TGF-β1 triggers oxidative modifications and enhances apoptosis in hit cells through accumulation of reactive oxygen species by suppression of catalase and glutathione peroxidase

Free Radical Biology and Medicine

Volumn 22, Issue 6, 1997, Pages 1007-1017

  Islam, Kazi N ^a   Kayanoki, Yoshiro ^a   Kaneto, Hideaki ^a   Suzuki, Keiichiro ^a   Asahi, Michio ^a   Fujii, Junichi ^a   Taniguchi, Naoyuki ^a  

^a OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

Author keywords

Apoptosis; Carbonyl groups; Catalase; Glutathione peroxidase; HIT cell; Lipid peroxidation; Reactive oxygen species; Transforming growth factor 1

Indexed keywords

ANTIOXIDANT; CARBONYL DERIVATIVE; CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; MALONALDEHYDE; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; TRANSFORMING GROWTH FACTOR BETA1; DNA; HYDROGEN PEROXIDE; PEROXIDE; TRANSFORMING GROWTH FACTOR BETA;

ANIMAL CELL; APOPTOSIS; ARTICLE; CELL STRAIN; CONTROLLED STUDY; DNA CLEAVAGE; ENZYME REPRESSION; ETIOLOGY; HAMSTER; LIPID PEROXIDATION; NONHUMAN; OXIDATION; PANCREAS ISLET BETA CELL; PANCREATITIS; PRIORITY JOURNAL; ANIMAL; CELL CULTURE; DRUG ANTAGONISM; FLOW CYTOMETRY; GENE EXPRESSION; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PANCREAS ISLET CELL TUMOR; PANCREAS TUMOR; PATHOLOGY;

ADENOMA, ISLET CELL; ANIMALS; APOPTOSIS; CATALASE; CRICETINAE; DNA; FLOW CYTOMETRY; GENE EXPRESSION; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE; OXIDATION-REDUCTION; PANCREATIC NEOPLASMS; PEROXIDES; REACTIVE OXYGEN SPECIES; RNA, MESSENGER; TRANSFORMING GROWTH FACTOR BETA; TUMOR CELLS, CULTURED;

EID: 0030614518     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00493-5     Document Type: Article

References (50)

