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2002 | 07 | 4 |
Tytuł artykułu

The isoform- and location-dependence of the functioning of the plasma membrane calcium pump

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The plasma membrane is a specialised multi-component structure with inter- and intracellular signalling functions. Ca2+ plays a crucial role in cellular physiology, and an ATP-driven plasma membrane calcium pump (PMCA) plays the greatest role in the maintenance of a low free Ca2+ concentration in the cytoplasm. The enzyme is coded by four separate genes (PMCA 1-4), and, due to alternative splicing, more than 20 variants can exist. PMCA 1 and 4 isoforms are present in almost all tissues, whereas PMCA 2 and 3 are found in more specialised cell types. The variants differ primarily in their regulatory regions, thus the modulation of calcium pump activity strongly depends on the isoform and the membrane composition. The unique function of PMCA isoforms was confirmed using the practical experimental models - a rat pheochromocytoma cell line, a human neuroblastoma cell line, or, more recently, knockout mice. In addition, based on the finding that PMCA could interact with several specific signaling proteins, it was concluded that its location in defined sites of the cell membrane could be a prerequisite for efficient intercellular communication.
Wydawca
-
Rocznik
Tom
07
Numer
4
Opis fizyczny
p.1037-1045,fig.,ref.
Twórcy
autor
  • Neurochemical Laboratory, Department of Biochemistry, Medical University, Mazowiecka 6/8, 92-215 Lodz, Poland
autor
  • Neurochemical Laboratory, Department of Biochemistry, Medical University, Mazowiecka 6/8, 92-215 Lodz, Poland
autor
  • Neurochemical Laboratory, Department of Biochemistry, Medical University, Mazowiecka 6/8, 92-215 Lodz, Poland
autor
  • Neurochemical Laboratory, Department of Biochemistry, Medical University, Mazowiecka 6/8, 92-215 Lodz, Poland
Bibliografia
  • 1. Shull, G. E. Gene knockout studies of Ca2+-transporting ATPases. Eur. J. Biochem. 267 (2000) 5284-5290.
  • 2. Van Baelen, K., Vanoevelen, J., Missiaen, L., Raeymaekers, L. and Wuytack, F. The Golgi PMR1 P-type ATPase of Caenorhabditis elegans. J. Biol. Chem. 276 (2001) 10683-10691.
  • 3. Missiaen, L., Van Acker, K., Parys, J. B., De Smedt, H., Van Baelen, K., Weidema, A. F., Jo Vanoevelen, J., Raeymaekers, L., Renders, J., Callewaert, G., Rizzuto, R. and Wuytack, F. Baseline cytosolic Ca2+ oscillations derived from a non-endoplasmic reticulum Ca2+ store J. Biol. Chem. 276 (2001) 39161-39170.
  • 4. Strehler, E. E. and Zacharias, D. A. Role of altemative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol. Rev. 81 (2001) 21-50.
  • 5. Carafoli, E., Genazzani, A. and Guerini, D. Calcium Controls the transcription of its own transporters and channels in developing neurons. Biochem. Biophys. Res. Commun. 266 (1999) 624-632.
  • 6. Garcia, M. L. and Strehler, E. E. Plasma membrane calcium ATPases as critical regulators of calcium homeostasis during neuronal cell function. Front. Biosci. 4 (1999) D869-882.
  • 7. Paszty, K., Verma, A. K., Padanyi, R., Filoteo, A. G., Penniston, J. T. and Enyedi, A. Plasma membrane Ca2+-ATPase isoform 4b is cleaved and activated by caspase-3 during the early phase of apoptosis. J. Biol. Chem. 277 (2002) 6822-6829.
  • 8. Caride, A. J, Filoteo, A. G., Penheiter,. A. R., Paszty, K., Enyedi, A. and Penniston, J. T. Delayed activation of the plasma membrane calcium pump by a sudden increase in Ca2+ : fast pumps reside in fast cells. Cell Calcium 30 (2001) 49-57.
  • 9. Penniston, J. T. and Enyedi, A. Modulation of the plasma membrane Ca2+ pump. J. Membr. Biol. 165 (1998) 101-109.
  • 10. Kim, E., DeMarco, S. J., Marfatia, S. M., Chishti, A. H., Sheng, M. and Strehler, E. E. Plasma membrane Ca2+-ATPase isoform 4b binds to membrane-associated guanylate kinase (MAGUK) proteins via their PDZ (Psd-95/Dlg/Zo-l) domains. J. Biol. Chem. 273 (1998) 1591-1595.
