Mitochondrial proteome, human

VAN Dorsselaer, A., Lunardi.J., Rabilloud, T. (2003). Progress in the definition of a reference human mitochondrial proteome. Proleomics 3, 157-167. 

It has been predicted that the human mitochondrial proteome comprises around 1500 distinct proteins (Taylor et al., 2003). This level of complexity... 

Rabilloud, T., Kieffer, S., Procaccio, V., Louwagie, M., Courchesne, P.L., Patterson, S.D., Martinez, P., Garin, J., and Lunardi, J., 1998, Two-dimensional electrophoresis of human placental mitochondria and protein identification by mass spectrometry toward a human mitochondrial proteome. Electrophoresis. 19 1006-1014. 

Gaucher, S.P., Taylor, S.W., Fahy, E., Zhang, B., Wamock, D.E., Ghosh, S.S., Gibson, B.W. (2004). Expanded coverage of the human heart mitochondrial proteome using multidimensional liquid chromatography coupled with tandem mass spectrometry. J. Proteome Res. 3, 495-505. 

Scharfe C et al. MITOP, the mitochondrial proteome database 2000 update. Nucleic Acids Res 2000 28 155-158. Molloy MP et al. Establishment of the human reflex tear two-dimensional polyacrylamide gel electrophoresis reference map new proteins of potential diagnostic value. Electrophoresis 1997 18 2811-2815. 

In human mitochondria, more than 600 proteins of 2000 proteins coded by mitochondrial and nuclear genes have been fully identified. These proteins include proteins of different pi, molecular weight, hydrophobicity, and localization, but they are all predominantly from the inner membrane of mitochondria. Many proteins were involved in energy production, signaling, biosynthesis, and ion transport. Similar amounts of proteins have been identified in the mitochondria of rats and mice by proteomic studies. In plants, the mitochondrial proteome of Arabidopsis has been well characterized. 

Rezaul, K L. Wu, V. Mayya, S.-n Wang, and D. Han. 2005. A systematic characterization of mitochondrial proteome from human T leukemia cells. Mol. Cell Proteom. 4, 169. 

Another approach to overcoming the limitations inherent in the lEF dimension of 2-DE is to use alternative types of 2-D separations. 2-D blue native (BN) electrophoresis (Schagger and von Jagow, 1991) can be used to separate membrane and other functional protein complexes as intact, enzymatically active complexes in the first dimension. This is followed with a second-dimension separation by Tricine-SDS-PAGE to separate the complexes into their component subunits. This method, combined with protein identification by MALDI PMF, has been applied to several studies of the mitochondrial proteome (Brookes et al., 2002 Kraft et al., 2001). In a study of human heart mitochondria using BN/SDS-PAGE, the individual subunits of all five complexes of the oxidative phosphorylation system were represented and a novel variant of cytochrome c oxidase subunit Vic was reported (Devreese et al., 2002). 

Theravath TP, Czerny C, Ramshesh VK, Zhong Z, Chavin KD, Lemasters JJ (2008) C-Jun N-terminal kinase 2 promotes graft injury via the mitochondrial ptameability transitirai after mouse liver transplantation. Am J Transplant 8(9) 1819-1828 Thome-Kromer B, Bonk 1, Klatt M, Nebrich G, Taufinann M, Bryant S, Wacker U, Kopke A (2003) Toward the identification of liver toxicity markers a proteome study in human cell culture and rats. Proteomics 3(10) 1835-1862... 

An alternative approach to increasing proteomic coverage is based on the analysis of isolated intact mitochondrial protein complexes. One strategy is based on the use of sucrose density gradients to separate intact mitochondrial complexes solubilised with n-dodecyl- 3-D-maltoside (Hanson et al., 2001). Initially the proteins from the individual fractions were analysed by 2-DE. However, subsequently this approach has been coupled with 1-D SDS-PAGE and MALDI PMF analysis of tryptic digests of excised protein bands (Taylor et al., 2003). When applied to human heart mitochondria, this... 

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