Inactivation of NADP⁺-dependent Isocitrate Dehydrogenase by Lipid Peroxidation Products

References

• Cerutti, PA. (1985) "Prooxidant states and tumor promotion", Science 227, 375–380.
   PubMed Web of Science ®Google Scholar
• Gutteridge, J.M.C. and Halliwell, B. (2000) "Free radicals and antioxidants in the year 2000", Ann. N. Y. Acad. Sci. 899, 136–147.
   PubMed Web of Science ®Google Scholar
• Ames, B.N., Shigenaga, M.K. and Hagen, T.M. (1993) "Oxidants, antioxidants, and the degenerative diseases of aging", Proc. Natl Acad. Sci. USA 90, 7915–7922.
   PubMed Web of Science ®Google Scholar
• Slater, T.F. (1984) "Free radical mechanism in tissue injury", Biochem., J. 222, 1–15.
   Google Scholar
• Ueda, K., Kobayashi, S., Morita, J. and Komano, T. (1985) "Site-specific DNA damage caused by lipid peroxidation products", Biochim. Biophys. Acta 824, 341–348.
   PubMed Web of Science ®Google Scholar
• Blair, I.A. (2001) "Lipid hydroperoxide-mediated DNA damage", Exp. Gerontol. 36, 1473–1481.
   PubMed Web of Science ®Google Scholar
• McCord, J.M. and Fridovich, I. (1969) "Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)", J. Biol. Chem. 224, 6049–6055.
   Google Scholar
• Chance, B., Sies, H. and Boveris, A. (1979) "Hydropermdde metabolism in mammalian organs", Physiol. Rev. 59,527–605.
   PubMed Web of Science ®Google Scholar
• Salvemini, F., Franze, A., Iervolino, A., Filosa, S., Salzano, S. and Ursini, M.V. (1999) "Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression", J. Biol. Chem. 274, 2750–2757.
   PubMed Web of Science ®Google Scholar
• Kono, Y. and Fridovich, I. (1982) "Superoxide radical inhibits catalase", J. Biol. Chem. 257, 5751–5754.
   PubMed Web of Science ®Google Scholar
• Pigeolet, E., Corbisier, P., Houbion, A., Lambert, D., Michiels, C., Raes, M., Zachary, M.D. and Remade, J. (1990) "Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals", Mech. Ageing 51, 283–297.
   PubMed Web of Science ®Google Scholar
• Tabatabaie, T. and Floyd, R.A. (1994) "Susceptibility of glutathione peroxidase and glutathione reductase to oxi-dative damage and the protective effect of spin trapping agents", Arch. Biochem. Biophys. 314, 112–119.
   PubMed Web of Science ®Google Scholar
• Koshland, D.E., Jr., Walsh, K. and LaPorte, D.C. (1985) "Sensitivity of metabolic fluxes to covalent control", Curr. Top. Cell. Regul. 27, 13–22.
   PubMedGoogle Scholar
• Chae, H.Z., Chung, S.J. and Rhee, S.G. (1994) "Thioredoxin-dependent peroxide reductase from yeast", J. Biol. Chem. 269, 27670–27678.
   PubMed Web of Science ®Google Scholar
• Kwon, S.J., Park, J.-W., Choi, W.K., Kim, I.H. and Kim, K. (1994) "Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin", Biochem. Biophys. Res. Commun. 201, 8–15.
   PubMedGoogle Scholar
• Jo, S.-H., Son, M.-K., Koh, H.-J., Lee, S.-M., Song, I.-H., Kim, Y-0., Lee, YS., Jeong, K-S., Kim, W.B., Park, J.-W., Song, B.J. and Huh, T.-L. (2001) "Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP±-dependent isocitrate dehydrogenase", J. Biol. Chem. 276, 16168–16176.
