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Volumn 325, Issue 1, 2004, Pages 32-38

Regulation of high glucose-induced apoptosis by mitochondrial NADP +-dependent isocitrate dehydrogenase

Author keywords

Antioxidant enzyme; Apoptosis; Diabetes; HEK293; Isocitrate dehydrogenase

Indexed keywords

COMPLEMENTARY DNA; GLUCOSE; ISOCITRATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 7444244981     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.218     Document Type: Article
Times cited : (20)

References (37)
  • 1
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • M. Brownlee Biochemistry and molecular cell biology of diabetic complications Nature 414 2000 813 820
    • (2000) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 2
    • 0033857531 scopus 로고    scopus 로고
    • The missing link: A single unifying mechanism for diabetic complications
    • T. Nishikawa, D. Edelstein, and M. Brownlee The missing link: a single unifying mechanism for diabetic complications Kidney Int. 58 2000 26 30
    • (2000) Kidney Int. , vol.58 , pp. 26-30
    • Nishikawa, T.1    Edelstein, D.2    Brownlee, M.3
  • 4
    • 0036238441 scopus 로고    scopus 로고
    • Oxidative stress and programmed cell death in diabetic neuropathy
    • M.A. Vincent, M. Brownlee, and J.W. Russell Oxidative stress and programmed cell death in diabetic neuropathy Ann. N. Y. Acad. Sci. 959 2002 368 383
    • (2002) Ann. N. Y. Acad. Sci. , vol.959 , pp. 368-383
    • Vincent, M.A.1    Brownlee, M.2    Russell, J.W.3
  • 5
    • 0141755317 scopus 로고    scopus 로고
    • Reactive oxygen species from mitochondria induce cyclooxygenase-2 gene expression in human mesangial cells: Potential role in diabetic nephropathy
    • S. Kiritoshi, T. Nishikawa, K. Sonoda, D. Kukidome, T. Senokuchi, T. Matsuo, T. Matsumura, H. Tokunaga, M. Brownlee, and E. Araki Reactive oxygen species from mitochondria induce cyclooxygenase-2 gene expression in human mesangial cells: potential role in diabetic nephropathy Diabetes 52 2003 2570 2577
    • (2003) Diabetes , vol.52 , pp. 2570-2577
    • Kiritoshi, S.1    Nishikawa, T.2    Sonoda, K.3    Kukidome, D.4    Senokuchi, T.5    Matsuo, T.6    Matsumura, T.7    Tokunaga, H.8    Brownlee, M.9    Araki, E.10
  • 6
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes
    • S.P. Wolff, and R.T. Dean Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes Biochem. J. 245 1987 243 250
    • (1987) Biochem. J. , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 8
    • 0037036345 scopus 로고    scopus 로고
    • Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells
    • S. Yamagishi, Y. Inagaki, T. Okamoto, S. Amano, K. Koga, M. Takeuchi, and Z. Aakita Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells J. Biol. Chem. 277 2002 20309 20315
    • (2002) J. Biol. Chem. , vol.277 , pp. 20309-20315
    • Yamagishi, S.1    Inagaki, Y.2    Okamoto, T.3    Amano, S.4    Koga, K.5    Takeuchi, M.6    Aakita, Z.7
  • 9
    • 0037984766 scopus 로고    scopus 로고
    • High glucose-induced oxidative stress causes apoptosis in proximal tubular epithelial cells and is mediated by multiple caspases
    • D.A. Allen, S. Harwood, M. Varagunam, M.J. Raftery, and M.M. Yaqoob High glucose-induced oxidative stress causes apoptosis in proximal tubular epithelial cells and is mediated by multiple caspases FASEB J. 17 2003 908 910
    • (2003) FASEB J. , vol.17 , pp. 908-910
    • Allen, D.A.1    Harwood, S.2    Varagunam, M.3    Raftery, M.J.4    Yaqoob, M.M.5
  • 10
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) J. Biol. Chem. 224 1969 6049 6055
    • (1969) J. Biol. Chem. , vol.224 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 11
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol. Rev. 59 1979 527 605
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 12
    • 0033613855 scopus 로고    scopus 로고
    • Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression
    • F. Salvemini, A. Franze, A. Iervolino, S. Filosa, S. Salzano, and M.V. Ursini Enhanced glutathione levels and oxidoresistance mediated by increased glucose-6-phosphate dehydrogenase expression J. Biol. Chem. 274 1999 2750 2757
    • (1999) J. Biol. Chem. , vol.274 , pp. 2750-2757
    • Salvemini, F.1    Franze, A.2    Iervolino, A.3    Filosa, S.4    Salzano, S.5    Ursini, M.V.6
  • 13
    • 0020490598 scopus 로고
    • Superoxide radical inhibits catalase
    • Y. Kono, and I. Fridovich Superoxide radical inhibits catalase J. Biol. Chem. 257 1982 5751 5754
    • (1982) J. Biol. Chem. , vol.257 , pp. 5751-5754
    • Kono, Y.1    Fridovich, I.2
  • 14
    • 0025057048 scopus 로고
    • Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals
    • E. Pigeolet, P. Corbisier, A. Houbion, D. Lambert, C. Michiels, M. Raes, M.D. Zachary, and J. Remacle Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals Mech. Ageing 51 1990 283 297
    • (1990) Mech. Ageing , vol.51 , pp. 283-297
    • Pigeolet, E.1    Corbisier, P.2    Houbion, A.3    Lambert, D.4    Michiels, C.5    Raes, M.6    Zachary, M.D.7    Remacle, J.8
  • 16
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • H.Z. Chae, S.J. Chung, and S.G. Rhee Thioredoxin-dependent peroxide reductase from yeast J. Biol. Chem. 269 1994 27670 27678
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 17
    • 0028283815 scopus 로고
    • Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin
    • S.J. Kwon, J.-W. Park, W.K. Choi, I.H. Kim, and K. Kim Inhibition of metal-catalyzed oxidation systems by a yeast protector protein in the presence of thioredoxin Biochem. Biophys. Res. Commun. 201 1994 8 15
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 8-15
    • Kwon, S.J.1    Park, J.-W.2    Choi, W.K.3    Kim, I.H.4    Kim, K.5
  • 21
    • 0023221206 scopus 로고
    • Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure
    • C.R. Zerez, S.J. Lee, and K.R. Tanaka Spectrophotometric determination of oxidized and reduced pyridine nucleotides in erythrocytes using a single extraction procedure Anal. Biochem. 164 1987 367 373
    • (1987) Anal. Biochem. , vol.164 , pp. 367-373
    • Zerez, C.R.1    Lee, S.J.2    Tanaka, K.R.3
  • 22
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples
    • T.P.M. Akerboom, and H. Sies Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples Methods Enzymol. 77 1981 373 382
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.M.1    Sies, H.2
  • 23
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • M.E. Anderson Determination of glutathione and glutathione disulfide in biological samples Methods Enzymol. 113 1985 548 555
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 24
    • 0026632930 scopus 로고
    • Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein
    • Z.Y. Jiang, J.V. Hunt, and S.P. Wolff Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein Anal. Biochem. 202 1992 384 389
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Z.Y.1    Hunt, J.V.2    Wolff, S.P.3
  • 26
    • 0029982148 scopus 로고    scopus 로고
    • The cytotoxicity of tumor necrosis factor depends on induction of the mitochondrial permeability transition
    • J.G. Pastorino, G. Simbula, K. Yamamoto, P.A. Glascott, R.J. Rothman, and J.L. Farber The cytotoxicity of tumor necrosis factor depends on induction of the mitochondrial permeability transition J. Biol. Chem. 271 1996 29792 29798
    • (1996) J. Biol. Chem. , vol.271 , pp. 29792-29798
    • Pastorino, J.G.1    Simbula, G.2    Yamamoto, K.3    Glascott, P.A.4    Rothman, R.J.5    Farber, J.L.6
  • 28
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • J.W. Baynes Role of oxidative stress in development of complications in diabetes Diabetes 40 1991 405 412
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 29
    • 0033805442 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis
    • K. Kannan, and S.K. Jain Oxidative stress and apoptosis Pathophysiology 7 2000 153 163
    • (2000) Pathophysiology , vol.7 , pp. 153-163
    • Kannan, K.1    Jain, S.K.2
  • 32
    • 0033582533 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells
    • M. Arai, H. Imai, T. Koumura, T. Yoshida, K. Emoto, M. Umeda, N. Chiba, and Y. Nakagawa Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells J. Biol. Chem. 274 1999 4924 4933
    • (1999) J. Biol. Chem. , vol.274 , pp. 4924-4933
    • Arai, M.1    Imai, H.2    Koumura, T.3    Yoshida, T.4    Emoto, K.5    Umeda, M.6    Chiba, N.7    Nakagawa, Y.8
  • 34
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • S.W. Kang, H.Z. Chae, M.S. Seo, K. Kim, I.C. Baines, and S. Rhee Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha J. Biol. Chem. 273 1998 6297 6301
    • (1998) J. Biol. Chem. , vol.273 , pp. 6297-6301
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.6
  • 35
    • 0029082801 scopus 로고
    • Possible function of SP-22, a substrate of mitochondrial ATP-dependent protease, as a radical scavenger
    • S. Watabe, H. Hasegawa, K. Takimoto, Y. Yamamoto, and S. Takahashi Possible function of SP-22, a substrate of mitochondrial ATP-dependent protease, as a radical scavenger Biochem. Biophys. Res. Commun. 213 1995 1010 1016
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1010-1016
    • Watabe, S.1    Hasegawa, H.2    Takimoto, K.3    Yamamoto, Y.4    Takahashi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.