  • 11. DeMarco, S. J. and Strehler, E. E. Plasma membrane Ca2+-ATPase isoforms 2b and 4b interact promiscuoisly and selectively with members of the membrane-associated guanylate kinase family of PDZ (Psd-95/Dlg/Zo-l) domain-containing proteins. J. Biol. Chem. 276 (2001) 21594-21600.
  • 12. DeMarco, S. J., Chicka, M. C. and Strehler, E. E. Plasma membrane Ca2+- ATPase isoform 2b interacts preferentially with Na+/H+exchanger regulatory factor2 in apical plasma membranes. J. Biol. Chem. 277 (2001) 10506-10511.
  • 13. Shaul, P. W. and Anderson, R. G. W. Role of plasmalemmal caveolae in signal transduction. Am. J. Physiol. 275 (1998) L843-51.
  • 14. Lehotsky, J., Kaplan, P., Racay, P. Mezesova, V. and Raeymaekers, L. Distribution of plasma membrane Ca2+ pump (PMCA) isoforms in the gerbil brain: effect of ischemia-reperfusion injury. Neurochem. Int. 35 (1999) 221-227.
  • 15. Stauffer, T. P., Guerini, D. and Carafoli, E. Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. A study using specific antibodies. J. Biol. Chem. 270 (1995) 12184-12190.
  • 16. Stauffer, T. P., Guerini, D., Celio, M. R. and Carafoli, E. Immunolocalization of the plasma membrane Ca2+ pump isoforms in the rat brain. Brain Res. 748 (1997) 21-29.
  • 17. Filoteo, A. G., Elwess, N. L., Enyedi, A., Caride, A., Aung, H. H. and Penniston, J. T. Plasma membranę Ca2+ pump in rat brain. Pattems of alternative splices seen by isoform-specific antibodies. J. Biol. Chem. 272 (1997) 23741-23747.
  • 18. Brandt, P. C., Sisken, J. E., Neve, R. L. and Vanaman, T. C. Blockade of plasma membrane calcium pumping ATPase isoform I impairs nerve growth factor-induced neurite extension in pheochromocytoma cells. Proc. Natl. Acad. Sci. USA 93 (1996) 13843-13848.
  • 19. Kozel, P. J., Friedman, R. A.. Erway, L. C., Yamoah, E. N., Liu, L. H., Riddle, T. Duffy, J. J., Doetschman, T., Miller, M. L., Cardell, E. L. and Shull, G. E. Balance and hearing deficits in mice with a null mutation in the gene encoding plasma membrane Ca2+ -ATPase isoform. J. Biol. Chem. 273 (1998) 18693-18696.
  • 20. Street, V. A., McKee-Johnson, J. W., Fonseca, R. C., Tempel, B. L. and Noben-Trauth, K. Mutations in a plasma membrane Ca2+-ATPase gene cause deafness in deafwaddler mice. Nat. Genet. 19 (1998) 390-394.
  • 21. Nakao, M., Furukawa, K., Satoh, E., Ono, K. and Iijima, T. Inhibition by antisense oligonucleotides of plasma membrane Ca2+-ATPase in vascular endothelial cells. Eur. J. Pharmacol. 387 (2000) 273-277.
  • 22. Garcia, M. L., Usachev, Y. M.,Thayer, S. A., Strehler, E. E. and Windebank, A. J. Plasma membrane calcium ATPase plays a role in reducing Ca2+- mediated cytotoxicity in PC12 cells. J. Neurosci. Res. 64 (2001) 661-669.
  • 23. Usachev, Y. M., Toutenhoofd, S. L., Goellner, G. M., Strehler, E. E. and Thayer, S. A. Differentiation induces up-regulation of plasma membrane Ca2+-ATPase and concomitant increase in Ca2+ efflux in human neuroblastoma cell line IMR-32. J. Neurochem. 76 (2001) 1756-1765.
  • 24. Zacharias, D. A. and Strehler, E. E. Change in plasma membrane Ca2+- ATPase splice-variant expression in response to a rise in intracellular Ca2+. Curr. Biol. 6 (1996) 1642-1652.
  • 25. Hammes, A., Oberdorf, S., Strehler, E. E., Stauffer, T., Carafoli, E., Vetter, H. and Neyses, L. Differentiation-specifc isoform mRNA expression of the calmodulin-dependent plasma membrane Ca2+-ATPase. FASEB J. 8 (1994) 428-435.
  • 26. Zylinska, L., Kawecka, I. and Szemraj, J. Modification of Ca2+ transport in PC12 cells after antisense oligonucleotides treatment. XIIth International Symposium “Calcium-binding Proteins and Calcium Function in Health and Disease” Cavalese (2002) P182.
Typ dokumentu
Bibliografia
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Identyfikator YADDA
bwmeta1.element.agro-4db0b4c0-ae09-4368-8a54-e973784f91ea
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