@article{Guerini1999Expre-6925,
  year={1999},
  doi={10.1074/jbc.274.3.1667},
  title={The Expression of Plasma Membrane Ca2+ Pump Isoforms in Cerebellar Granule Neurons Is Modulated by Ca²+},
  number={3},
  volume={274},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={1667--1676},
  author={Guerini, Danilo and García-Martin, Elena and Gerber, Andreas and Volbracht, Christiane and Leist, Marcel and Gutiérrez Merino, Carlos and Carafoli, Ernesto}
}

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    <dc:creator>Gutiérrez Merino, Carlos</dc:creator>
    <dcterms:bibliographicCitation>First publ. in: Journal of Biological Chemistry 274 (1999), 3, pp. 1667-1676</dcterms:bibliographicCitation>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:30:12Z</dc:date>
    <dc:contributor>Guerini, Danilo</dc:contributor>
    <dc:creator>Gerber, Andreas</dc:creator>
    <dc:contributor>Gerber, Andreas</dc:contributor>
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    <dc:contributor>García-Martin, Elena</dc:contributor>
    <dc:creator>Volbracht, Christiane</dc:creator>
    <dc:creator>Carafoli, Ernesto</dc:creator>
    <dcterms:title>The Expression of Plasma Membrane Ca2+ Pump Isoforms in Cerebellar Granule Neurons Is Modulated by Ca²+</dcterms:title>
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    <dc:creator>García-Martin, Elena</dc:creator>
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    <dc:creator>Leist, Marcel</dc:creator>
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    <dcterms:abstract xml:lang="eng">Plasma membrane Ca²+  ATPase (PMCA) pump isoforms 2, 3, and 1CII are expressed in large amounts in the cerebellum of adult rats but only minimally in neonatal cerebellum. These isoforms were almost undetectable in rat neonatal cerebellar granule cells 1 3 days after plating, but they became highly expressed after 7 9 days of culturing under membrane depolarizing conditions (25 mM KCl). The behavior of isoform 4 was different: it was clearly detectable in adult cerebellum but was down-regulated by the depolarizing conditions in cultured cells. 25 mM KCl-activated L-type Ca²+ channels, significantly increasing cytosolic Ca²+. Changes in the concentration of Ca²+ in the culturing medium affected the expression of the pumps. L-type Ca²+ channel blockers abolished both the up-regulation of the PMCA1CII, 2, and 3 isoforms and the down-regulation of PMCA4 isoform. When granule cells were cultured in high concentrations of N-methyl-D-aspartic acid, a condition that increased cytosolic Ca²+ through the activation of glutamate-operated Ca²+ channels, up-regulation of PMCA1CII, 2, and 3 and down-regulation of PMCA4 was also observed. The activity of the isoforms was estimated by measuring the phosphoenzyme intermediate of their reaction cycle: the up-regulated isoforms, the activity of which was barely detectable at plating time, accounted for a large portion of the total PMCA activity of the cells. No up-regulation of the sarcoplasmic/ endoplasmic reticulum calcium pump was induced by the depolarizing conditions.</dcterms:abstract>
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    <dc:contributor>Leist, Marcel</dc:contributor>
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    <dcterms:issued>1999</dcterms:issued>
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    <dc:contributor>Volbracht, Christiane</dc:contributor>
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