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J. Biol. Chem., Vol. 277, Issue 39, 36085-36091, September 27, 2002
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From the Departments of We examined the ability of carbonic anhydrase II
to bind to and affect the transport efficiency of the NHE1 isoform of
the mammalian Na+/H+ exchanger. The
C-terminal region of NHE1 was expressed in Escherichia coli fused with an N-terminal glutathionine
S-transferase or with a C-terminal polyhistidine tag. Using
a microtiter plate binding assay we showed that the C-terminal region
of NHE1 binds carbonic anhydrase II (CAII) and binding was stimulated
by low pH and blocked by antibodies against the C-terminal of NHE1. The
binding to NHE1 was confirmed by demonstrating protein-protein
interaction using affinity blotting with CAII and immobilized NHE1
fusion proteins. CAII co-immunoprecipitated with NHE1 from CHO cells
suggesting the proteins form a complex in vivo. In cells
expressing CAII and NHE1, the H+ transport rate was almost
2-fold greater than in cells expressing NHE1 alone. The CAII inhibitor
acetazolamide significantly decreased the H+ transport rate
of NHE1 and transfection with a dominant negative CAII inhibited NHE1
activity. Phosphorylation of the C-terminal of NHE1 greatly increased
the binding of CAII. Our study suggests that NHE1 transport
efficiency is influenced by CAII, likely through a direct interaction
at the C-terminal region. Regulation of NHE1 activity by
phosphorylation could involve modulation of CAII binding.
Carbonic Anhydrase II Binds to and Enhances Activity of the
Na+/H+ Exchanger*
§,¶,¶
,
Biochemistry and
¶ Physiology, Canadian Institute of Health Research Membrane
Protein Group, University of Alberta, Edmonton, Alberta T6G 2H7,
Canada, and the ** Canadian Institute of Health Research
Group in Membrane Biology, Department of Medicine and Biochemistry,
University of Toronto, Toronto, Ontario M5S 1A8, Canada
*
This work was supported by grants from the Canadian
Institute of Health Research (to L. F., J. R. C. and R. R.) and by
a grant from the Heart and Stroke Foundation of Canada (to L. F.).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.
Supported by the Alberta Heritage Foundation for Medical Research.
To whom correspondence should be addressed: 347 Medical Science
Bldg., Dept. of Biochemistry, University of Alberta, Edmonton, Alberta
T6G 2H7, Canada. Tel.: 780-492-1848; Fax: 780-492-0886; E-mail:
lfliegel@ualberta.ca.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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