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J. Biol. Chem., Vol. 277, Issue 48, 45734-45740, November 29, 2002
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From the Departments of We explored the involvement of protein kinase
C (PKC) and its isoforms in the regulation of BNaC2. Reverse
transcriptase PCR evaluation of PKC isoform expression at the
level of mRNA revealed the presence of
Protein Kinase C Isoform Antagonism Controls BNaC2 (ASIC1)
Function*
,,,§,,, and
Physiology and Biophysics and
§ Surgery, University of Alabama at Birmingham,
Birmingham, Alabama 35294 and the ¶ Department of Neurosurgery,
Emory University, Atlanta, Georgia 30322
and 
/' in all
glioma cell lines analyzed; most, but not all cell lines expressed 
and 
. No messages were found for the 
I and II isotypes of PKC
in the tumor cells. Normal astrocytes expressed but not 
. The
essential features of these results were confirmed at the protein level
by Western analysis. This disproportionate pattern of PKC isoform
expression in glioma cell lines was further echoed in the
functional effects of these PKC isoforms on BNaC2 activity in bilayers.
PKC holoenzyme or the combination of PKCI and PKCII isoforms
inhibited BNaC2. Neither PKC nor PKC or their combination had any
effect on BNaC2 activity in bilayers. The inhibitory effect of the
PKCI and PKCII mixture on BNaC2 activity was abolished by a
5-fold excess of a PKC and PKC combination. PKC holoenzymes,
PKCI, PKCII, PKC, PKC, and PKC phosphorylated BNaC2
in vitro. In patch clamp experiments, the combination of
PKCI and PKCII inhibited the basally activated inward
Na+ conductance. The variable expression of the PKC
isotypes and their functional antagonism in regulating BNaC2 activity
support the idea that the participation of multiple PKC isotypes
contributes to the overall activity of BNaC2.
*
This work was supported by National Institutes of Health
Grants DK37206 and CA71933 and the Brain Tumor Foundation for Children.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: University of
Alabama at Birmingham, 1918 University Blvd., MCLM 704, Birmingham, AL
35294-0005. Tel.: 205-934-6220; Fax: 205-934-2377; E-mail: benos@physiology.uab.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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