Characterization of the human heart mitochondrial proteome.

Autor: Taylor SW; MitoKor, 11494 Sorrento Valley Road, San Diego, California 92121, USA. taylors@mitokor.com, Fahy E, Zhang B, Glenn GM, Warnock DE, Wiley S, Murphy AN, Gaucher SP, Capaldi RA, Gibson BW, Ghosh SS
Jazyk: angličtina
Zdroj: Nature biotechnology [Nat Biotechnol] 2003 Mar; Vol. 21 (3), pp. 281-6. Date of Electronic Publication: 2003 Feb 18.
DOI: 10.1038/nbt793
Abstrakt: To gain a better understanding of the critical role of mitochondria in cell function, we have compiled an extensive catalogue of the mitochondrial proteome using highly purified mitochondria from normal human heart tissue. Sucrose gradient centrifugation was employed to partially resolve protein complexes whose individual protein components were separated by one-dimensional PAGE. Total in-gel processing and subsequent detection by mass spectrometry and rigorous bioinformatic analysis yielded a total of 615 distinct protein identifications. All protein pI values, molecular weight ranges, and hydrophobicities were represented. The coverage of the known subunits of the oxidative phosphorylation machinery within the inner mitochondrial membrane was >90%. A significant proportion of identified proteins are involved in signaling, RNA, DNA, and protein synthesis, ion transport, and lipid metabolism. The biochemical roles of 19% of the identified proteins have not been defined. This database of proteins provides a comprehensive resource for the discovery of novel mitochondrial functions and pathways.
Databáze: MEDLINE