Mitochondrial gene-knockout (ρ0) cells: A versatile model for exploring the secrets of trans-plasma membrane electron transport

BioFactors

Volumn 20, Issue 4, 2004, Pages 213-220

  Scarlett, Debbie Jane ^a   Herst, Patries ^a,b   Tan, An ^a   Prata, Cecilia ^c   Berridge, Michael ^a  

^a MALAGHAN INSTITUTE OF MEDICAL RESEARCH   (New Zealand)

^b UNIVERSITY OF OTAGO   (New Zealand)

^c UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

CNOX; Non mitochondrial oxygen consumption; Trans plasma membrane electron transport; WST 1; 0 cells

Indexed keywords

OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; TETRAZOLIUM;

ARTICLE; CELL GROWTH; CELL MEMBRANE PERMEABILITY; CELL MEMBRANE TRANSPORT; CELL STRAIN; CELL SURFACE; ELECTRON; ELECTRON TRANSPORT; INTRACELLULAR SPACE; KNOCKOUT GENE; MITOCHONDRIAL GENETICS; OXYGEN CONSUMPTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; UPREGULATION;

EID: 13444310780     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520200404     Document Type: Article

References (23)

1. M.V. Berridge and A.S. Tan, Trans-plasma membrane electron transport: a cellular assay for NADH- and NADPH-oxidase based on extracellular, superoxide-mediated reduction of the sulfonated tetrazolium salt WST-1, Protoplasma 205 (1998), 74-82.
2. M.V. Berridge and A.S. Tan, High-capacity redox control at the plasma membrane of mammalian cells: trans-membrane, cell surface, and serum NADH-oxidases, Antiox. Redox Signal. 2 (2000), 231-242.
3. M.V. Berridge and A.S. Tan, Cell-surface NAD(P)H-oxidase: relationship to trans-plasma membrane NADH-oxidoreductase and a potential source of circulating NADH-oxidase, Antiox. Redox Signal. 2 (2000), 277-288.
4. M.D. Brand, L.F. Chien, E.K. Ainscow, D.F. Rolfe and R.K. Porter, The causes and functions of mitochondrial proton leak, Biochim. Biophys. Acta 1187 (1994), 132-139.
5. N.S. Chandel, E. Maltepe, E. Goldwasser, C.E. Mathieu, M.C. Simon and P.T. Schumacker, Mitochondrial reactive oxygen species trigger hypoxia-induced transcription, Proc. Natl. Acad. Sci. USA 95 (1998), 11715-11720.
6. P. Desjardins, E. Frost and R. Morais, Ethidium bromide-induced loss of mitochondrial DNA from primary chicken embryo fibroblasts, Mol. Cell. Biol. 5 (1985), 1163-1169.
7. 10 increase at the plasma membrane, Biochem. Biophys. Res. Commun. 234 (1997), 79-81.
8. M. Grégoire, R. Morais, M.A. Quilliam and D. Gravel, On auxotrophy for pyrimidines of respiration-deficient chick embryo cells, Eur. J. Biochem. 142 (1984), 49-55.
9. P.M. Herst, A.S. Tan, D.-J.G. Scarlett and M.V. Berridge, Cell surface oxygen consumption by mitochondrial gene knockout cells, Biochim. Biophys. Acta 1656 (2004), 79-87.
10. 0 tumor cells: a model for studying whether mitochondria are targets for rhodamine 123, doxorubicin, and other drugs, Biochem. Pharmacol. 60 (2000), 1897-1905.
11. A.M. Joseph, A.A. Rungi, B.H. Robinson and D.A. Hood, Compensatory responses of protein import and transcription factor expression in mitochondrial DNA defects, Am. J. Physiol. Cell Physiol. 286 (2003), C867-C875.
12. M.P. King and G. Attardi, Human cells lacking mtDNA: re-population with exogenous mitochondria by complementation, Science 246 (1989), 500-503.
13. M.E. Kolbuch-Braddon, E. Peterhans, R. Stocker and M.J. Weidemann, Oxygen uptake associated with Sendai-virus-stimulated chemiluminescence in rat thymocytes contains a significant non-mitochondrial component, Biochem. J. 222 (1984), 541-551.
14. 0 cells, J. Biol. Chem. 269 (1994), 30097-30100.
15. J.D. Ly and A. Lawen, Transplasma membrane electron transport: enzymes involved and biological function, Redox Report 8 (2003), 1-19.
16. 10 putatively acting through the plasma membrane oxidase, Biochem. Mol. Biol. Int. 31 (1993), 997-1005.
17. R. Morais, M. Grégoire, E. Jeannotte and D. Gravel, Chick embryo cells rendered respiration-deficient by chloramphenicol and ethidium bromide are auxotrophic for pyrimidines, Biochem. Biophys. Res. Commun. 94 (1980), 71-77.
18. D.J. Morré and D.M. Morré, Cell surface NADH oxidases (ECTO-NOX proteins) with roles in cancer, cellular time-keeping, growth, aging and neurodegenerative diseases, Free Radic. Res. 37 (2003), 795-808.
19. M. Saraste, Oxidative phosphorylation at the fin de siécle, Science 283 (1999), 1488-1493.
20. D. Sedlak, D.M. Morré and D.J. Morré, A drug-unresponsive and protease-resistant CNOX protein from human sera, Arch. Biochem. Biophys. 386 (2001), 106-116.
21. 0) mutants, Biophys. J. 84 (2003), 1291-1298.
22. A.S. Tan and M.V. Berridge, Distinct trans-plasma membrane redox pathways reduce cell-impermeable dyes in HeLa cells, Redox Rep. (2004), in press.
23. O. Warburg, On the origin of cancer cells, Science 123 (1956), 309-314.