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, Volume 12, Issue 4, pp 530–535 | Cite as

Concerning the possibility of redox drugs

  • J. Chayen
Immunosuppression and Inflammation Editorial

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References

  1. [1]
    L.F. Hewitt,Oxidation-Reduction Potentials in Bacteriology and Biochemistry, 6th edn. Livingstone, Edinburgh 1950.Google Scholar
  2. [2]
    W.M. Clark,Oxidation-Reduction Potentials of Organic Systems, Williams and Wilkins, Baltimore, Maryland 1960.Google Scholar
  3. [3]
    K. Burton, Free energy data of biological interest. InEnergy Transformation in Living Matter, pp. 275–285. (EdsH.A. Krebs andH.L. Kornberg), Springer Berlin 1957.Google Scholar
  4. [4]
    H.A. Krebs andH.L. Kornberg (Eds),Energy Transformations in Living Matter, Springer, Berlin 1957.Google Scholar
  5. [5]
    L.L. Madison, A. Lochner andJ. Wulff,Ethanol-induced hypoglycaemia. II. Mechanism of suppression of hepatic gluconeogenesis, Diabetes16, 252–258 (1967).PubMedGoogle Scholar
  6. [6]
    L.L. Madison,Ethanol-induced hypoglycaemia, Adv. Metab. Disorders3, 85–109 (1968).Google Scholar
  7. [7]
    H.A. Krebs andL.V. Eggleston,The regulation of the pentose phosphate cycle in rat liver, Adv. Enzyme Regul.12, 421–434 (1974).CrossRefPubMedGoogle Scholar
  8. [8]
    J. Chayen, F.P. Altman andR.G. Butcher, The effect of certain drugs on the production and possible utilization of reducing equivalents outside the mitochondria. InFundamentals of Cell Pharmacology, pp. 196–230. (Ed.S. Dikstein). Chas. C. Thomas, Springfield, Illinois 1973.Google Scholar
  9. [9]
    J. Chayen, L. Bitensky, R.G. Butcher andF.P. Altman,Cellular biochemical assessment of steroid activity, Advs. Steroid Biochem. Pharmacol.4, 1–60 (1974).Google Scholar
  10. [10]
    L.V. Eggleston andH.A. Krebs,Regulation of the pentose phosphate cycle, Biochem. J.138, 425–435 (1974).PubMedGoogle Scholar
  11. [11]
    L.A. Coulton,Temporal relationship between glucose 6-phosphate dehydrogenase activity and DNA-synthesis, Histochemistry50, 207–215 (1977).CrossRefPubMedGoogle Scholar
  12. [12]
    J.R. Gillette, A.R. Conney, G.J. Cosmides, R.W. Estabrook, J.R. Fouts andG.J. Mannering (Eds),Microsomes and Drug Oxidations. Academic Press, New York 1969.Google Scholar
  13. [13]
    K. Takeshige andS. Minakami,NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J.180, 129–135 (1979).PubMedGoogle Scholar
  14. [14]
    M.U. Dianzani andG. Ugazio, Lipid peroxidation. InBiochemical Mechanisms of Liver Injury, pp. 669–707. (Ed.T.F. Slater). Academic Press, London 1978.Google Scholar
  15. [15]
    T.F. Slater, Mechanisms of protection. InBiochemical Mechanisms of Liver Injury, pp. 744–801. (Ed.T.F. Slater). Academic Press, London 1978.Google Scholar
  16. [16]
    R. Shedden, J. Dunham, L. Bitensky, A. Catterall andJ. Chayen,Changes in alkaline phosphatase activity in periosteal cells in healing fractures, Calcif. Tiss. Res.22, 19–25 (1976).Google Scholar
  17. [17]
    R.E. Pinto andW. Bartley,The nature of the sex-linked differences in glutathione peroxidase activity and aerobic oxidation of glutathione in male and female rat liver, Biochem. J.115, 449–456 (1969).PubMedGoogle Scholar
  18. [18]
    E.E. Bittar,Cell pH. Butterworths, London (1964).Google Scholar
  19. [19]
    W.E. Hornby, M.D. Lilly andE.M. Crook,The preparation and properties of ficin chemically attached to carboxymethylcellulose, Biochem. J.98, 420–425 (1966).PubMedGoogle Scholar
  20. [20]
    W.E. Hornby, M.D. Lilly andE.M. Crook,Some changes in the reactivity of enzymes resulting from their chemical attachment to water-insoluble derivatives of cellulose, Biochem. J.107, 669–674 (1968).Google Scholar
  21. [21]
