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J Biol Chem, Vol. 274, Issue 3, 1667-1676, January 15, 1999
From the Institute of Biochemistry, Swiss Federal Institute of
Technology, Biochemie III, Universitätstrasse 16, CH-8092 Zürich, Switzerland, the 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.
The Expression of Plasma Membrane Ca2+ Pump Isoforms
in Cerebellar Granule Neurons Is Modulated by Ca2+
, and Departamento de
Bioquimica y Biologia Molecular, Universidad de Extremadura,
E-06080 Badajoz, Spain, and the ¶ Department of Toxicology,
University of Konstanz, D-78465 Konstanz, Germany
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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