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2004 | z. 3 | 20-28
Tytuł artykułu

Rola wolnych rodników w organizmie

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Rocznik
Tom
Strony
20-28
Opis fizyczny
Bibliogr. 62 poz., rys.
Twórcy
  • Instytut Chemii i Techniki Jądrowej, Warszawa
Bibliografia
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  • 2. McCord, J. M. and Fridovich, I.: Superoxide Dismutase. An enzymie function for erythrocuprein (hemocupreln). J. Biol. Chem. 244: 6049-6055, 1969.
  • 3. Kruszewski, M.: Free radicals, DNA damage and cardkwascular diseases. Ann. Diagn. Paed. Pathol. 7: 25-33, 2003.
  • 4. George, V. B.: Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (HO/O-) in aqueous solution. J. Phys. Chem. Ref. Data 17: 513-886, 1988.
  • 5. Asada, K.: In: Molecular biology of free radical scavenging systems. Ed. J. G. Scandalios. Plainview, N. Y.: Cold Spring Harbor Laboratory Press, 1992.
  • 6. Halliwell, B. and Gutteridge, J. M.: Free Radicals in Biology & Medicine. Clarendon Press, Oxford, 1989.
  • 7. Bors, W., Saran, M., Lengfelder, E., Michel, C , Fuchs, C, and Frenzel, C : Detection of oxygen radicals in biological reactions. Photochem. Photobiol. 28: 629-638,1978.
  • 8. Dix, T. A. and Aikens, J.: Mechanisms and biological relevance of lipid peroxidation initiation. Chem. Res. Toxicol. 6: 2-18,1993.
  • 9. Halliwell, B. and GrooWeld, M.: The measurement of free radical reactions in humans: Some thoughts for future experimentation. FEBS Letters 213: 9-14, 1987.
  • 10. Esterbauer, H. and Zollner, H.: Methods for determination of aldehydic lipid peroxidation produets. Free Rad/c. Biol. Med. 7:197-203,1989.
  • 11. Siems, W„ Kowalewski, J., David, H., Grune, T., and Bimmler, M.: Discrepancy between biochemical normalization and morphological recovery of jejunal mucosa during postischemic reperfusion in presence of the xanthine oxidase inhibitor oxypurinol. Celi Mol. Biol. 37: 213-226,1991.
  • 12. Halliwell, B. and Aruoma, O. I.: In: Molecular Biology of Free Radical Scavenging Systems. Ed. J. G. Scandalios. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1992, pp. 47-67.
  • 13. Chiu, D., Kuypers, F., and Lubin, B.: Lipid peroxidation in human red cells. Semin. Hematol. 26: 257-276, 1989.
  • 14. Ueda, K., Kobayashi, S., Morita, J., and Komano, T.: Site-specific DNA damage caused by lipid peroxidation produets. Biochim. Biophys. Acta 19; 824: 341-348, 1985.
  • 15. Benamira, M. and Marnett, L. J.: The lipid peroxidation product 4-hydroxynonenal is a potent inducer of the SOS response. Mutat. Res. 293:1-10, 1992.
  • 16. Yonei, S. and Furui, H.: Lethal and mutagenic effects of malondialdehyde, a decomposition product of peroxidized lipids, on Escherichia coli with different DNA-repair capacities. Mutat. Res. 88: 23-32, 1981.
  • 17. Jain, S. K.: In vivo externalization of phosphatidylserine and phosphatidylethanolamine in the membrane bilayer and hypercoagulability by the lipid peroxidation of erythrocytes in rats. J. Clin. Invest 76: 281-286,1985.
  • 18. Jain, S. K.: The accumulation of malonyldialdehyde, a product of fatty acid peroxidation, can disturb aminophospholipid organization in the membrane bilayer of human erythrocytes. J. Biol. Chem. 259: 3391-3394, 1984.
  • 19. Filipek, J., Gelienova, K., Kovacs, P., and Balgavy, P.: Effect of lipid autoperoxidation on the activity of the sarcoplasmic reticulum (Ca2+-Mg2+) ATPase reconstituted into egg yolk phosphatidylcholine bilayers. Gen. Physiol Biophys. 12: 55-68, 1993.
  • 20. Halliwell. B. and Gutteridge. J. M.: Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol. 186:1-85.: 1-85, 1990.
