Proteomic profiling of the mitochondrial inner membrane of rat renal proximal convoluted tubules

Dana M. Freund, Jessica E. Prenni, Norman P. Curthoys

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

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-e{open}-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 ProteomeXchange with the identifier PXD000121.

Original languageEnglish (US)
Pages (from-to)2495-2499
Number of pages5
JournalProteomics
Volume13
Issue number16
DOIs
StatePublished - Aug 2013

Keywords

  • Animal proteomics
  • Lysine acetylation
  • Mitochondrial inner membrane
  • Proximal convoluted tubule

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