Journal Mobile Options
Table of Contents
Vol. 10, No. 3-4, 2001
Issue release date: May–August 2001
Biol Signals Recept 2001;10:189–199
(DOI:10.1159/000046887)

Mitochondrial Catalase and Oxidative Injury

Bai J. · Cederbaum A.I.
To view the fulltext, log in and/or choose pay-per-view option

Individual Users: Register with Karger Login Information

Please create your User ID & Password





Contact Information











I have read the Karger Terms and Conditions and agree.

To view the fulltext, please log in

To view the pdf, please log in

Abstract

Mitochondria dysfunction induced by reactive oxygen species (ROS) is related to many human diseases and aging. In physiological conditions, the mitochondrial respiratory chain is the major source of ROS. ROS could be reduced by intracellular antioxidant enzymes including superoxide dismutase, glutathione peroxidase and catalase as well as some antioxidant molecules like glutathione and vitamin E. However, in pathological conditions, these antioxidants are often unable to deal with the large amount of ROS produced. This inefficiency of antioxidants is even more serious in mitochondria, because mitochondria in most cells lack catalase. Therefore, the excessive production of hydrogen peroxide in mitochondria will damage lipid, proteins and mDNA, which can then cause cells to die of necrosis or apoptosis. In order to study the important role of mitochondrial catalase in protecting cells from oxidative injury, a HepG2 cell line overexpressing catalase in mitochondria was developed by stable transfection of a plasmid containing catalase cDNA linked with a mitochondria leader sequence which would encode a signal peptide to lead catalase into the mitochondria. Mitochondria catalase was shown to protect cells from oxidative injury induced by hydrogen peroxide and antimycin A. However, it increased the sensitivity of cells to tumor necrosis factor-α-induced apoptosis by changing the redox-oxidative status in the mitochondria. Therefore, the antioxidative effectiveness of catalase when expressed in the mitochondrial compartment is dependent upon the oxidant and the locus of ROS production.



Copyright / Drug Dosage

Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher or, in the case of photocopying, direct payment of a specified fee to the Copyright Clearance Center.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in goverment regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

References

  1. Chance B, Sies H, Boveris A: Hydroperoxide metabolism in mammalian organs. Physiol Rev 1979;59:527–605.
  2. Taylor DE, Ghio AJ, Piantadosi CA: Reactive oxygen species produced by liver mitochondria of rats in sepsis. Arch Biochem Biophys 1995;316:70–76.
  3. Boveris A, Chance B: The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen. Biochem J 1973;134:707–716.
  4. Turrens JF: Superoxide production by the mitochondrial respiratory chain. Biosci Rep 1997;17:3–8.
  5. Zamzami N, Susin SA, Marchetti P, Hirsch T, Gomez-Monterrey I, Castedo M, Kroemer G: Mitochondrial control of nuclear apoptosis. J Exp Med 1996;183:1533–1544.
  6. Fridovich I: Superoxide anion radical (O2–.), superoxide dismutases, and related matters. J Biol Chem 1997;272:18515–18517.
  7. Emerit J, Michelson AM: Free radicals in medicine and biology. Sem Hop 1982;58:2670–2675.
  8. Yildiz G, Demiryurek AT: Ferrous iron-induced luminol chemiluminescence: A method for hydroxyl radical study. J Pharmacol Toxicol Methods 1998;39:179–184.

    External Resources

  9. Wardman P, Candeias LP: Fenton chemistry: An introduction. Radiat Res 1996;145:523–531.
  10. Tappel AL: Lipid peroxidation damage to cell components. Fed Proc 1973;32:1870–1874.
  11. Kowaltowski AJ, Vercesi AE: Mitochondrial damage induced by conditions of oxidative stress. Free Radic Biol Med 1999;26:463–471.

    External Resources

  12. Tatsumi T, Kako KJ: Effects of hydrogen peroxide on mitochondrial enzyme function studied in situ in rat heart myocytes. Basic Res Cardiol 1993;88:199–211.
  13. Yang JC, Cortopassi GA: Induction of the mitochondrial permeability transition causes release of the apoptogenic factor cytochrome c. Free Radic Biol Med 1998;24:624–631.

    External Resources

  14. Anup R, Madesh M, Balasubramanian KA: Enterocyte mitochondrial dysfunction due to oxidative stress. Indian J Biochem Biophys 1999;36:266–271.