   PubMedGoogle Scholar
• Lee, S.M., Koh, H.J., Park, D.C., Song, B.J., Huh, T.L. and Park, J.W. (2002) "Cytosolic NADP±-dependent isocitrate dehydrogenase status modulates oxidative damage to cells", Free Radic. Biol. Med. 32, 1185–1196.
   PubMed Web of Science ®Google Scholar
• Dooley, M.M., Sano, N., Kawashima, H. and Nakamura, T. (1990) "Effects of 2,2'-azobis (2-amidinopropane) hydro-chloride in vivo and protection by vitamin E", Free Radic. Biol. Med. 9, 199–204.
   PubMed Web of Science ®Google Scholar
• Smith, D.B. and Johnson, KS. (1988) "Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase", Gene 67, 31–40.
   PubMed Web of Science ®Google Scholar
• Csallany, AS., Der Guan, M., Manwaring, J.D. and Addis, P.B. (1984) "Free malonaldehyde determination in tissues by high-performance liquid chromatography", Anal. Biochem. 146, 277–283.
   Google Scholar
• Graff, G., Anderson, L.A. and Jaques, L.W. (1990) "Preparation and purification of soybean lipoxygenase-derived unsaturated hydroperoxy and hydroxy fatty acids and determination of molar absorptivities of hydroxy fatty acids", Anal. Biochem. 188, 38–47.
   PubMedGoogle Scholar
• Levine, R.L., Willams, J.A., Stadtman, E.R. and Shacter, E. (1994) "Carbonyl assays for determination of mddatively modified proteins", Methods Enzymol. 233, 346–357.
   PubMed Web of Science ®Google Scholar
• Schwarz, M.A., Lazo, J.S., Yalowich, J.C., Reynolds, I., Kagan, V.E., Tyurin, V, Kim, Y.M., Watkins, S.C. and Pitt, B.R. (1994) "Cytoplasmic metallothionein overexpres-sion protects NIH 3T3 cells from tert-butyl hydropermdde toxicity", J. Biol. Chem. 269, 15238–15243.
   PubMed Web of Science ®Google Scholar
• Sundaresan, M., Yu, Z.-X., Ferrans, C.J., Irani, K. and Finkel, T. (1995) "Requirement for generation of H202 for platelet-derived growth factor signal transduction", Science 270, 296–299.
   PubMed Web of Science ®Google Scholar
• Zerez, C.R., Lee, S.J. and Tanaka, K.R. (1987) "Spectro-photometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure", Anal. Biochem. 164, 367–373.
   PubMed Web of Science ®Google Scholar
• Akerboom, T.P.M. and Sies, H. (1981) "Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples", Methods Enzymol. 77, 373–382.
   PubMedGoogle Scholar
• Anderson, M.E. (1985) "Determination of glutathione and glutathione disulfide in biological samples", Methods Enzymol. 113, 548–555.
   PubMed Web of Science ®Google Scholar
• Szweda, L.L. and Stadtman, E.R. (1993) "Oxidative modifi-cation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides by an iron(II)-citrate complex", Arch. Biochem. Biophys. 301, 391–395.
   PubMedGoogle Scholar
• Uchida, K., Szweda, L.I., Chae, H.Z. and Sradtman, E.R. (1993) "Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes", Proc. Natl Acad. Sci. USA 90, 8742–8746.
   PubMed Web of Science ®Google Scholar
• Munkres, K.D. (1976) "Ageing of Neurospora crassa Iv", Mech. Aging Dev. 5, 171–191.
   PubMed Web of Science ®Google Scholar
• Sevanian, A. and Kim, E. (1985) "Phospholipase A2 dependent release of fatty acids from peroxidized mem-branes", J. Free Radic. Biol. Med. 1, 263–271.
   PubMedGoogle Scholar
• Szweda, L.I., Uchida, K., Tsai, L. and Stadtman, E.R. (1993) "Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine", J. Biol. Chem. 268, 3342–3347.
