| Response of the mitochondrial proteome of rat renal proximal convoluted tubules to chronic metabolic acidosis. | |
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MedLine Citation:
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PMID: 23136003 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Metabolic acidosis is a common clinical condition that is caused by a decrease in blood pH and bicarbonate concentration. Increased extraction and mitochondrial catabolism of plasma glutamine within the renal proximal convoluted tubule generates ammonium and bicarbonate ions that facilitate the excretion of acid and partially restore acid-base balance. Previous studies identified only a few mitochondrial proteins, including two key enzymes of glutamine metabolism, which are increased during chronic acidosis. A workflow was developed to characterize the mitochondrial proteome of the proximal convoluted tubule. Based upon the increase in specific activity of cytochrome c oxidase, the isolated mitochondria were enriched eightfold. Two-dimensional liquid chromatography coupled with mass spectrometry was utilized to compare mitochondrial-enriched samples from control and chronic acidotic rats. Proteomic analysis identified 901 proteins in the control and acidotic samples. Further analysis identified 37 peptides that contain an N-ε-acetyl-lysine; of these, 22 are novel sites. Spectral counting analysis revealed 33 proteins that are significantly altered in abundance in response to chronic metabolic acidosis. Western blot analysis was performed to validate the calculated changes in abundance. Thus the current study represents the first comprehensive analysis of the mitochondrial proteome of the rat renal proximal convoluted tubule and its response to metabolic acidosis. |
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Authors:
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Dana M Freund; Jessica E Prenni; Norman P Curthoys |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2012-11-07 |
Journal Detail:
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Title: American journal of physiology. Renal physiology Volume: 304 ISSN: 1522-1466 ISO Abbreviation: Am. J. Physiol. Renal Physiol. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-01-16 Completed Date: 2013-03-06 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 100901990 Medline TA: Am J Physiol Renal Physiol Country: United States |
Other Details:
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Languages: eng Pagination: F145-55 Citation Subset: IM |
Affiliation:
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Dept. of Biochemistry and Molecular Biology, Colorado State Univ., Ft. Collins, CO 80523-1870, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Acetylation Acidosis / metabolism* Ammonium Chloride Animals Blotting, Western Chronic Disease Electron Transport Complex IV / metabolism Gene Expression Regulation / physiology Hypertrophy Kidney Tubules, Proximal / cytology*, pathology, physiology* Lysine / metabolism Male Mitochondria / metabolism* Peroxisomes / enzymology Proteome / metabolism* Rats Rats, Sprague-Dawley Transcriptome |
| Grant Support | |
ID/Acronym/Agency:
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DK-37124/DK/NIDDK NIH HHS; DK-75517/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Proteome; 12125-02-9/Ammonium Chloride; 56-87-1/Lysine; EC 1.9.3.1/Electron Transport Complex IV |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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