  • 21. Puchala, M. and Schuessler. H.: Oxygen effect in the radiolysis of proteins. III. Haemoglobin. Int. J. Radiat. Biol. 64: 149-156, 1993.
  • 22. Klotz, L. O., Schroeder, R, and Sies, H.: Peroxynitrite signaling: receptor tyrosine kinases and activation of stress-responsive pathways. Free Radic. Biol. Med. 33: 737-743, 2002.
  • 23. Radi, R., Cassina, A., Hodara, R., Ouijano, C , and Castro, L: Peroxynitrite reactions and formation in mitochondria. Free Radic. Biol. Med. 33: 1451-1464, 2002.
  • 24. Gebicki, S. and Gebicki, J. M.: Formation of peroxides in amino acids and proteins exposed to oxygen free radicals. Biochem. J. 289: 743-749, 1993.
  • 25. Stadtman, E. R.: Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic. Biol. Med. 9: 315-325,1990.
  • 26. Stadtman, E. R.: Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62: 797-821.: 797-821, 1993.
  • 27. Simpson, J. A., Gieseg, S. P, and Dean, R. T.: Free radical and enzymatic mechanisms for the generation of protein bound reducing moieties. Biochim. Biophys. Acta 1156: 190-196, 1993.
  • 28. Pouget, J. P„ Douki, T, Richard, M. J., and Cadet, J.: DNA damage induced in cells by gamma and UVA radiation as measured by HPLC/GC-MS and HPLC-EC and Comet assay. Chem. Res. Toxicol. 13: 541-549, 2000.
  • 29. Le, X. C , Xing, J. Z., Lee, J., Leadon, S. A., and Weinfeld, M.: Inducible repair of thymine glycol detected by an ultrasensitive assay for DNA damage. Science 280: 1066-1069, 1998.
  • 30. Lipinski, R, Drapier, J. C , Oliveira, L., Retmanska, H., Sochanowicz, B., and Kruszewski, M.: Intracellular iron status as a hallmark of mammalian celi susceptibility to oxidative stress: a study of L5178Y mouse lymphoma celi lines differentially sensitive to H (2) O (2). Blood 95: 2960-2966, 2000.
  • 31. Moncada S., Palmer R. M., and Higgs E. A.: Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol. Rev. 43: 109-142, 1991.
  • 32. Curnutte, J. T. and Babior, B. M.: Chronic granulomatous disease. Adv. Rum. Genet. 16: 229-97.: 229-297, 1987.
  • 33. Klebanoff, S. J.: In: Inflammation: Basic Principles and Clinical Correlates. Eds. J. I. Gallin, R. Snyderman, and B. F. Haynes. Lippincott Williams & Wilkins Publishers, 1992, pp. 541-588.
  • 34. Meier, B., Cross, A. R., Hancock, J. T., Kaup, F. J., and Jones, O. T.: Identification of a superoxide-generating NADPH oxidase system in human fibroblasts. Biochem. J. 275: 241-245, 1991.
  • 35. Matsubara, T. and Ziff, M.: Increased superoxide anion release from human endothelial cells in response to cytokines. J. Immunol. 137: 3295-3298, 1986.
  • 36. Kyriazis, M.: Neuroprotective, anti-apoptotic effects of apomorphine. J. Anti. Aging Med. 6: 21-28, 2003.
  • 37. Beal, M. F: Mitochondria, oxidative damage, and inflammation in Parkinson's disease. Ann. N. Y. Acad. Sci. 991:120-31.: 120-131, 2003.
  • 38. Thun, M. J., Henley, S. J., and Gansler, T.: Inflammation and cancer: an epidemiological perspective. Novartis. Found. Symp. 256: 6-21; discussion 22-8,49-52, 266-9.: 6-21, 2004.
  • 39. Bartosz, G.: Druga twarz tlenu. Wolne rodniki w przyrodzie. Wydawnictwo Naukowe PWN, 1995.
  • 40. Ames, B. N , Shigenaga, M. K., and Hagen, T. M.: Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. U. S. A. 90: 7915-7922, 1993.
  • 41. Galhenage, S. P, Viiala, C. H., and Olynyk, J. K.: Screening for hemochromatosis: patients with liver disease, families, and populations. Curr. Gastroenterol. Rep. 6: 44-51. 2004.
