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Oxidation–reduction respiratory chains and ATP synthase complex are localized in detergent‐resistant lipid rafts
Author(s) -
Kim KiBum,
Lee JoongWon,
Lee Chang Seok,
Kim BongWoo,
Choo HyoJung,
Jung SoonYoung,
Chi SungGil,
Yoon YoungSil,
Yoon Gyesoon,
Ko YoungGyu
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500574
Subject(s) - atp synthase , lipid raft , chemistry , biochemistry , raft , microbiology and biotechnology , respiratory chain , enzyme , biology , membrane , organic chemistry , copolymer , polymer
In order to detect and identify ubiquitous lipid raft marker proteins, we isolated lipid rafts from different mouse organs, including the liver, lung, large brain, and kidney, and analyzed their proteins via 2‐DE. Many protein spots were determined to be ubiquitous in all of the lipid rafts, and were annotated via LC and MS/MS. Twelve proteins were identified as ubiquitous raft proteins, and most of these were determined to be mitochondrial proteins, including mortalin, prohibitin, voltage‐dependent anion channel, ATP synthase, NADH dehydrogenase, and ubiquinol‐cytochrome c reductase. Via immunoblotting, these proteins were shown to exist in detergent‐resistant lipid rafts prepared using different organ tissues. Since these oxidation–reduction respiratory chains and ATP synthase complex were detected in detergent‐resistant lipid raft fractions which had been isolated from the plasma membrane but not from the mitochondria, and found in the cell surface when determined by immunofluoresence and immunohistochemistry, we conclude that plasma membrane lipid rafts might contain oxidation–reduction respiratory chains and ATP synthase complex.