1. Heine U. I., Munoz E. F., Flanders K. C., Ellingsworth L. R., Lam H-Y. P., Thompson N. L., Roberts A. B., Sporn M. B. Role of transforming growth factor- β in the development of the mouse embryo. J. Cell Biol. 105:1987;2861-2876.
2. Raghow R., Postlethwait A. E., Keshi-oja J., Moses H. L., Kang A. H. Transforming growth factor- β increases steady state levels of type 1 procollagen and fibronectin messenger RNAs posttranscriptionally in cultured human dermal fibroblasts. J. Clin. Invest. 79:1987;1285-1288.
3. Kehrl J. H., Wakefield L. M., Roberts A. B., Jakowlew S., Alverz-Mon M., Derynck R., Sporn M. B., Fauci A. S. Production of transforming growth factor β by human T lymphocytes and its potential role in the regulation of cell growth. J. Exp. Med. 163:1986;1037-1050.
4. Shipley G. D., Pittelkow M. R., Wille J. J. Jr., Scott R. E., Moses H. L. Reversible inhibition of normal human prokeratinocyte proliferation by type β transforming growth factor-growth inhibition in serum-free medium. Cancer Res. 46:1986;2068-2071.
5. Masui T., Wakefield L. M., Lechner J. F., La Veck M. A., Sporn M. B., Harris C. C. Type β transforming growth factor is the primary differentiation-inducing serum factor for normal human bronchial epithelial cells. Proc. Natl. Acad. Sci. USA. 83:1986;2438-2442.
6. Carr B. I., Hayashi I., Branum E. L., Moses H. L. Inhibition of DNA synthesis in rat hepatocytes by platelet-derived type β transforming growth factor. Cancer Res. 46:1986;2330-2334.
7. Roberts A. B., Sporn M. B., Assoian R. K., Smith J. M., Roche N. S., Wakefield L. M., Heine U. I., Liotta L. A., Falanga V., Kehrl J. H., Fauci A. S. Transforming growth factor type β : Rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro. Proc. Natl. Acad. Sci. USA. 83:1986;4167-4171.
8. Farter-Shroder M., Muller G., Birchmeier W., Bohlen P. Transforming growth factor-beta inhibits endothelial cell proliferation. Biochem. Biophys. Res. Commun. 137:1986;295-302.
9. Braun L., Mead J. E., Panzica M., Mikumo R., Bell G. I., Fausto N. Transforming growth factor β mRNA increases during liver regeneration: A possible paracrine mechanism of growth regulation. Proc. Natl. Acad. Sci. USA. 85:1988;1539-1543.
10. Laethem J.-L. V., Deviere J., Resibois A., Rickaert F., Vertongen P., Ohtani V., Cremer M., Miyazono K., Robberecht P. Localization of transforming growth factor β1 and its latent binding protein in human chronic pancreatitis. Gastroenterology. 108:1995;1873-1881.
11. Taniguchi N. Clinical significances of superoxide dismutases: Changes in aging, diabetes, ischemia, and cancer. Adv. Clin. Chem. 29:1992;1-59.
12. Halliwell B., Gutteridge J.M.C. Free radicals in biology and medicine. 2nd Ed:1989;Oxford University Press, London.
13. Mandrup-Poulsen T., Helqvist S., Wogensen L.D., Molvig J., Pociot F., Johannesen J., Nerup J. Cytokines and free radicals as effector molecules in the destruction of pancreatic beta cells. Curr. Top. Microbiol. Immunol. 164:1990;169-193.
14. Hockenbery D. M., Oltvai Z. N., Yin X.-M., Milliman C. L., Korsmeyer S. J. Bcl-2 functions in an antioxidant pathway to prevent apoptosis. Cell. 75:1993;241-251.
15. Ratan R. R., Murphy T. H., Baraban J. M. Oxidative stress induces apoptosis in embryonic cortical neurons. J. Neurochem. 62:1994;376-379.
16. Sandstrom P. A., Buttke T. M. Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium. Proc. Natl. Acad. Sci. USA. 90:1993;4708-4712.
17. Dypbukt J. M., Ankarcrona M., Burkitt M., Sjoholm A., Strom K., Orrenius S., Nicotera P. Different prooxidant levels stimulate growth, trigger apoptosis, or produce necrosis of insulin-secreting RINm5F cells. J. Biol. Chem. 269:1994;30553-30560.
18. Michiels C., Raes M., Toussaint O., Remacle J. Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17:1994;235-248.
19. Yoshimura S., Takekoshi S., Watanabe K., Fujii-Kuriyama Y. Determination of nucleotide sequence of cDNA coding rat glutathione peroxidase and diminished expression of the mRNA in selenium deficient rat liver. Biochem. Biophys. Res. Commun. 154:1988;1024-1028.
20. Korsmeyer S. J. Bcl-2 initiates a new category of oncogenes: Regulators of cell death. Blood. 80:1992;879-886.
21. Kayanoki Y., Fujii J., Suzuki K., Kawata S., Matsuzawa Y., Taniguchi N. Suppression of antioxidative enzyme expression by transforming growth factor- β1 in rat hepatocytes. J. Biol. Chem. 269:1994;15488-15492.
22. Yamazaki S., Onishi E., Enami K., Natori K., Kohase M., Sakamoto H., Tanouchi M., Hayashi H. Proposal of standardized methods and reference for assaying recombinant human tumor necrosis factor. Jpn. J. Med. Sci. Biol. 39:1986;105-118.
