A metabolic model describing the H2O2 elimination by mammalian cells including H2O2 permeation through cytoplasmic and peroxisomal membranes: Comparison with experimental data

Biochimica et Biophysica Acta - General Subjects

Volumn 1673, Issue 3, 2004, Pages 149-159

  Makino, Nobuo ^a   Sasaki, Kayoko ^a   Hashida, Kanae ^a   Sakakura, Yuki ^a  

^a IBARAKI PREFECTURAL UNIVERSITY OF HEALTH SCIENCES   (Japan)

Author keywords

6 phosphogluconate dehydrogenase; 6PGD; Catalase; Endothelial cell; G6P; G6PD; glucose 6 phosphate; glucose 6 phosphate dehydrogenase; glutathione peroxidase; Glutathione peroxidase; glutathione reductase; GPx; GR; Hydrogen peroxide; Metabolic model; PC12 cell

Indexed keywords

CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL LINE; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CELL STRAIN; CONCENTRATION RESPONSE; CYTOSOL; ENZYME ACTIVITY; ENZYME MECHANISM; FIBROBLAST; HUMAN; HUMAN CELL; MAMMAL CELL; MOLECULAR MODEL; NONHUMAN; PENTOSE PHOSPHATE CYCLE; PEROXISOME; PRIORITY JOURNAL; RAT; STEADY STATE;

ANIMALS; CELLS, CULTURED; CYTOPLASM; HUMANS; HYDROGEN PEROXIDE; MODELS, BIOLOGICAL; NADP; PERMEABILITY; PEROXISOMES;

MAMMALIA;

EID: 3242774397     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.04.011     Document Type: Article

References (29)

1. Hofmann B., Hecht H.J., Flohé L. Peroxiredoxins. Biol. Chem. 383:2002;347-364
2. Makino N., Mochizuki Y., Bannai S., Sugita Y. Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. J. Biol. Chem. 269:1994;1020-1025
3. Sasaki K., Bannai S., Makino N. Kinetics of hydrogen peroxide elimination by human umbilical vein endothelial cells in culture. Biochim. Biophys. Acta. 1380:1998;275-288
4. Hashida K., Sakakura Y., Makino N. Kinetic studies on the hydrogen peroxide elimination by cultured PC12 cells: rate limitation by glucose-6-phosphate dehydrogenase. Biochim. Biophys. Acta. 1572:2002;85-90
5. +. Biochem. J. 210:1983;685-693
6. Mendes P. GEPASI: a software package for modelling the dynamics, steady states and control of biochemical and other systems. Comput. Appl. Biosci. 9:1993;563-571
7. Straume M., Johnson M.L. Analysis of residuals: criteria for determining goodness-of-fit. Methods Enzymol. 210:1992;87-105
8. Seaver L.C., Imlay J.A. Hydrogen peroxide fluxes and compartmentalization inside growing Escherichia coli. J. Bacteriol. 183:2001;7182-7189
9. Carlberg I., Mannervik B. Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J. Biol. Chem. 250:1975;5475-5480
10. Makino N., Bannai S., Sugita Y. Kinetic studies on the removal of extracellular tert-butyl hydroperoxide by cultured fibroblasts. Biochim. Biophys. Acta. 1243:1995;503-508
11. Cohen G., Hochstein P. Glutathione peroxidase: the primary agent for the elimination of hydrogen peroxide in erythrocytes. Biochemistry. 2:1963;1420-1428
12. 2. Arch. Biochem. Biophys. 210:1981;505-516
13. Björkman U., Eknolm R. Hydrogen peroxide degradation and glutathione peroxidase activity in cultures of thyroid cells. Mol. Cell. Endocrinol. 111:1995;99-107
14. Boveris A., Oshino N., Chance B. The cellular production of hydrogen peroxide. Biochem. J. 128:1972;617-630
15. Stone J.R. An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems. Arch. Biochem. Biophys. 422:2004;119-124
16. de Duve C., Baudhuin P. Perosixomes (microbodies and related particles). Physiol. Rev. 46:1966;323-357
17. Mathai J.C., Sitaramam V. Stretch sensitivity of transmembrane mobility of hydrogen peroxide through voids in the bilayer. Role of cardiolipin. J. Biol. Chem. 269:1994;17784-17793
18. 2 gradients across biomembranes. FEBS Lett. 475:2000;121-126
19. Sampath D., Jackson G.R., Werrbach-Perez K., Perez-Polo J.R. Effects of nerve growth factor on glutathione peroxidase and catalase in PC12 cells. J. Neurochem. 62:1994;2476-2479
20. 2 in Saccharomyces cerevisiae. J. Biol. Chem. 279:2004;6501-6506
21. Damier P., Hirsch E.C., Zhang P., Agid Y., Javoy-Agid F. Glutathione peroxidase, glial cells and Parkinson's disease. Neuroscience. 52:1993;1-6
22. Ariga T., Macala L.J., Saito M., Margolis R.K., Greene L.A., Margolis R.U., Yu R.K. Lipid composition of PC12 pheochromocytoma cells: characterization of globoside as a major neutral glycolipid. Biochemistry. 27:1988;52-58
23. Sabate L., Franco R., Canela E.I., Centelles J.J., Cascante M. A model of the pentose phosphate pathway in rat liver cells. Mol. Cell. Biochem. 142:1995;9-17
24. Kanji M.I., Toews M.L., Carper W.R. A kinetic study of glucose-6-phosphate dehydrogenase. J. Biol. Chem. 251:1976;2258-2262
25. m enzyme. Biochem. Biophys. Res. Commun. 71:1976;1313-1318
26. Flohé L., Loschen G., Guenzler W.A., Eichele E. Glutathione peroxidase: V. The kinetic mechanism. Hoppe-Seyler Z. Physiol. Chem. 353:1972;987-999
27. Thorburn D.R., Kuchel P.W. Regulation of the human-erythrocyte hexose-monophosphate shunt under conditions of oxidative stress. A study using NMR spectroscopy, a kinetic isotope effect, a reconstituted system and computer simulation. Eur. J. Biochem. 150:1985;371-386
28. de Duve C. The separation and characterization of subcellular particles. Harvey Lect. 59:1965;49-87
29. 2 across water channels. J. Exp. Bot. 51:2000;2053-2066