATPase 3 expression is an early event during the multistep process of colon carcinogenesis. Brouland, J.P., Gélébart, P., Kovàcs, T., Enouf, J., Grossmann, J., Papp, B. Am. J. Pathol. (2005) [Pubmed]
  4. Inhibition of human SERCA3 by PL/IM430. Molecular analysis of the interaction. Chandrasekera, C.P., Lytton, J. J. Biol. Chem. (2003) [Pubmed]
  5. Three novel sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) 3 isoforms. Expression, regulation, and function of the membranes of the SERCA3 family. Martin, V., Bredoux, R., Corvazier, E., Van Gorp, R., Kovacs, T., Gelebart, P., Enouf, J. J. Biol. Chem. (2002) [Pubmed]
  6. Transcription of the sarcoplasmic/endoplasmic reticulum Ca2+-ATPase type 3 gene, ATP2A3, is regulated by the calcineurin/NFAT pathway in endothelial cells. Hadri, L., Pavoine, C., Lipskaia, L., Yacoubi, S., Lompré, A.M. Biochem. J. (2006) [Pubmed]
  7. Sequence variants of the sarco(endo)plasmic reticulum Ca(2+)-transport ATPase 3 gene (SERCA3) in Caucasian type II diabetic patients (UK Prospective Diabetes Study 48). Varadi, A., Lebel, L., Hashim, Y., Mehta, Z., Ashcroft, S.J., Turner, R. Diabetologia (1999) [Pubmed]
  8. cDNA cloning, expression and chromosomal localization of the human sarco/endoplasmic reticulum Ca(2+)-ATPase 3 gene. Dode, L., Wuytack, F., Kools, P.F., Baba-Aissa, F., Raeymaekers, L., Briké, F., van de Ven, W.J., Casteels, R., Brik, F. Biochem. J. (1996) [Pubmed]
  9. A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells. Wuytack, F., Papp, B., Verboomen, H., Raeymaekers, L., Dode, L., Bobe, R., Enouf, J., Bokkala, S., Authi, K.S., Casteels, R. J. Biol. Chem. (1994) [Pubmed]
  10. Expression of the sarco/endoplasmic reticulum calcium ATPase type 2 and 3 isoforms in normal skin and Darier's disease. Tavadia, S., Authi, K.S., Hodgins, M.B., Munro, C.S. Br. J. Dermatol. (2004) [Pubmed]
  11. 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]
  12. Physiological functions of plasma membrane and intracellular Ca2+ pumps revealed by analysis of null mutants. Shull, G.E., Okunade, G., Liu, L.H., Kozel, P., Periasamy, M., Lorenz, J.N., Prasad, V. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  13. Molecular regulation of phospholamban function and gene expression. Tada, M., Yabuki, M., Toyofuku, T. Ann. N. Y. Acad. Sci. (1998) [Pubmed]
  14. Phospholamban regulates the Ca2+-ATPase through intramembrane interactions. Kimura, Y., Kurzydlowski, K., Tada, M., MacLennan, D.H. J. Biol. Chem. (1996) [Pubmed]
  15. Biogenesis of endoplasmic reticulum proteins involved in Ca2+ signalling during megakaryocytic differentiation: an in vitro study. Lacabaratz-Porret, C., Launay, S., Corvazier, E., Bredoux, R., Papp, B., Enouf, J. Biochem. J. (2000) [Pubmed]
  16. Functional characterization of alternatively spliced human SERCA3 transcripts. Poch, E., Leach, S., Snape, S., Cacic, T., MacLennan, D.H., Lytton, J. Am. J. Physiol. (1998) [Pubmed]
  17. The rat platelet 97-kDa Ca2+ATPase isoform is the sarcoendoplasmic reticulum Ca2+ATPase 3 protein. Bobe, R., Bredoux, R., Wuytack, F., Quarck, R., Kovàcs, T., Papp, B., Corvazier, E., Magnier, C., Enouf, J. J. Biol. Chem. (1994) [Pubmed]
  18. Role of SERCA2b in mobilization of nuclear Ca2+ in HeLa cells. Xu, J.W., Morita, L., Murota, S. J. Med. Dent. Sci. (2001) [Pubmed]
  19. All three splice variants of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene are translated to proteins: a study of their co-expression in platelets and lymphoid cells. Kovács, T., Felföldi, F., Papp, B., Pászty, K., Bredoux, R., Enyedi A, n.u.l.l., Enouf, J. Biochem. J. (2001) [Pubmed]
 
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