Document Detail


Role of the Rhesus glycoprotein, Rh B glycoprotein, in renal ammonia excretion.
MedLine Citation:
PMID:  20719974     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Rh B glycoprotein (Rhbg) is a member of the Rh glycoprotein family of ammonia transporters. In the current study, we examine Rhbg's role in basal and acidosis-stimulated acid-base homeostasis. Metabolic acidosis induced by HCl administration increased Rhbg expression in both the cortex and outer medulla. To test the functional significance of increased Rhbg expression, we used a Cre-loxP approach to generate mice with intercalated cell-specific Rhbg knockout (IC-Rhbg-KO). On normal diet, intercalated cell-specific Rhbg deletion did not alter urine ammonia excretion, pH, or titratable acid excretion significantly, but it did decrease glutamine synthetase expression in the outer medulla significantly. After metabolic acidosis was induced, urinary ammonia excretion was significantly less in IC-Rhbg-KO than in control (C) mice on days 2-4 of acid loading, but not on day 5. Urine pH and titratable acid excretion and dietary acid intake did not differ significantly between acid-loaded IC-Rhcg-KO and C mice. In IC-Rhbg-KO mice, acid loading increased connecting segment (CNT) cell and outer medullary collecting duct principal cell Rhbg expression. In both C and IC-Rhbg-KO mice, acid loading decreased glutamine synthetase in both the cortex and outer medulla; the decrease on day 3 was similar in IC-Rhbg-KO and C mice, but on day 5 it was significantly greater in IC-Rhbg-KO than in C mice. We conclude 1) intercalated cell Rhbg contributes to acidosis-stimulated renal ammonia excretion, 2) Rhbg in CNT and principal cells may contribute to renal ammonia excretion, and 3) decreased glutamine synthetase expression may enable normal rates of ammonia excretion under both basal conditions and on day 5 of acid loading in IC-Rhbg-KO mice.
Authors:
Jesse M Bishop; Jill W Verlander; Hyun-Wook Lee; Raoul D Nelson; Arthur J Weiner; Mary E Handlogten; I David Weiner
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2010-08-18
Journal Detail:
Title:  American journal of physiology. Renal physiology     Volume:  299     ISSN:  1522-1466     ISO Abbreviation:  Am. J. Physiol. Renal Physiol.     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-11-04     Completed Date:  2010-12-02     Revised Date:  2013-05-28    
Medline Journal Info:
Nlm Unique ID:  100901990     Medline TA:  Am J Physiol Renal Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  F1065-77     Citation Subset:  IM    
Affiliation:
Div. of Nephrology, Hypertension, and Transplantation, P.O. Box 100224, Univ. of Florida College of Medicine, Gainesville, FL 32610-0224, USA.
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MeSH Terms
Descriptor/Qualifier:
Acidosis / genetics,  metabolism
Acids / pharmacology
Alleles
Ammonia / urine*
Animals
Bicarbonates / blood
Blotting, Western
Diet
Electrolytes / metabolism
Gene Deletion
Gene Expression Regulation, Enzymologic / physiology
Glutamate-Ammonia Ligase / biosynthesis
Glycoproteins / genetics,  metabolism*
Immunohistochemistry
Kidney / metabolism*
Membrane Transport Proteins / genetics,  metabolism*
Mice
Mice, Inbred C57BL
Mice, Knockout
Mice, Transgenic
Potassium / blood
Grant Support
ID/Acronym/Agency:
R01 DK045788/DK/NIDDK NIH HHS; R01 DK045788-15/DK/NIDDK NIH HHS; R01-DK-45788/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Acids; 0/Bicarbonates; 0/Electrolytes; 0/Glycoproteins; 0/Membrane Transport Proteins; 0/RhBG protein, mouse; 7440-09-7/Potassium; 7664-41-7/Ammonia; EC 6.3.1.2/Glutamate-Ammonia Ligase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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