23. Kaneto H., Fujii J., Seo H. G., Suzuki K., Matsuoka T., Nakamura M., Tatsumi H., Yamasaki Y., Kamada T., Taniguchi N. Apoptotic cell death triggered by nitric oxide in pancreatic β -cell. Diabetes. 44:1995;733-738.
24. Levine R. L., Garland D., Oliver C. N., Amici A., Climent I., Lenz A.-G., Ahn B.-W., Shaltiel S., Stadtman E. R. Determination of carbonyl content in oxidatively modified protein. Methods Enzymol. 186:1990;464-478.
25. Esterbauer H., Cheeseman K. H. Determination of aldehydic lipid peroxidation products: Malondialdehyde and 4-hydroxynonenal. Methods Enzymol. 186:1990;407-421.
26. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
27. Furuta S., Hayashi H., Hijikata M., Miyazawa S., Osumi T., Hashimoto T. Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase. Proc. Natl. Acad. Sci. USA. 83:1986;313-317.
28. Delabar J-M., Nicole A., D'auriol L., Jacob Y., Meunier-Rotival M., Galibert F., Sinet P-M., Jerome H. Cloning and sequencing of a rat CuZn superoxide dismutase cDNA: Correlation between CuZn superoxide dismutase mRNA level and enzyme activity in rat and mouse tissues. Eur. J. Biochem. 166:1987;181-187.
29. Maniatis, T.; Fritsch, E. F.; Sambrook, J. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY: 1982.
30. Geiger P. G., Lin F., Girotti A. W. Selenoperoxidase-mediated cytoprotection against the damaging effects of tert-butyl hydroperoxide on leukemia cells. Free Radic. Biol. Med. 14:1993;251-266.
31. Claiborne A. Handbook of methods for oxygen free radical research. 1985;283-284 CRC Press Inc, Boca Raton, FL.
32. Bass D. A., Parce J. W., Dechatelet L. R., Szejda P., Seeds M. C., Thomas M. Flow cytometric studies of oxidative product formation by neutrophils: A graded response to membrane stimulation. J. Immunol. 130:1983;1910-1917.
33. Sies H. Oxidative Stress. 1985;Academic Press, New York.
34. Jones T. W., Thor H., Orrenius S. Cellular defense mechanisms against toxic substances. Arch. Toxicol. 9:(Suppl.):1986;259-271.
35. Oberhammer F. A., Pavelka M., Sharma S., Tifenbacher R., Purchio A. F., Bursch W., Schulte-Hermann R. Induction of apoptosis in cultured hepatocytes and in regressing liver by transforming growth factor β1 . Proc. Natl. Acad. Sci. USA. 89:1992;5408-5412.
36. Lennon S. V., Martin S. J., Cotter T. G. Dose dependent induction of apoptosis in human tumour cell lines by widely diverging stimuli. Cell Prolif. 24:1991;203-214.
37. 2 and phosphorylation of 30 kilodalton proteins as early responses of cell cycle-dependent inhibition of DNA synthesis by transforming growth factor β1 . Cell Growth Diff. 2:1991;583-591.
38. Aruoma O. I., Halliwell B., Hoey B. M., Butler J. The antioxidant action of N-acetylcysteine: Its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid. Free Radic. Biol. Med. 6:1989;593-597.
39. Meister A. Glutathione metabolism and its selective modification. J. Biol. Chem. 263:1988;17205-17208.
40. Simon R. H., Scoggin C. H., Patterson D. Hydrogen peroxide causes the fatal injury to human fibroblasts exposed to oxygen radicals. J. Biol. Chem. 256:1981;7181-7186.
41. Nakamura Y., Colburn N. H., Gindhart T. D. Role of reactive oxygen in tumor promotion: Implication of superoxide anion in promotion of neoplastic transformation in JB-6 cells by TPA. Carcinogenesis. 6:1985;229-235.
42. Ookawara T., Kawamura N., Kitagawa Y., Taniguchi N. Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction: Implication of reactive oxygen species. J. Biol. Chem. 267:1992;18505-18510.
43. Islam K. N., Takahashi M., Higashiyama S., Myint T., Uozumi N., Kayanoki Y., Kaneto H., Kosaka H., Taniguchi N. Fragmentation of ceruloplasmin following non-enzymatic glycation reaction. J. Biochem. 118:1995;1054-1060.
44. Tian L., Cai Q., Bowen R, Wei H. Effects of caloric restriction on age-related oxidative modifications of macromolecules and lymphocyte proliferation in rats. Free Radic. Biol. Med. 19:1995;859-865.
45. Halliwell B., Gutteridge J. M. C., Cross C. E. Free radicals, antioxidants, and human disease: Where are we now? J. Lab. Clin. Med. 119:1992;598-620.
46. Emerit I., Cerutti P. A. Tumour promoter phorbol-12-myristate-13-acetate induces chromosomal damage via indirect action. Nature. 293:1981;144-146.
47. Kinsella A. R., Radman M. Tumor promoter induces sister chromatid exchanges: Relevance to mechanisms of carcinogenesis. Proc. Natl. Acad. Sci. USA. 75:1978;6149-6153.
48. Stadtman E. R. Metal ion catalyzed oxidation of proteins: Biochemical mechanism and biological consequences. Free Radic. Biol. Med. 9:1990;315-325.
49. Oliver C. N., Bong-Whan A., Moerman E. J., Goldstein S., Stadtman E. R. Age-related changes in oxidized proteins. J. Biol. Chem. 262:1987;5488-5491.
50. Starke-Reed P. E., Oliver C. N. Protein oxidation and proteolysis during aging and oxidative stress. Arch. Biochem. Biophys. 275:1989;559-567.