    A.D. McLaren andL. Packer,Some aspects of enzyme reactions in heterogeneous systems, Advs. Enzymol33, 245–308 (1970).Google Scholar
  22. [22]
    J.T. Davies andE.K. Rideal, InInterfacial Phenomena, p. 91. Academic Press, New York 1961.Google Scholar
  23. [23]
    R.T. Dean andA.J. Barrett,Lysosomes, Essays in Biochemistry12, 1–40 (1976).PubMedGoogle Scholar
  24. [24]
    A. Bonsignore andA. de Flora,Regulatory properties of glucose-6-phosphate dehydrogenase, Curr. Top. Cell Regul.6, 21–52 (1972).Google Scholar
  25. [25]
    H.A. Krebs,The redox state of nicotinamide adenine dinucleotide in the cytoplasm and mitochondria of rat liver, Adv. Enzyme Regul.5, 409–434 (1967).CrossRefPubMedGoogle Scholar
  26. [26]
    R.L. Veech, L.V. Eggleston andH.A. Krebs,The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver, Biochem. J.115, 609–619 (1969).PubMedGoogle Scholar
  27. [27]
    R.L. Veech, Regulation of co-enzyme potential by near equilibrium reactions. InMicroenvironments and Metabolic Compartmentation, pp. 17–64. (EdsP.A. Srere andR.W. Estabrook). Academic Press, New York 1978.Google Scholar
  28. [28]
    C.H. Barnett, D.V. Davies andM.M. MacConaill,Synovial Joints: Their Structure and Mechanics, p. 36. Longmans, London 1961.Google Scholar
  29. [29]
    N.A. Cummings andG.L. Nordby,Measurement of synovial fluid pH in normal and arthritic knees, Arth. and Rheum.9, 47–56 (1966).Google Scholar
  30. [30]
    L.W. Poulter, L. Bitensky, B. Cashman andJ. Chayen,The maintenance of human synovial tissue in vitro, Virchows Arch. Abt. B Zellpath4, 303–309 (1970).Google Scholar
  31. [31]
    J.-P. Famaey andM.W. Whitehouse,Interaction between nonsteroidal anti-inflammatory drugs and biological membranes. IV. Effects of nonsteroidal anti-inflammatory drugs and various ions on the availability of sulfhydryl groups on lymphoid cells and mitochondrial membranes, Biochem. Pharmacol.24, 1609–1615 (1975).CrossRefPubMedGoogle Scholar
  32. [32]
    G. Weissmann,Lysosomes and joint disease, Arth. and Rheum.9, 834–840 (1966).Google Scholar
  33. [33]
    G. Weissmann,The role of lysosomes in inflammation and disease, Ann. Rev. Med.18, 97–108 (1967).CrossRefPubMedGoogle Scholar
  34. [34]
    R.G. Butcher, L. Bitensky, B. Cashman andJ. Chayen,Differences in the redox balance in human rheumatoid and non-rheumatoid synovial lining cells, Beitr. Path.148, 265–274 (1973).Google Scholar
  35. [35]
    J. Chayen, L. Bitensky, R.G. Butcher andB. Cashman,The effect of experimentally induced redox changes on human rheumatoid and non-rheumatoid synovial tissue in vitro, Beitr. Path.149, 127–144 (1973).Google Scholar
  36. [36]
    J. Chayen, L. Bitensky, R.G. Butcher andL.W. Poulter,Redox control of lysosomes in human synovia, Nature222, 281–282 (1969).PubMedGoogle Scholar
  37. [37]
    U. Israelsson, M. Hamberg andB. Samuelsson,Biosynthesis of 19-hydroxy-prostaglandin A 1, Eur. J. Biochem.11, 390–394 (1969).CrossRefPubMedGoogle Scholar
  38. [38]
    E.D. Wills,Effects of vitamin K and naphthoquinones on lipid peroxide formation and oxidative demethylation by liver microsomes, Biochem. Pharmacol.21, 1879–1883 (1972).CrossRefPubMedGoogle Scholar
  39. [39]
    I.C. Calder, P.J. Williams, R.A. Woods, C.C. Funder, C.R. Green, K.N. Ham andJ.D. Tange,Nephrotoxicity and molecular structure, Xenobiotica5, 303–307 (1975).PubMedGoogle Scholar
  40. [40]
    A. Sellars, E. Cartwright, G. Murphy andJ.J. Reynolds,Evidence that latent collagenases are enzyme-inhibitor complexes, Biochem. J.163, 303–307 (1977).PubMedGoogle Scholar

Copyright information

© Birkhäuser Verlag 1982

Authors and Affiliations

  • J. Chayen
    • 1
  1. 1.Division of Cellular BiologyThe Mathilda and Terence Kennedy Institute of RheumatologyLondonUK

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