    External Resources

  15. Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES: Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol Cell 1998;1:949–957.
  16. Hu Y, Benedict MA, Ding L, Nunez G: Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J 1999;18:3586–3595.
  17. Zhang Y, Marcillat O, Giulivi C, Ernster L, Davies KJ: The oxidative inactivation of mitochondrial electron transport chain components and ATPase. J Biol Chem 1990;265:16330–16336.
  18. Yuan G, Kaneko M, Masuda H, Hon RB, Kobayashi A, Yamazaki N: Decrease in heart mitochondrial creatine kinase activity due to oxygen free radicals. Biochim Biophys Acta 1992;1140:78–84.
  19. Brawn K, Fridovich I: DNA strand scission by enzymically generated oxygen radicals. Arch Biochem Biophys 1981;206:414–419.
  20. Ehlers RA, Hernandez A, Bloemendal LS, Ethridge RT, Farrow B, Evers BM: Mitochondrial DNA damage and altered membrane potential (delta psi) in pancreatic acinar cells induced by reactive oxygen species. Surgery 1999;126:148–155.
  21. Esposito LA, Melov S, Panov A, Cottrell BA, Wallace DC: Mitochondrial disease in mouse results in increased oxidative stress. Proc Natl Acad Sci USA 1999;96:4820–4825.
  22. Wei YH: Oxidative stress and mitochondrial DNA mutations in human aging. Proc Soc Exp Biol Med 1998;217:53–63.

    External Resources

  23. Radi R, Turrens JF, Chang LY, Bush KM, Crapo JD, Freeman BA: Detection of catalase in rat heart mitochondria. J Biol Chem 1991;266:22028–22034.
  24. O’Donovan DJ, Katkin JP, Tamura T, Husser R, Xu X, Smith CV, Welty SE: Gene transfer of mitochondrially targeted glutathione reductase protects H441 cells from t-butyl hydroperoxide-induced oxidant stresses. Am J Respir Cell Mol Biol 1999;20: 256–263.
  25. Arai M, Imai H, Koumura T, Yoshida M, Emoto K, Umeda M, Chiba N, Nakagawa Y: Mitochondrial phospholipid hydroperoxide glutathione peroxidase plays a major role in preventing oxidative injury to cells. J Biol Chem 1999;274:4924–4933.
  26. Nomura K, Imai H, Koumura T, Arai M, Nakagawa Y: Mitochondrial phospholipid hydroperoxide glutathione peroxidase suppresses apoptosis mediated by a mitochondrial death pathway. J Biol Chem 1999;274:29294–29302.
  27. Esposito LA, Kokoszka JE, Waymire KG, Cottrell B, MacGregor GR, Wallace DC: Mitochondrial oxidative stress in mice lacking the glutathione peroxidase-1 gene. Free Radic Biol Med 2000;28:754–766.
  28. Nohl H, Hegner D: Evidence for the existence of catalase in the matrix space of rat-heart mitochondria. FEBS Lett 1978;89:126–130.
  29. Nohl H, Jordan W: The metabolic fate of mitochondrial hydrogen peroxide. Eur J Biochem 1980;111:203–210.

    External Resources

  30. Nohl H, Hegner D: Do mitochondria produce oxygen radicals in vivo? Eur J Biochem 1978;82:563–567.
  31. Radi R, Bush KM, Freeman BA: The role of cytochrome c and mitochondrial catalase in hydroperoxide-induced heart mitochondrial lipid peroxidation. Arch Biochem Biophys 1993;300:409–415.
  32. Radi R, Sims S, Cassina A, Turrens JF: Roles of catalase and cytochrome c in hydroperoxide-dependent lipid peroxidation and chemiluminescence in rat heart and kidney mitochondria. Free Radic Biol Med 1993;15:653–659.

    External Resources

  33. Dev IK, Ray PH: Signal peptidases and signal peptide hydrolases. J Bioenerg Biomembr 1990;22:271–290.

    External Resources

  34. Roise D, Theiler F, Horvath SJ, Tomich JM, Richards JH, Allison DS, Schatz G: Amphiphilicity is essential for mitochondrial presequence function. EMBO J 1988;7: 649–653.
  35. Lemire BD, Fankhauser C, Baker A, Schatz G: The mitochondrial targeting function of randomly generated peptide sequences correlates with predicted helical amphiphilicity. J Biol Chem 1989;264:20206–20215.

