Methioninase gene therapy with selenomethionine induces apoptosis in bcl-2-overproducing lung cancer cells

Cancer Gene Therapy

Volumn 10, Issue 6, 2003, Pages 445-450

  Yamamoto, Norio ^a,b,c   Gupta, Anshu ^a,b   Xu, Mingxu ^a   Miki, Kenji ^a,d   Tsujimoto, Yoshihide ^e   Tsuchiya, Hiroyuki ^c   Tomita, Katsuro ^c   Moossa, A R ^b   Hoffman, R M ^a,b  

^a ANTICANCER INC   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c KANAZAWA UNIVERSITY   (Japan)

^d UNIVERSITY OF TOKYO   (Japan)

^e OSAKA UNIVERSITY   (Japan)

Author keywords

A549; MET gene therapy; Methyl selenol; Prodrug; Suicide therapy

Indexed keywords

ADENOVIRUS VECTOR; CYTOCHROME C; METHIONINE GAMMA LYASE; METHYLSELENOL; OXIDIZING AGENT; PRODRUG; PROTEIN BCL 2; RECOMBINANT ENZYME; SELENOMETHIONINE; STAUROSPORINE; UNCLASSIFIED DRUG;

APOPTOSIS; ARTICLE; BYSTANDER EFFECT; CANCER CELL; CANCER CELL CULTURE; CANCER THERAPY; CELL CLONE; CELL TRANSFORMATION; CONTROLLED STUDY; DRUG EFFICACY; ENZYME RELEASE; GENE DIRECTED ENZYME PRODRUG THERAPY; GENE OVEREXPRESSION; GENE THERAPY; HUMAN; HUMAN CELL; LUNG CANCER; METHIONINE GAMMA LYASE GENE; MITOCHONDRION; MOLECULAR CLONING; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN SYNTHESIS; PSEUDOMONAS PUTIDA; SUICIDE GENE THERAPY; VIRUS GENE;

APOPTOSIS; BISBENZIMIDE; BLOTTING, WESTERN; CARBON-SULFUR LYASES; CELL LINE, TUMOR; CELL NUCLEUS; CELL SURVIVAL; COLORING AGENTS; CYTOCHROMES C; CYTOSOL; DNA FRAGMENTATION; ENZYME-LINKED IMMUNOSORBENT ASSAY; GENE THERAPY; HUMANS; LUNG NEOPLASMS; MITOCHONDRIA; MODELS, BIOLOGICAL; OXIDANTS; OXIDATIVE STRESS; PROTO-ONCOGENE PROTEINS C-BCL-2; PSEUDOMONAS PUTIDA; SELENOMETHIONINE; STAUROSPORINE; TETRAZOLIUM SALTS; THIAZOLES; TRANSFECTION;

ADENOVIRIDAE; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0038616070     PISSN: 09291903     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cgt.7700587     Document Type: Article

References (29)

1. Miki K, Xu M, Gupta A, et al. Methioninase cancer gene therapy with selenomethionine as suicide prodrug substrate. Cancer Res. 2001;61:6805-6810.
2. Wolter KG, Hsu YT, Smith CL, Nechushtan A, Xi XG, Youle RJ. Movement of Bax from the cytosol to mitochondria during apoptosis. J Cell Biol. 1997;139:1281-1292.
3. Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med. 2000;6:513-519.
4. Costantini P, Jacotot E, Decaudin D, Kroemer G. Mitochondrion as a novel target of anticancer chemotherapy. J Nat Cancer Inst. 2000;92:1042-1053.
5. Susin SA, Zamzami N, Castedo M, et al. Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J Exp Med. 1996;184:1331-1341.
6. Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 reguration of apoptosis. Science. 1997;275:1132-1136.
7. Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 1997;275:1129-1132.
8. Weller M, Malipiero U, Aguzzi A, Reed JC, Fontana A. Protooncogene bcl-2 gene transfer abrogates Fas/APO-1 antobody-mediated apoptosis of human malignant glioma cells and confers to resistance to chemotherapeutic drugs and therapeutic irradiation. J Clin Invest. 1995;95:2633-2643.
9. Hamel W, Magnelli L, Chiarugi VP, Israel MA. Herpes simplex virus thymidine kinase/ganciclovir-mediated apoptosis death of bystander cells. Cancer Res. 1996;56:2697-2702.
10. Carsten F, Christoph S, Barbara H, et al. Bcl-2 expression in high-grade human glioma: clinical and experimental study. J Neurooncol. 2000;48:207-216.
11. Tu Y, Xu FH, Liu J, et al. Upregulated expression of BCL-2 in multiple myeloma cells induced by exposure to doxorubicin, etoposide, and hydrogen peroxide. Blood. 1996;88:1805-1812.
12. Elstein KH, Zucker RM. Comparison of cellular and nuclear flow cytometirc techniques for discriminating apoptotic subpopulations. Exp Cell Res. 1994;211:322-331.
13. Susin SA, Lorenzo HK, Zamzami N, et al. Mitochondrial release of caspase-2 and -9 during the apoptotic process. J Exp Med. 1999;189:381-394.
14. Susin SA, Lorenzo HK, Zamzami N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature. 1999;397:441-446.
15. 2+ mobilization promotes cytochrome c release during apoptosis. J. Biol Chem. 2002;277:20301-20308.
16. Spallholz JE. On the nature of selenium toxicity and carcinostatic activity. Free Radic Biol Med. 1994;17:45-64.
17. Stewart MS, Spallholz JE, Nelder KH, Pence BC. Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis. Free Radic Biol Med. 1999;26:42-48.
18. Clark LC, Combs GF, Turnbull BW, et al. Effects of selenium supplementation for cancer prevention in patients with carcinoma of the skin. A randomized controlled trial. JAMA. 1996;276:1957-1963.
19. Chaudiere J, Courtin O, Leclaire J. Glutathione oxidase activity of selenocystamine: a mechanistic study. Arch Biochem Biophys. 1992;296:328-336.
20. Yan L, Spallholz E. Generation of reactive oxygen species from the reaction of selenium compounds with thiols and mammary tumor cells. Biochem Pharmacol. 1993;45:429-437.
21. Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998;281:1309-1312.
22. Cai J, Yang J, Jones DP. Mitochondrial control of apoptosis: The role of cytochrome c. Biochim Biophys Acta. 1998;1366:139-149.
23. Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-caspase-9 complex initiates an apoptotic protease cascades. Cell. 1997;91:479-489.
24. Thornberry NA, Lazebnik Y. Caspase: enemies within. Science. 1998;281:1312-1316.
25. Tanaka H, Esaki N, Soda K. Properties of L-methionine γlyase from Pseudomonas ovalis. Biochemistry. 1977;16:100- 106.
26. Inoue H, Inagaki K, Sugimoto M, Esaki N, Soda K, Tanaka H. Structure analysis of the L-methionine y-lyase gene from Pseudomonas putida. J Biochem. 1995;117:1120-1125.
27. Esaki N, Tanaka H, Uemura S, Suzuki T, Soda K. Catalytic action of L-methionine gamma-lyase on selenomethionine and selenols. Biochemistry. 1979;18:407-410.
28. Akhaven-Tafti H, et al. Clin Chem. 1995;41:1368-1369.
29. Iwahashi H, Eguchi Y, Yasuhara N, et al. Synergistic antiapoptotic activity between Bcl-2 and SMN implicated in spinal atrophy. Nature. 1997;390:413-417.