AJP - Renal Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Renal Physiol 284: F1199-F1206, 2003. First published February 25, 2003; doi:10.1152/ajprenal.00131.2002
0363-6127/03 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
284/6/F1199    most recent
00131.2002v1
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 ISI 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 ISI Web of Science (13)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Choi, I.
Right arrow Articles by Boron, W. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Choi, I.
Right arrow Articles by Boron, W. F.
Vol. 284, Issue 6, F1199-F1206, June 2003

Role of glycosylation in the renal electrogenic Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporter (NBCe1)

Inyeong Choi, Lihui Hu, José D. Rojas, Bernhard M. Schmitt, and Walter F. Boron

Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut 06520

The electrogenic Na+-HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> cotransporter NBCe1 is important for the regulation of intracellular pH (pHi) and for epithelial HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> transport in many tissues, including kidney, pancreas, and brain. In the present study, we investigate glycosylation sites in NBCe1. Treatment of rat kidney membrane extracts with peptide N-glycosidase F (PNGase F) shifted the apparent molecular weight (MW) of NBCe1 from 130 to 116, the MW predicted from the deduced amino acid sequence. Treatment with endoglycosidase F2 or H or O-glycosidase did not affect the MW of NBCe1. Lectin-binding studies, together with the enzyme data, suggest that the N-linked carbohydrates are of tri- or tetra-antennary type. To localize glycosylation sites, we individually mutated the seven consensus N-glycosylation sites by replacing asparagine (N) with glutamine (Q) and assessing mutant transporters in Xenopus laevis oocytes. Immunoblotting of oocyte membrane extracts treated with PNGase F indicates that NBCe1 is normally glycosylated at N597 and N617 (both on the third extracellular loop). However, N592 (on the same loop) is glycosylated when the other two sites are mutated. The triple mutant (N592Q/N597Q/N617Q) is completely unglycosylated but, based on microelectrode measurements of membrane potential and pHi in oocytes, preserves the Na+ and HCO<UP><SUB>3</SUB><SUP>−</SUP></UP> dependence and electrogenicity of wild-type NBCe1.

transporter; pH measurement; acid-base mechanism


This article has been cited by other articles:


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
J. Lu and W. F. Boron
Reversible and irreversible interactions of DIDS with the human electrogenic Na/HCO3 cotransporter NBCe1-A: role of lysines in the KKMIK motif of TM5
Am J Physiol Cell Physiol, May 1, 2007; 292(5): C1787 - C1798.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
A. M. Toye, M. D. Parker, C. M. Daly, J. Lu, L. V. Virkki, M. F. Pelletier, and W. F. Boron
The human NBCe1-A mutant R881C, associated with proximal renal tubular acidosis, retains function but is mistargeted in polarized renal epithelia
Am J Physiol Cell Physiol, October 1, 2006; 291(4): C788 - C801.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
W. F. Boron
Acid-Base Transport by the Renal Proximal Tubule
J. Am. Soc. Nephrol., September 1, 2006; 17(9): 2368 - 2382.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
R. M. Pelis, W. M. Suhre, and S. H. Wright
Functional influence of N-glycosylation in OCT2-mediated tetraethylammonium transport
Am J Physiol Renal Physiol, May 1, 2006; 290(5): F1118 - F1126.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
A. Pushkin and I. Kurtz
SLC4 base (HCO3-, CO32-) transporters: classification, function, structure, genetic diseases, and knockout models
Am J Physiol Renal Physiol, March 1, 2006; 290(3): F580 - F599.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
C. Perry, J. Blaine, H. Le, and I. I. Grichtchenko
PMA- and ANG II-induced PKC regulation of the renal Na+-HCO3- cotransporter (hkNBCe1)
Am J Physiol Renal Physiol, February 1, 2006; 290(2): F417 - F427.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
N. Abuladze, R. Azimov, D. Newman, P. Sassani, W. Liu, S. Tatishchev, A. Pushkin, and I. Kurtz
Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport
J. Physiol., June 15, 2005; 565(3): 717 - 730.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online
Copyright © 2003 by the American Physiological Society.