메뉴 건너뛰기




Volumn 57, Issue 3, 2006, Pages 357-367

Bcl-2-mediated potentiation of neocarzinostatin-induced apoptosis: Requirement for caspase-3, sulfhydryl groups, and cleavable Bcl-2

Author keywords

Apoptosis; Caspase 3; Chemotherapeutic agent; Enediyne; Reduced glutathione

Indexed keywords

CASPASE 3; PROTEIN BCL 2; THIOL GROUP; ZINOSTATIN; ANTINEOPLASTIC ANTIBIOTIC; CASP3 PROTEIN, HUMAN; CASP3 PROTEIN, RAT; CASPASE; GLUTATHIONE; NAPHTHALENE DERIVATIVE; PROTEIN BAX; PYRROLE DERIVATIVE; THIOGLO 1; THIOGLO-1; THIOL DERIVATIVE;

EID: 33644837259     PISSN: 03445704     EISSN: 14320843     Source Type: Journal    
DOI: 10.1007/s00280-005-0054-z     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0027164144 scopus 로고
    • High expression of bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy
    • Campos L, Rouault JP, Sabido O, Oriol P, Roubi N, Vasselon C et al (1993) High expression of bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy. Blood 81(11):3091-3096
    • (1993) Blood , vol.81 , Issue.11 , pp. 3091-3096
    • Campos, L.1    Rouault, J.P.2    Sabido, O.3    Oriol, P.4    Roubi, N.5    Vasselon, C.6
  • 3
    • 0028979439 scopus 로고
    • Bcl-xL is expressed in neuroblastoma cells and modulates chemotherapy-induced apoptosis
    • Dole MG, Jasty R, Cooper MJ, Thompson CB, Nunez G, Castle VP (1995) Bcl-xL is expressed in neuroblastoma cells and modulates chemotherapy-induced apoptosis. Cancer Res 55(12):2576-2582
    • (1995) Cancer Res , vol.55 , Issue.12 , pp. 2576-2582
    • Dole, M.G.1    Jasty, R.2    Cooper, M.J.3    Thompson, C.B.4    Nunez, G.5    Castle, V.P.6
  • 4
    • 0029157380 scopus 로고
    • Estrogen promotes chemotherapeutic drug resistance by a mechanism involving Bcl-2 proto-oncogene expression in human breast cancer cells
    • Teixeira C, Reed JC, Pratt MA (1995) Estrogen promotes chemotherapeutic drug resistance by a mechanism involving Bcl-2 proto-oncogene expression in human breast cancer cells. Cancer Res 55(17):3902-3907
    • (1995) Cancer Res , vol.55 , Issue.17 , pp. 3902-3907
    • Teixeira, C.1    Reed, J.C.2    Pratt, M.A.3
  • 5
    • 84996702994 scopus 로고    scopus 로고
    • Bcl-2 confers resistance to androgen deprivation in prostate carcinoma cells
    • Beham AW, McDonnell TJ (1996) Bcl-2 confers resistance to androgen deprivation in prostate carcinoma cells. Proc Amer Assoc Cancer Res 37:224
    • (1996) Proc Amer Assoc Cancer Res , vol.37 , pp. 224
    • Beham, A.W.1    McDonnell, T.J.2
  • 7
    • 0033549248 scopus 로고    scopus 로고
    • Selective oxidation and externalization of membrane phosphatidylserine: Bcl-2-induced potentiation of the final common pathway for apoptosis
    • Schor NF, Tyurina YY, Fabisiak JP, Tyurin VA, Lazo JS, Kagan VE (1999) Selective oxidation and externalization of membrane phosphatidylserine: Bcl-2-induced potentiation of the final common pathway for apoptosis. Brain Res 831(1-2):125-130
    • (1999) Brain Res , vol.831 , Issue.1-2 , pp. 125-130
    • Schor, N.F.1    Tyurina, Y.Y.2    Fabisiak, J.P.3    Tyurin, V.A.4    Lazo, J.S.5    Kagan, V.E.6
  • 8
    • 0028863552 scopus 로고
    • Induction of apoptosis in murine and human neuroblastoma cell lines by the enediyne natural product neocarzinostatin
    • Hartsell TL, Yalowich JC, Ritke MK, Martinez AJ, Schor NF (1995) Induction of apoptosis in murine and human neuroblastoma cell lines by the enediyne natural product neocarzinostatin. J Pharmacol Exp Ther 275(1):479-485