    External Resources

  36. Bai J, Rodriguez AM, Melendez JA, Cederbaum AI: Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury. J Biol Chem 1999;274:26217–26224.
  37. Matsura T, Kai M, Fujii Y, Ito H, Yamada K: Hydrogen peroxide-induced apoptosis in HL-60 cells requires caspase-3 activation. Free Radic Res 1999;30:73–83.
  38. Teramoto S, Tomita T, Matsui H, Ohga E, Matsuse T, Ouchi Y: Hydrogen peroxide-induced apoptosis and necrosis in human lung fibroblasts: Protective roles of glutathione. Jpn J Pharmacol 1999;79:33–40.
  39. Lemasters JJ, Qian T, Elmore SP, Trost LC, Nishimura Y, Herman B, Bradham CA, Brenner DA, Nieminen AL: Confocal microscopy of the mitochondrial permeability transition in necrotic cell killing, apoptosis and autophagy. Biofactors 1998;8:283–285.

    External Resources

  40. Gores GJ, Miyoshi H, Botla R, Aguilar HI, Bronk SF: Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: A potential role for mitochondrial proteases. Biochim Biophys Acta 1998;1366:167–175.
  41. Melendez JA, Davies KJA: Manganese superoxide dismutase modulates interleukin-1alpha levels in HT-1080 fibrosarcoma cells. J Biol Chem 1996;271:18898–18903.
  42. Castilho RF, Kowaltowski AJ, Vercesi AE: 3,5,3′-Triiodothyronine induces mitochondrial permeability transition mediated by reactive oxygen species and membrane protein thiol oxidation. Arch Biochem Biophys 1998;354:151–157.

    External Resources

  43. Lehninger AL, Vercesi A, Bababunmi EA: Regulation of Ca2+ release from mitochondria by the oxidation-reduction state of pyridine nucleotides. Proc Natl Acad Sci USA 1978;75:1690–1694.
  44. Kowaltowski AJ, Castilho RF, Vercesi AE: Opening of the mitochondrial permeability transition pore by uncoupling or inorganic phosphate in the presence of Ca2+ is dependent on mitochondrial-generated reactive oxygen species. FEBS Lett 1996;378:150–152.

    External Resources

  45. Tan S, Sagara Y, Liu Y, Maher P, Schubert D: The regulation of reactive oxygen species production during programmed cell death. J Cell Biol 1998;141:1423–1432.
  46. Garcia-Ruiz C, Colell A, Mari M, Morales A, Fernandez-Checa JC: Direct effect of ceramide on the mitochondrial electron transport chain leads to generation of reactive oxygen species. Role of mitochondrial glutathione. J Biol Chem 1997;272:11369–11377.
  47. Hildeman DA, Mitchell T, Teague TK, Henson P, Day BJ, Kappler J, Marrack PC: Reactive oxygen species regulate activation-induced T cell apoptosis. Immunity 1999;10:735–744.
  48. Sidoti-de Fraisse C, Rincheval V, Risler Y, Mignotte B, Vayssiere JL: TNF-alpha activates at least two apoptotic signaling cascades. Oncogene 1998;17:1639–1651.

    External Resources

  49. Hagar H, Ueda N, Shah SV: Role of reactive oxygen metabolites in DNA damage and cell death in chemical hypoxic injury to LLC-PK1 cells. Am J Physiol 1996;271:F209–F215.

    External Resources

  50. Chen YC, Lin-Shiau SY, Lin JK: Involvement of reactive oxygen species and caspase 3 activation in arsenite-induced apoptosis. J Cell Physiol 1998;177:324–333.
  51. Bai J, Cederbaum AI: Overexpression of catalase in mitochondrial or cytosolic compartment increases sensitivity of HepG2 cells to TNF-alpha induced apoptosis. J Biol Chem 2000;275:19241–19249.
  52. Leist M, Single B, Castoldi AF, Kuhnle S, Nicotera P: Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis. J Exp Med 1997;185:1481–1486.
  53. Eguchi Y, Shimizu S, Tsujimoto Y: Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res 1997;57:1835–1840.
  54. Nicotera P, Leist M, Ferrando-May E: Intracellular ATP, a switch in the decision between apoptosis and necrosis. Toxicol Lett 1998;102–103:139–142.
  55. Sanchez-Alcazar JA, Ruiz-Cabello J, Hernandez-Munoz I, Pobre PS, de la Torre P, Siles-Rivas E, Garcia I, Kaplan O, Munoz-Yague MT, Solis-Herruzo JA: Tumor necrosis factor-alpha increases ATP content in metabolically inhibited L929 cells preceding cell death. J Biol Chem 1997;272:30167–30177.
  56. Wong GH, Elwell JH, Oberley LW, Goeddel DV: Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell 1989;58:923–931.


Pay-per-View Options
Direct payment This item at the regular price: USD 38.00
Payment from account With a Karger Pay-per-View account (down payment USD 150) you profit from a special rate for this and other single items.
This item at the discounted price: USD 26.50