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Vol. 100, No. 3, 2005
Issue release date: July 2005
Section title: Original Paper
Nephron Physiol 2005;100:p31–p42
(DOI:10.1159/000085114)

Distribution of Rab GTPases in Mouse Kidney and Comparison with Vacuolar H+-ATPase

Curtis L.M. · Gluck S.
Departments of aMedicine and bAnatomy and Cell Biology, University of Florida, Gainesville, Fla., USA

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Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 8/28/2004
Accepted: 11/7/2004
Published online: 6/10/2005

Number of Print Pages: 1
Number of Figures: 7
Number of Tables: 2

ISSN: (Print)
eISSN: 1660-2137 (Online)

For additional information: http://www.karger.com/NEP

Abstract

Background: Vacuolar H+-ATPases (V-ATPases) are essential for renal bicarbonate transport in both the proximal and distal nephron. Regulation of proton transport occurs, in part, by vesicle-mediated traffic of V-ATPases between intracellular vacuoles and the plasma membrane. Although the proteins involved in regulated V-ATPase traffic are largely unknown, Rab GTPases have a central role in the traffic and recycling of other membrane proteins. Methods: To identify candidate Rab GTPases potentially involved in V-ATPase traffic, immunocytochemical and subcellular fractionation studies were used to evaluate the distribution to sites of abundant V-ATPase of 5 Rab GTPases expressed in kidney, Rab5a, Rab11, Rab13, Rab18, and Rab20. Results: The immunocytochemical distribution of Rab5a and Rab13 and the subcellular distribution of Rab18 were not compatible with a role in V-ATPase traffic. In contrast, Rab11 colocalized with V-ATPase in apical regions of proximal tubule, and Rab20 colocalized with the enzyme in intercalated cells. Rab11 and Rab20 were enriched in membrane fractions that were also enriched in V-ATPase B2 and B1 subunit isoforms, respectively. Conclusions: The immunohistochemical data in combination with the membrane fractionation studies are consistent with a potential role for Rab11 and Rab20 in regulating V-ATPase traffic in specific segments of the nephron.


  

Author Contacts

Lisa M. Curtis, PhD
Department of Microbiology, WTI 387
1824 6th Avenue South, University of Alabama at Birmingham
Birmingham AL 35294 (USA)
Tel. +1 205 975 7154, Fax +1 205 934 1875, E-Mail lmcurtis@uab.edu

  

Article Information

Received: August 28, 2004
Accepted: November 7, 2004
Published online: April 15, 2005
Number of Print Pages : 12
Number of Figures : 7, Number of Tables : 2, Number of References : 39

  

Publication Details

Nephron Physiology

Vol. 100, No. 3, Year 2005 (Cover Date: July 2005)

Journal Editor: Unwin, R.J. (London)
ISSN: 1660–2137 (print), 1660–2137 (Online)

For additional information: http://www.karger.com/nep


Article / Publication Details

First-Page Preview
Abstract of Original Paper

Received: 8/28/2004
Accepted: 11/7/2004
Published online: 6/10/2005

Number of Print Pages: 1
Number of Figures: 7
Number of Tables: 2

ISSN: (Print)
eISSN: 1660-2137 (Online)

For additional information: http://www.karger.com/NEP


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