    • (1995) J Pharmacol Exp Ther , vol.275 , Issue.1 , pp. 479-485
    • Hartsell, T.L.1    Yalowich, J.C.2    Ritke, M.K.3    Martinez, A.J.4    Schor, N.F.5
  • 9
    • 0030435331 scopus 로고    scopus 로고
    • Determinants of the response of neuroblastoma cells to DNA damage: The roles of pre-treatment cell morphology and chemical nature of the damage
    • Hartsell TL, Hinman LM, Hamann PR, Schor NF (1996) Determinants of the response of neuroblastoma cells to DNA damage: the roles of pre-treatment cell morphology and chemical nature of the damage. J Pharmacol Exp Ther 277(2):1158-1166
    • (1996) J Pharmacol Exp Ther , vol.277 , Issue.2 , pp. 1158-1166
    • Hartsell, T.L.1    Hinman, L.M.2    Hamann, P.R.3    Schor, N.F.4
  • 10
    • 0027717968 scopus 로고
    • Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species
    • Kane DJ, Sarafian TA, Anton R, Hahn H, Gralla EB, Valentine JS et al (1993) Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species. Science 262(5137):1274-1247
    • (1993) Science , vol.262 , Issue.5137 , pp. 1247-1274
    • Kane, D.J.1    Sarafian, T.A.2    Anton, R.3    Hahn, H.4    Gralla, E.B.5    Valentine, J.S.6
  • 11
    • 0029923503 scopus 로고    scopus 로고
    • Potentiation of enediyne-induced apoptosis and differentiation by Bcl-2
    • Cortazzo M, Schor NF (1996) Potentiation of enediyne-induced apoptosis and differentiation by Bcl-2. Cancer Res 56(6):1199-1203
    • (1996) Cancer Res , vol.56 , Issue.6 , pp. 1199-1203
    • Cortazzo, M.1    Schor, N.F.2
  • 13
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng EH, Kirsch DG, Clem RJ, Ravi R, Kastan MB, Bedi A et al (1997) Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 278(5345):1966-1968
    • (1997) Science , vol.278 , Issue.5345 , pp. 1966-1968
    • Cheng, E.H.1    Kirsch, D.G.2    Clem, R.J.3    Ravi, R.4    Kastan, M.B.5    Bedi, A.6
  • 14
    • 0036140941 scopus 로고    scopus 로고
    • Role of caspase 3-dependent Bcl-2 cleavage in potentiation of apoptosis by Bcl-2
    • Liang Y, Nylander KD, Yan C, Schor NF (2002) Role of caspase 3-dependent Bcl-2 cleavage in potentiation of apoptosis by Bcl-2. Mol Pharmacol 61(1):142-149
    • (2002) Mol Pharmacol , vol.61 , Issue.1 , pp. 142-149
    • Liang, Y.1    Nylander, K.D.2    Yan, C.3    Schor, N.F.4
  • 15
    • 0017364886 scopus 로고
    • Single-strand nicking of DNA in vitro by neocarzinostatin and its possible relationship to the mechanism of drug action
    • Beerman TA, Poon R, Goldberg IH (1977) Single-strand nicking of DNA in vitro by neocarzinostatin and its possible relationship to the mechanism of drug action. Biochim Biophys Acta 475(2):294-306
    • (1977) Biochim Biophys Acta , vol.475 , Issue.2 , pp. 294-306
    • Beerman, T.A.1    Poon, R.2    Goldberg, I.H.3
  • 16
    • 0022387875 scopus 로고
    • Glutathione dependence of neocarzinostatin cytotoxicity and mutagenicity in Chinese hamster V-79 cells
    • DeGraff WG, Mitchell JB (1985) Glutathione dependence of neocarzinostatin cytotoxicity and mutagenicity in Chinese hamster V-79 cells. Cancer Res 45(10):4760-4762
    • (1985) Cancer Res , vol.45 , Issue.10 , pp. 4760-4762
    • DeGraff, W.G.1    Mitchell, J.B.2
  • 17
    • 0026533105 scopus 로고
    • Targeted enhancement of the biological activity of the antineoplastic agent, neocarzinostatin. Studies in murine neuroblastoma cells
    • Schor NF (1992) Targeted enhancement of the biological activity of the antineoplastic agent, neocarzinostatin. Studies in murine neuroblastoma cells. J Clin Invest 89(3):774-781