  • 42. Ayoub, W., Martin, P, and Tran, T: Hereditary hemochromatosis. MedGenMed. 5: 11, 2003.
  • 43. Pawliczak, R.: [The role of radical oxygen species in airway inflammation]. Pol. Merkuriusz. Lek. 14: 493-496, 2003.
  • 44. Davidson, J. K. and MacPherson, P.: Pulmonary changes in paraquat poisoning. Clin. Radio/. 23: 18-25, 1972.
  • 45. Rilke, F. and Pilotti, S.: [Pulmonary histopathological changes in subjects with malignant tumors treated with bleomycin]. Tumori 57: 287-296, 1971.
  • 46. Britton, R. S. and Bacon, B. R.: Role of free radicals in liver diseases and hepatic fibrosis. Hepatogastroenterology'41: 343-348, 1994.
  • 47. Cuthbert, J. A.: Wilson's disease. Update of a systemie disorder with protean manifestations. Gastroenterol. Clin. North Am. 27: 655-vii, 1998.
  • 48. Gilbert, E. F: The effects of metabolic diseases on the cardiovascular system. Am. J. Cardiovasc. Pathol. 1: 189-213, 198.
  • 49. Kamp, D. W. and Weitzman, S. A.: The molecular basis of asbestos induced lung injury. Thorax 54: 638-652, 1999.
  • 50. Kamp, D. W., Graceffa, P., Pryor, W. A., and Weitzman, S. A.: The role of free radicals in asbestos-induced diseases. Free Radic. Biol. Med. 12: 293-315, 1992.
  • 51. Brown, R. K. and Kelly, F. J.: Role of free radicals in the pathogenesis of cystic fibrosis. Thorax49: 738-742, 1994.
  • 52. Ponka, R: Hereditary causes of disturbed iron homeostasis in the central nervous system. Ann. N. Y.Acad. Sci. 1012: 267-81.: 267-281, 2004.
  • 53. Shim, H. and Harris, Z. L.: Genetic defects in copper metabolism. J. Nutr. 133:1527S-1531S, 2003.
  • 54. Kawada, J.: [New hypotheses for the mechanisms of streptozotocin and alloxan inducing diabetes mellitus]. YakugakuZasshi 112: 773-791, 1992.
  • 55. RAKIETEN, N., RAKIETEN, M. L, and NADKARNI, M. R.: Studies on the diabetogenic action of streptozotocin (NSC-37917). Cancer Chemother. Rep. 29: 91-8.: 91-98, 1963.
  • 56. Piconi, L., Ouagliaro, L., and Ceriello, A.: Oxidative stress in diabetes. Clin. Chem. Lab Med. 41: 1144-1149, 2003.
  • 57. Hohenwallner, W., Wimmer, E., and Sommer, R.: [Determination of alpha-amylase by an enzymatic kinetic method on the ABA-100 (author's transl) ]. J. Clin. Chem. Clin. Biochem. 17: 349-352, 1979.
  • 58. Tachibana, M.: Sound needs sound melanocytes to be heard. Pigment Celi Res. 12: 344-354, 1999.
  • 59. COTZIAS, G. C , PAPAVASILIOU, P. S., VANWOERT, M. H., and Sakamoto, A.: MELANOGENESIS AND EXTRAPYRAMIDAL DISEASES. Fed. Proc. 23: 713-8.: 713-718, 1964.
  • 60. Van Nieuwpoort, F, Smit, N. R, Kolb, R., Van Der, M. H., Koerten, H., and Pavel, S.: Tyrosine-induced melanogenesis shows differences in morphologic and melanogenic preferences of melanosomes from light and dark skin types. J. Invest Dermatol. 122: 1251-1255, 2004.
  • 61. Vidotto, C , Fousert, D., Akkermann, M., Griesmacher, A., and Muller, M. M.: Purine and pyrimidine metabolites in children's urine. Clin. Chim. Acta335: 27-32, 2003.
  • 62. Hilliker, A. J., Duyf, B„ Evans, D., and Phillips, J. R: Urate-null rosy mutants of Drosophila melanogaster are hypersensitive to oxygen stress. Proc. Natl. Acad. Sci. U. S. A. 89:4343-4347, 1992.
Typ dokumentu
Bibliografia
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Identyfikator YADDA
bwmeta1.element.baztech-article-BPS1-0015-0051
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