Oxidation-reduction respiratory chains and ATP synthase complex are localized in detergent-resistant lipid rafts

被引:76
作者
Kim, KB
Lee, JW
Lee, CS
Kim, BW
Choo, HJ
Jung, SY
Chi, SG
Yoon, YS
Yoon, G
Ko, YG
机构
[1] Korea Univ, Sch Life Sci & Biotechnol, Seoul 136701, South Korea
[2] Ajou Univ, Coll Med, Suwon 441749, Kyunggi, South Korea
关键词
ATP synthase; 2-D PAGE; lipid raft; mitochondria; oxidation-reduction respiratory chains;
D O I
10.1002/pmic.200500574
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2444 / 2453
页数:10
相关论文
共 46 条
[1]   The caveolae membrane system [J].
Anderson, RGW .
ANNUAL REVIEW OF BIOCHEMISTRY, 1998, 67 :199-225
[2]   Lipid raft proteome reveals ATP synthase complex in the cell surface [J].
Bae, TJ ;
Kim, MS ;
Kim, JW ;
Kim, BW ;
Choo, HJ ;
Lee, JW ;
Kim, KB ;
Lee, CS ;
Kim, JH ;
Chang, SY ;
Kang, CY ;
Lee, SW ;
Ko, YG .
PROTEOMICS, 2004, 4 (11) :3536-3548
[3]   Porin is present in the plasma membrane where it is concentrated in caveolae and caveolae-related domains [J].
Bàthori, G ;
Parolini, I ;
Tombola, F ;
Szabò, I ;
Messina, A ;
Oliva, M ;
De Pinto, V ;
Lisanti, M ;
Sargiacomo, M ;
Zoratti, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (42) :29607-29612
[4]   Extensive temporally regulated reorganization of the lipid raft proteome following T-cell antigen receptor triggering [J].
Bini, L ;
Pacini, S ;
Liberatori, S ;
Valensin, S ;
Pellegrini, M ;
Raggiaschi, R ;
Pallini, V ;
Baldari, CT .
BIOCHEMICAL JOURNAL, 2003, 369 :301-309
[5]   A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling [J].
Blagoev, B ;
Kratchmarova, I ;
Ong, SE ;
Nielsen, M ;
Foster, LJ ;
Mann, M .
NATURE BIOTECHNOLOGY, 2003, 21 (03) :315-318
[6]   SORTING OF GPI-ANCHORED PROTEINS TO GLYCOLIPID-ENRICHED MEMBRANE SUBDOMAINS DURING TRANSPORT TO THE APICAL CELL-SURFACE [J].
BROWN, DA ;
ROSE, JK .
CELL, 1992, 68 (03) :533-544
[7]  
Calvo M, 2000, ELECTROPHORESIS, V21, P3386, DOI 10.1002/1522-2683(20001001)21:16<3386::AID-ELPS3386>3.3.CO
[8]  
2-C
[9]   Interaction of the C-terminal domain of p43 and the α subunit of ATP synthase -: Its functional implication in endothelial cell proliferation [J].
Chang, SY ;
Park, SG ;
Kim, S ;
Kang, CY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (10) :8388-8394
[10]   Interaction of a receptor tyrosine kinase, EGF-R, with caveolins - Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities [J].
Couet, J ;
Sargiacomo, M ;
Lisanti, MP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (48) :30429-30438