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Int J Biochem Cell Biol. 2005 May;37(5):927-34. Epub 2005 Jan 8.

The human mitochondrial proteome: oxidative stress, protein modifications and oxidative phosphorylation.

Author information

  • Chemistry Department, Buck Institute for Age Research, 8001 Redwood Blvd, Novato, CA 94945, USA. bgibson@buckinstitute.org

Abstract

Mitochondria are one of the most complex of subcellular organelles and play key roles in many cellular functions including energy production, fatty acid metabolism, pyrimidine biosynthesis, calcium homeostasis, and cell signaling. In recent years, we and other groups have attempted to identify the complete set of proteins that are localized to human mitochondria as a way to better understand its cellular functions and how it communicates with other cell compartment in complex signaling pathways such as oxidative stress and apoptosis. Indeed, there is an increasing interest in understanding the molecular details of oxidative stress and the mitochondrial role in this process, as well as assessing how mitochondrial proteins become damaged or posttranslationally modified as a consequence of a major change in a cell's redox status. In this review, we report on the current status of the human mitochondrial proteome with an emphasis towards understanding how mitochondrial proteins, especially the proteins that make up the respiratory chain or oxidative phosphorylation (OXPHOS) enzymes, are modified in various models of age-related diseases such as cancer and Parkinson's disease (PD).

PMID:
15743667
[PubMed - indexed for MEDLINE]
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