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Redox Report
Communications in Free Radical Research
Volume 8, 2003 - Issue 1
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Research Articles

Redox regulation of homocysteine-dependent glutathione synthesis

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Pages 57-63 | Published online: 19 Jul 2013

REFERENCES

  • Martensson J, Meister A. Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester. Proc Natl Acad Sci USA 1989; 86: 471–475.
  • Jha N, Jurma O, Lalli G et al. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J Biol Chem 2000; 275: 26096–26101.
  • Merad-Boudia M, Nicole A, Santiard-Baron D, Saille C, Ceballos-Picot I. Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells: Relevance to Parkinson's disease. Biochem Pharmacol 1998; 56: 645–655.
  • Nicole A, Santiard-Baron D, Ceballos-Picot I. Direct evidence for glutathione as mediator of apoptosis in neuronal cells. Biomed Pharmacother 1998; 52: 349–355.
  • Meister A, Anderson ME. Glutathione. Annu Rev Biochem 1983; 52: 711–760.
  • Meister A. Glutathione biosynthesis and its inhibition. Methods Enzymol 1995; 252: 26–30.
  • Meister A. Glutathione metabolism. Methods Enzymol 1995; 251: 3–7.
  • Huang ZA, Yang H, Chen C, Zeng Z, Lu SC. Inducers of gamma-glutamylcysteine synthetase and their effects on glutathione synthetase expression. Biochim Biophys Acta 2000; 1493: 48–55.
  • Lu SC. Regulation of glutathione synthesis. Curr Top Cell Regul2000; 36: 95–116.
  • Yao KS, Godwin AK, Johnson SW, Ozols RF, O'Dwyer PJ, Hamilton TC. Evidence for altered regulation of gamma-glutamylcysteine synthetase gene expression among cisplatin-sensitive and cisplatin-resistant human ovarian cancer cell lines. Cancer Res 1995; 55: 4367–4374.
  • Sekhar KR, Long M, Long J, Xu ZQ, Summar ML, Freeman ML. Alteration of transcriptional and post-transcriptional expression of gamma-glutamylcysteine synthetase by diethyl maleate. Radiat Res 1997; 147: 592–597.
  • Morales A, Garcia-Ruiz C, Miranda M et al. Tumor necrosis factor increases hepatocellular glutathione by transcriptional regulation of the heavy subunit chain of gamma- glutamyl-cysteine synthetase. J Biol Chem 1997; 272: 30371–30379.
  • Tian L, Shi MM, Forman HJ. Increased transcription of the regulatory subunit of gamma-glutamylcysteine synthetase in rat lung epithelial L2 cells exposed to oxidative stress or glutathione depletion. Arch Biochem Biophys 1997; 342: 126–133.
  • Mulcahy RT, Wartman MA, Bailey HH, Gipp JJ. Constitutive and beta-naphthoflavone-induced expression of the human gamma-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/tre sequence. J Biol Chem 1997; 272: 7445–7454.
  • Lu SC. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J 1999; 13: 1169–1183.
  • Mulcahy RT, Gipp JJ. Identification of a putative antioxidant response element in the 5' -flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun 1995; 209: 227–233.
  • Mosharov E, Cranford MR, Banerjee R. The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 2000; 39: 13005–13011.
  • Chen Z, Chakraborty S, Banerjee R. Demonstration that the mammalian methionine synthases are predominantly cobalamin-loaded. J Biol Chem 1995; 270: 19246–19249.
  • Taoka S, Ohja S, Shan X, Kruger WD, Banerjee R. Evidence for heme-mediated redox regulation of human cystathionine p-synthase activity. J Biol Chem 1998; 273: 25179–25184.
  • Liu RM, Gao L, Choi J, Fonnan HJ. Gamma-glutamylcysteine synthetase: mRNA stabilization and independent subunit transcription by 4-hydroxy-2-nonenal. Am J Physiol 1998; 275: L861–L869.
  • Abeles RH, Walsh C. Acetylenic enzyme inactivators. Inactivation of y-cystathionase. J Am Chem Soc 1973; 95: 6124–6125.
  • Rao AM, Drake MR, Stipanuk MH. Role of the transsulfuration pathway and of y-cystathionase activity in the formation of cysteine and sulfate from methionine in rat hepatocytes. J Nutr 1990; 120: 837–845.
  • Orrenius S, Nobel CS, van den Dobbelsteen DJ, Burkitt MJ, Slater AF. Dithiocarbamates and the redox regulation of cell death. Biochem Soc Trans 1996; 24: 1032–1038.
  • Lutz LM, Glende Jr EA, Recknagel RO. Protection by diethyldithiocarbamate against carbon tetrachloride lethality in rats and against carbon tetrachloride-induced lipid peroxidation in vitro. Biochem Pharmacol 1973; 22: 1729–1734.
  • Bartoli GM, Muller A, Cadenas E, Sies H. Antioxidant effect of diethyldithiocarbamate on microsomal lipid peroxidation assessed by low-level chemiluminescence and alkane production. FEBS Lett 1983; 164: 371–374.
  • Meyer M, Schreck R, Baeuerle PA. H202 and antioxidants have opposite effects on activation of NF-kappaB and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J 1993; 12: 2005–2015.
  • Schenk H, Klein M, Erdbrugger W, Droge W, Schulze-Osthoff K. Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappaB and AP-1. Proc Nall Acad Sci USA 1994; 91: 1672–1676.
  • Wild AC, Mulcahy RT. Pyrrolidine dithiocarbamate up-regulates the expression of genes encoding the catalytic and regulatory subunits of y-glutamylcysteine synthetase and increases intracellular glutathione levels. Biochem J 1999; 338: 659–665.
  • Ip C. Comparative effects of antioxidants on enzymes involved in glutathione metabolism. Life Sci 1984; 34: 2501–2506.
  • Borroz KI, Buetler TM, Eaton DL. Modulation of gamma-glutamyl-cysteine synthetase large subunit mRNA expression by butylated hydroxyanisole. Toxicol Appl Pharmacol 1994; 141: 150–155.
  • Maclean KN, Janosik M, Kraus E et al. Cystathionine beta-synthase is co-ordinately regulated with proliferation through a redox-sensitive mechanism in cultured human cells and Saccharomyces cerevisiae. J Cell Physiol 2002; 192: 81–92.

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