Mitochondrial proteomics

Abstract

Abstract. Alteration of the mitochondrial proteome and altered mitochondrial function has been implicated in a variety of degenerative\rdiseases, heart disease, aging and cancer. Based upon the human genome there is estimated to be approximately 1000 to 2000\rproteins constituting the mitochondrial proteome. Despite the ability of a traditional proteomic approach involving two-dimensional\rgel electrophoresis (2-DE) to resolve and identify thousands of proteins in a single gel, just over 600 mitochondrial proteins\rhave been identified and characterized at the molecular level. The limitations and recent advances of 2-DE in its ability\rto study mitochondrial proteins and create a database of the mitochondrial proteome is discussed, as well as the alternative\rmethods that are being employed, including different mass spectrometry based approaches following both one-dimensional SDS-PAGE\rand gel-free approaches, blue native gel electrophoresis (BN-PAGE), proteome simplification by submitochondrial fractionation,\rand affinity chromatography. In addition, the successful application of proteomics to the investigation of some specific mitochondrial\rcardiomyopathies is discussed.