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


     

Am J Physiol Renal Physiol 281: F763-F768, 2001;
0363-6127/01 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 (11)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kraut, J. A.
Right arrow Articles by Sachs, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kraut, J. A.
Right arrow Articles by Sachs, G.
Vol. 281, Issue 4, F763-F768, October 2001

Detection and localization of H+-K+-ATPase isoforms in human kidney

Jeffrey A. Kraut1,2, Kerstin G. Helander3, Herbert F. Helander2,4, Ngozi D. Iroezi1,2, Elizabeth A. Marcus2, and George Sachs2

1 Division of Nephrology and 2 Membrane Biology Laboratory, Research Service and Department of Medicine, Veterans Affairs Greater Los Angeles Health Care System, and University of California School of Medicine, Los Angeles, California 90073; 4 AstraZeneca, Mölndal, Sweden; and 3 Department of Biomedical Laboratory Science, University of Göteborg, Göteborg, Sweden

An H+-K+-ATPase contributes to hydrogen secretion and potassium reabsorption by the rat and rabbit collecting ducts. Transport of these ions appears to be accomplished by one or both of two isoforms of the H+-K+-ATPase, HKalpha 1 and HKalpha 2, because both isoforms are found in the collecting ducts and transport of hydrogen and potassium is attenuated by exposure to inhibitors of these transport proteins. To evaluate whether an H+-K+-ATPase is present in the human kidney, immunohistochemical studies were performed using normal human renal tissue probed with antibodies directed against epitopes of three of the known isoforms of the H+-K+-ATPase, HKalpha 1, HKalpha 2, and HKalpha 4, and the V-type H+-ATPase. Cortical and medullary tissue probed with antibodies against HKalpha 1 showed cytoplasmic staining of intercalated cells that was less intense than that observed in the parietal cells of normal rat stomach stained with the same antibody. Also, weak immunoreactivity was detected in principal cells of the human collecting ducts. Cortical and medullary tissue probed with antibodies directed against HKalpha 4 revealed weak, diffuse staining of intercalated cells of the collecting ducts and occasional light staining of principal cells. Cortical and medullary tissue probed with antibodies directed against the H+-ATPase revealed staining of intercalated cells of the collecting ducts and some cells of the proximal convoluted tubules. By contrast, no discernible staining was noted with the use of the antibody against HKalpha 2. These data indicate that HKalpha 1 and HKalpha 4 are present in the collecting ducts of the human kidney. In this location, these isoforms might contribute to hydrogen and potassium transport by the kidney.

renal hydrogen-potassium-adenosinetriphosphatase; hydrogen; potassium; immunohistochemistry


This article has been cited by other articles:


Home page
 PhysiologyHome page
A. C. Fry and F. E. Karet
Inherited Renal Acidoses
Physiology, June 1, 2007; 22(3): 202 - 211.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
N. B. Pestov, T. V. Korneenko, M. I. Shakhparonov, G. E. Shull, and N. N. Modyanov
Loss of acidification of anterior prostate fluids in Atp12a-null mutant mice indicates that nongastric H-K-ATPase functions as proton pump in vivo
Am J Physiol Cell Physiol, August 1, 2006; 291(2): C366 - C374.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
M. M. Dufner, P. Kirchhoff, C. Remy, P. Hafner, M. K. Muller, S. X. Cheng, L.-Q. Tang, S. C. Hebert, J. P. Geibel, and C. A. Wagner
The calcium-sensing receptor acts as a modulator of gastric acid secretion in freshly isolated human gastric glands
Am J Physiol Gastrointest Liver Physiol, December 1, 2005; 289(6): G1084 - G1090.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
K. P. Choe, J. W. Verlander, C. S. Wingo, and D. H. Evans
A putative H+-K+-ATPase in the Atlantic stingray, Dasyatis sabina: primary sequence and expression in gills
Am J Physiol Regulatory Integrative Comp Physiol, October 1, 2004; 287(4): R981 - R991.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
N. B. Pestov, T. V. Korneenko, R. Radkov, H. Zhao, M. I. Shakhparonov, and N. N. Modyanov
Identification of the {beta}-subunit for nongastric H-K-ATPase in rat anterior prostate
Am J Physiol Cell Physiol, June 1, 2004; 286(6): C1229 - C1237.
[Abstract] [Full Text] [PDF]

Home page
 J. Am. Soc. Nephrol.Home page
F. E. Karet
Inherited Distal Renal Tubular Acidosis
J. Am. Soc. Nephrol., August 1, 2002; 13(8): 2178 - 2184.
[Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
G. Crambert, J.-D. Horisberger, N. N. Modyanov, and K. Geering
Human nongastric H+-K+-ATPase: transport properties of ATP1al1 assembled with different beta -subunits
Am J Physiol Cell Physiol, July 1, 2002; 283(1): C305 - C314.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
N. B. Pestov, T. V. Korneenko, G. Adams, M. Tillekeratne, M. I. Shakhparonov, and N. N. Modyanov
Nongastric H-K-ATPase in rodent prostate: lobe-specific expression and apical localization
Am J Physiol Cell Physiol, April 1, 2002; 282(4): C907 - C916.
[Abstract] [Full Text] [PDF]


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