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. 1975 Jan;11(1):8–13. doi: 10.1128/iai.11.1.8-13.1975

Liver glutathione and glutathione reductase response of endotoxin-treated mice.

P L Brown, C D Jeffires
PMCID: PMC415018  PMID: 234913

Abstract

The decrease in the level of liver glutathione (GSH) in endotoxin-treated mice was in part due to formation of glutathione disulfide (GSSG). An electron-generating system (EGS) had no effect when incubated with soluble liver extracts from normal controls but resulted in recovery of GSH amounting to 25% in endotoxin-treated animals. Incubation in the absence of the EGS caused a decline of 16% in the GSH in extracts from normal animals compared with a 50% decrease in endotoxin-treated animals. Exclusion of nicotinamide adenine dinucleotide phosphate (NADP) from the EGS resulted in a slight decline in the GSH of the extract from the normal controls but 25% for the endotoxin-treated animals. Reduction of exogenous GSSG by the liver extracts required that exogenous NADP be added to ghe incubation mixtures.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BARTLETT R. G., Jr, REGISTER U. D. Chlorpromazine and anesthetic agents on tissue non-protein sulfhydryl compounds in normothermic and hypothermic rats. Proc Soc Exp Biol Med. 1955 Nov;90(2):500–502. doi: 10.3181/00379727-90-22077. [DOI] [PubMed] [Google Scholar]
  2. BECK L. V., LINKENHEIMER W. Effects of shock and cold on mouse liver sulfhydryl. Proc Soc Exp Biol Med. 1952 Oct;81(1):291–294. doi: 10.3181/00379727-81-19853. [DOI] [PubMed] [Google Scholar]
  3. BERRY L. J., SMYTHE D. S. EFFECTS OF BACTERIAL ENDOTOXINS ON METABOLISM. VI. THE ROLE OF TRYPTOPHAN PYRROLASE IN RESPONSE OF MICE TO ENDOTOXIN. J Exp Med. 1963 Oct 1;118:587–603. doi: 10.1084/jem.118.4.587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. BEUTLER E., DURON O., KELLY B. M. Improved method for the determination of blood glutathione. J Lab Clin Med. 1963 May;61:882–888. [PubMed] [Google Scholar]
  5. BEUTLER E., YEH M. K. Erythrocyte glutathione reductase. Blood. 1963 May;21:573–585. [PubMed] [Google Scholar]
  6. BHATTACHARYA S. K., ROBSON J. S., STEWART C. P. The determination of glutathione in blood and tissues. Biochem J. 1955 Aug;60(4):696–702. doi: 10.1042/bj0600696. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Christophersen B. O. Oxidation of reduced glutathione by subcellular fractions of rat liver. Biochem J. 1966 Jul;100(1):95–101. doi: 10.1042/bj1000095. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. JEFFRIES C. D. LIVER NONPROTEIN SULFHYDRYL OF ENDOTOXIN-TREATED MICE. J Bacteriol. 1963 Dec;86:1358–1359. doi: 10.1128/jb.86.6.1358-1359.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. JOCELYN P. C. The importance of thiol compounds in the causation of disease. Clin Chim Acta. 1958 Sep;3(5):401–418. doi: 10.1016/0009-8981(58)90031-7. [DOI] [PubMed] [Google Scholar]
  10. Kosower N. S., Vanderhoff G. A., Kosower E. M. Glutathione. 8. The effects of glutathione disulfide on initiation of protein synthesis. Biochim Biophys Acta. 1972 Jul 31;272(4):623–637. [PubMed] [Google Scholar]
  11. MARTIN H., McILWAIN H. Glutathione, oxidized and reduced, in the brain and in isolated cerebral tissue. Biochem J. 1959 Feb;71(2):275–280. doi: 10.1042/bj0710275. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. MENNEAR J. H., BRADLEY C. A., MIYA T. S. A study of the chlorpromazine-induced decreased liver glutathione reaction. Proc Soc Exp Biol Med. 1963 Jan;112:199–202. doi: 10.3181/00379727-112-27991. [DOI] [PubMed] [Google Scholar]
  13. MILLS G. C. Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem. 1957 Nov;229(1):189–197. [PubMed] [Google Scholar]
  14. PINTO R. E. Comparison of the aerobic and anaerobic reduction of oxidized glutathione in liver homogenates. Biochem J. 1961 Apr;79:43–51. doi: 10.1042/bj0790043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Pinto R. E., Bartley W. A negative correlation between oxygen uptake and glutathione oxidation in rat liver homogenates. Biochem J. 1969 Aug;114(1):5–9. doi: 10.1042/bj1140005. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pinto R. E., Bartley W. The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates. Biochem J. 1969 Mar;112(1):109–115. doi: 10.1042/bj1120109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. RALL T. W., LEHNINGER A. L. Glutathione reductase of animal tissues. J Biol Chem. 1952 Jan;194(1):119–130. [PubMed] [Google Scholar]
  18. REGISTER U. D., BARTLETT R. G., Jr Relationship of adrenalin to tissue sulfhydryl compounds. Science. 1954 Jul 16;120(3107):109–110. doi: 10.1126/science.120.3107.109. [DOI] [PubMed] [Google Scholar]
  19. Rieber E. E., Kosower N. S., Jaffé E. R. Reduced nicotinamide adenine dinucleotide and the reduction of oxidized glutathione in human erythrocytes. J Clin Invest. 1968 Jan;47(1):66–71. doi: 10.1172/JCI105715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Szymanski D. C., Jeffries C. D. The effect of glutathione on survival of endotoxin treated mice. Proc Soc Exp Biol Med. 1968 Dec;129(3):966–968. doi: 10.3181/00379727-129-33470. [DOI] [PubMed] [Google Scholar]
  21. ZATMAN L. J., KAPLAN N. O., COLOWICK S. P., CIOTTI M. M. Effect of isonicotinic acid hydrazide on diphosphopyridine nucleotidases. J Biol Chem. 1954 Aug;209(2):453–466. [PubMed] [Google Scholar]

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