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Proteomic profiling of the mitochondrial inner membrane of rat renal proximal convoluted tubules
Author(s) -
Freund Dana M.,
Prenni Jessica E.,
Curthoys Norman P.
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200558
Subject(s) - inner mitochondrial membrane , inner membrane , proteomics , microbiology and biotechnology , mitochondrion , chemistry , biology , biochemistry , gene
The proximal convoluted tubule is the primary site of renal fluid, electrolyte, and nutrient reabsorption, processes that consume large amounts of adenosine‐5′‐triphosphate. Previous proteomic studies have profiled the adaptions that occur in this segment of the nephron in response to the onset of metabolic acidosis. To extend this analysis, a proteomic workflow was developed to characterize the proteome of the mitochondrial inner membrane of the rat renal proximal convoluted tubule. Separation by LC coupled with analysis by MS / MS ( LC ‐ MS / MS ) confidently identified 206 proteins in the combined samples. Further proteomic analysis identified 14 peptides that contain an N ‐ɛ‐acetyl‐lysine, seven of which are novel sites. This study provides the first proteomic profile of the mitochondrial inner membrane proteome of this segment of the rat renal nephron. The MS data have been deposited in the P roteome X change with the identifier PXD 000121.