   PubMed Web of Science ®Google Scholar
• Burcham, P.C. and Kuhan, YT. (1997) "Diminished suscepti-bility to proteolysis after protein modification by the lipid permddation product malondialdehyde: inhibitory role for crosslinked and noncrosslinked adducted proteins", Arch. Biochem. Biophys. 340, 331–337.
   PubMed Web of Science ®Google Scholar
• Smyth, G.E. and Colman, RE (1991) "Cysteinyl peptides of pig heart NADP-dependent isocitrate dehydrogenase that are modified upon inactivation by N-ethylmaleimide", J. Biol. Chem. 266, 14918–14925.
   PubMedGoogle Scholar
• Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J. (2002) "Crystal structure of porcine mitochondrial NADP±-dependent isocitrate dehydrogenase complexed with Mn2±and isocitrate. Insights into the enzyme mechanism", J. Biol. Chem. 277, 43454–43462.
   PubMed Web of Science ®Google Scholar
• Scott, M.D., Zuo, L., Lubin, B.H. and Chiu, D.Y.T. (1991) "NADPH, not glutathione, status modulates oxidant sensi-tivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes", Blood 77, 2059–2064.
   PubMed Web of Science ®Google Scholar
• Pandolfi, EP., Sonati, E, Rivi, R., Mason, P., Grosveld, F. and Luzzatto, L. (1995) "Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress", EMBO J. 14, 5209–5215.
   PubMed Web of Science ®Google Scholar
• Kletzien, R.F., Harris, P.K.W. and Foellmi, L.A. (1994) "Glucose-6-phosphate dehydrogenase: a housekeeping enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress", FASEB J. 8, 174–181.
   PubMed Web of Science ®Google Scholar
• Veech, R.L., Eggleston, L.V. and Krebs, HA. (1969) "The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver", Biochem. J. 115, 609–619.
   PubMed Web of Science ®Google Scholar
• Sun, L., Sun, T.T. and Lavker, R.A. (1999) "Identification of a cytosolic NADP±-dependent isocitrate dehydrogenase that is preferentially expressed in bovine corneal epithelium. A corneal epithelial crystalline", J. Biol. Chem. 274, 17334–17341.
   PubMed Web of Science ®Google Scholar
• Hruszkewycz, A.M. (1988) "Evidence for mitochondrial DNA damage by lipid peroxidation", Biochem. Biophys. Res. Commun. 153, 191–197.
   PubMed Web of Science ®Google Scholar
• Arai, M., Imai, H., Koumura, T., Yoshida, T., Emoto, K., Umeda, M., Chiba, N. and Nakagawa, Y. (1999) "Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells", J. Biol. Chem. 274, 4924–4933.
   PubMed Web of Science ®Google Scholar
• Araki, M., Nanri, H., Ejima, K., Murasato, Y., Fujiwara, T., Nakashima, Y. and Ikeda, M. (1999) "Antioxidant function of the mitochondrial protein SP-22 in the cardiovascular system", J. Biol. Chem. 274, 2271–2278.
   PubMed Web of Science ®Google Scholar
• Kang, S.W., Chae, HZ., Seo, MS., Kim, K., Baines, IC. and Rhee, S.G. (1998) "Mammalian permdredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-a", J. Biol. Chem. 273, 6297–6301.
   PubMed Web of Science ®Google Scholar
• Watabe, S., Hasegawa, H., Takimoto, K., Yamamoto, Y. and Takahashi, S.Y. (1995) "Possible function of SP-22, a substrate of mitochondrial ATP-dependent protease, as a radical scavenger", Biochem. Biophys. Res. Commun. 213, 1010–1016.
   PubMed Web of Science ®Google Scholar
• Knoops, B., Clippe, A., Bogard, C., Arsalane, K., Wattiez, R., Hermans, C., Duconseille, E., Falmagne, P. and Bernard, A. (1999) "Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family", J. Biol Chem. 274, 30451–30458.
   PubMed Web of Science ®Google Scholar