Am J Physiol Cell Physiol Ad Instruments
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 284: C1235-C1246, 2003. First published January 15, 2003; doi:10.1152/ajpcell.00522.2002
0363-6143/03 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
284/5/C1235    most recent
00522.2002v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (17)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chernova, M. N.
Right arrow Articles by Alper, S. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chernova, M. N.
Right arrow Articles by Alper, S. L.
Vol. 284, Issue 5, C1235-C1246, May 2003

Structure-function relationships of AE2 regulation by Ca<UP><SUB>i</SUB><SUP>2+</SUP></UP>-sensitive stimulators NH<UP><SUB>4</SUB><SUP>+</SUP></UP> and hypertonicity

Marina N. Chernova, Andrew K. Stewart, Lianwei Jiang, David J. Friedman, Yune Z. Kunes, and Seth L. Alper

Molecular Medicine and Renal Units, Beth Israel Deaconess Medical Center, Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215

We showed previously that the nonerythroid anion exchanger AE2 and the erythroid anion exchanger AE1 differ greatly in their regulation by acute changes in intracellular pH (pHi) and extracellular pH (pHo). We have now examined how AE2, but not AE1, is activated by two stimuli with opposing effects on oocyte pHi: an alkalinizing stimulus, hypertonicity, and an acidifying stimulus, NH<UP><SUB>4</SUB><SUP>+</SUP></UP>. We find that both NH2-terminal cytoplasmic and COOH-terminal transmembrane domains of AE2 are required for activation by either stimulus. Directed by initial deletion mutagenesis studies of the NH2-terminal cytoplasmic domain, an alanine scan of AE2 amino acids 336-347 identified residues whose individual mutation abolished or severely attenuated sensitivity to both or only one activating stimulus. Chelation of cytoplasmic Ca2+ (Ca<UP><SUB>i</SUB><SUP>2+</SUP></UP>) diminished or abolished AE2 stimulation by NH<UP><SUB>4</SUB><SUP>+</SUP></UP> and by hypertonicity. Calmidazolium inhibited AE2 activity, but not that of AE1. AE2 was insensitive to many other modifiers of Ca2+ signaling. Unlike AE2 stimulation by NH<UP><SUB>4</SUB><SUP>+</SUP></UP> and by hypertonicity, AE2 inhibition by calmidazolium required only AE2's COOH-terminal transmembrane domain.

band 3; Xenopus oocyte; isotopic flux; site-directed mutagenesis; chloride-bicarbonate exchange; chloride-bicarbonate exchanger; intracellular calcium ion


This article has been cited by other articles:


Home page
 J. Exp. Biol.Home page
S. L. Alper
Molecular physiology and genetics of Na+-independent SLC4 anion exchangers
J. Exp. Biol., June 1, 2009; 212(11): 1672 - 1683.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Gonzalez-Begne, T. Nakamoto, H.-V. Nguyen, A. K. Stewart, S. L. Alper, and J. E. Melvin
Enhanced Formation of a Formula Transport Metabolon in Exocrine Cells of Nhe1 / Mice
J. Biol. Chem., November 30, 2007; 282(48): 35125 - 35132.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
A. K. Stewart, C. E. Kurschat, R. D. Vaughan-Jones, B. E. Shmukler, and S. L. Alper
Acute regulation of mouse AE2 anion exchanger requires isoform-specific amino acid residues from most of the transmembrane domain
J. Physiol., October 1, 2007; 584(1): 59 - 73.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
P. M. Piermarini, I. Choi, and W. F. Boron
Cloning and characterization of an electrogenic Na/HCO3- cotransporter from the squid giant fiber lobe
Am J Physiol Cell Physiol, June 1, 2007; 292(6): C2032 - C2045.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
J. Xu, R. T. Worrell, H. C. Li, S. L. Barone, S. Petrovic, H. Amlal, and M. Soleimani
Chloride/Bicarbonate Exchanger SLC26A7 Is Localized in Endosomes in Medullary Collecting Duct Cells and Is Targeted to the Basolateral Membrane in Hypertonicity and Potassium Depletion
J. Am. Soc. Nephrol., April 1, 2006; 17(4): 956 - 967.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
B. E. Shmukler, C. E. Kurschat, G. E. Ackermann, L. Jiang, Y. Zhou, B. Barut, A. K. Stuart-Tilley, J. Zhao, L. I. Zon, I. A. Drummond, et al.
Zebrafish slc4a2/ae2 anion exchanger: cDNA cloning, mapping, functional characterization, and localization
Am J Physiol Renal Physiol, October 1, 2005; 289(4): F835 - F849.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
P. Ripoche, O. Bertrand, P. Gane, C. Birkenmeier, Y. Colin, and J.-P. Cartron
Human Rhesus-associated glycoprotein mediates facilitated transport of NH3 into red blood cells
PNAS, December 7, 2004; 101(49): 17222 - 17227.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Bakouh, F. Benjelloun, P. Hulin, F. Brouillard, A. Edelman, B. Cherif-Zahar, and G. Planelles
NH3 Is Involved in the NH4 Transport Induced by the Functional Expression of the Human Rh C Glycoprotein
J. Biol. Chem., April 16, 2004; 279(16): 15975 - 15983.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online