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J. Biol. Chem., Vol. 275, Issue 27, 20903-20910, July 7, 2000
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From the The Na+/Ca2+
exchanger (NCX) and the plasma membrane Ca2+-ATPase export
Ca2+ from the cytosol to the extracellular space. Three NCX
genes (NCX1, NCX2, and NCX3),
encoding proteins with very similar properties, are expressed at
different levels in tissues. Essentially, no information is available
on the mechanisms that regulate their expression. Specific antibodies
have been prepared and used to explore the expression of NCX1 and NCX2
in rat cerebellum. The expression of NCX2 became strongly up-regulated
during development, whereas comparatively minor effects were seen for
NCX1. This was also observed in cultured granule cells induced to
mature in physiological concentrations of potassium. By contrast,
higher K+ concentrations, which induce partial
depolarization of the plasma membrane and promote the influx of
Ca2+, caused the complete disappearance of NCX2. Reverse
transcription-polymerase chain reaction analysis showed that the
process occurred at the transcriptional level and depended on the
activation of the Ca2+ calmodulin-dependent
protein phosphatase, calcineurin. The NCX1 and
NCX3 genes were also affected by the depolarizing
treatment: the transcription of the latter became up-regulated, and the
pattern of expression of the splice variants of the former changed. The effects on the NCX1 and NCX3 genes were
calcineurin-independent.
Calcineurin Controls the Transcription of
Na+/Ca2+ Exchanger Isoforms in Developing
Cerebellar Neurons*
,§, and¶
Institute of Biochemistry, Swiss Federal
Institute of Technology, 8092 Zürich, Switzerland, the
§ Laboratory of Metabolic and Cardiovascular Diseases,
Novartis AG, 4002 Basle, Switzerland, and the ¶ Department of
Biochemistry, University of Padova, 35121 Padova, Italy
*
This work was made possible by the support of the Swiss
National Science foundation, the Italian Ministry of University and Scientific Research (MURST-PRIN 1998), the National Research Council of
Italy (Target Project on Biotechnology), and the Armenise-Harvard Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
0039-049-8276137; Fax: 0039-049-8276125; E-mail:
carafoli@civ.bio.unipd.it.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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