    • (1992) J Clin Invest , vol.89 , Issue.3 , pp. 774-781
    • Schor, N.F.1
  • 18
    • 0027282044 scopus 로고
    • Bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
    • Boise LH, Gonzalez-Garcia M, Postema CE, Ding L, Lindsten T, Turka LA et al (1993) bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 74(4):597-608
    • (1993) Cell , vol.74 , Issue.4 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3    Ding, L.4    Lindsten, T.5    Turka, L.A.6
  • 19
    • 0035502997 scopus 로고    scopus 로고
    • Pro-oxidant and antioxidant mechanisms of etoposide in HL-60 cells: Role of myeloperoxidase
    • Kagan VE, Kuzmenko AI, Tyurina YY, Shvedova AA, Matsura T, Yalowich JC (2001) Pro-oxidant and antioxidant mechanisms of etoposide in HL-60 cells: role of myeloperoxidase. Cancer Res 61(21):7777-7784
    • (2001) Cancer Res , vol.61 , Issue.21 , pp. 7777-7784
    • Kagan, V.E.1    Kuzmenko, A.I.2    Tyurina, Y.Y.3    Shvedova, A.A.4    Matsura, T.5    Yalowich, J.C.6
  • 20
    • 0029961387 scopus 로고    scopus 로고
    • Comparative analysis of flow cytometric methods for apoptosis quantitation in murine thymocytes and human peripheral lymphocytes from controls and HIV-infected persons evidence for interference by granulocytes and erythrocytes
    • Lecoeur H, Gougeon ML (1996) Comparative analysis of flow cytometric methods for apoptosis quantitation in murine thymocytes and human peripheral lymphocytes from controls and HIV-infected persons evidence for interference by granulocytes and erythrocytes. J Immunol Meth 198(1):87-99
    • (1996) J Immunol Meth , vol.198 , Issue.1 , pp. 87-99
    • Lecoeur, H.1    Gougeon, M.L.2
  • 22
    • 0019827110 scopus 로고
    • Neocarzinostatin: Report of a phase II clinical trial
    • McKelvey EM, Murphy W, Zander A, Bodey GP (1981) Neocarzinostatin: report of a phase II clinical trial. Cancer Treat Rep 65(7-8):699-701
    • (1981) Cancer Treat Rep , vol.65 , Issue.7-8 , pp. 699-701
    • McKelvey, E.M.1    Murphy, W.2    Zander, A.3    Bodey, G.P.4
  • 23
    • 0018860287 scopus 로고
    • Phase II trial of neocarzinostatin in patients with bladder and prostatic cancer: Toxicity of a five-day iv bolus schedule
    • Natale RB, Yagoda A, Watson RC, Stover DE (1980) Phase II trial of neocarzinostatin in patients with bladder and prostatic cancer: toxicity of a five-day iv bolus schedule. Cancer 45(11):2836-2842
    • (1980) Cancer , vol.45 , Issue.11 , pp. 2836-2842
    • Natale, R.B.1    Yagoda, A.2    Watson, R.C.3    Stover, D.E.4
  • 24
    • 0035807288 scopus 로고    scopus 로고
    • Apoptosis in the absence of caspase 3
    • Liang Y, Yan C, Schor NF (2001) Apoptosis in the absence of caspase 3. Oncogene 20(45):6570-6578
    • (2001) Oncogene , vol.20 , Issue.45 , pp. 6570-6578
    • Liang, Y.1    Yan, C.2    Schor, N.F.3
  • 25
    • 0242551451 scopus 로고    scopus 로고
    • Early events in Bcl-2-enhanced apoptosis
    • Liang Y, Yan C, Nylander KD, Schor NF (2003) Early events in Bcl-2-enhanced apoptosis. Apoptosis 8(6):609-616
    • (2003) Apoptosis , vol.8 , Issue.6 , pp. 609-616
    • Liang, Y.1    Yan, C.2    Nylander, K.D.3    Schor, N.F.4
  • 27
    • 0032189535 scopus 로고    scopus 로고
    • Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells
    • Fulda S, Susin SA, Kroemer G, Debatin KM (1998) Molecular ordering of apoptosis induced by anticancer drugs in neuroblastoma cells. Cancer Res 58(19):4453-4460
    • (1998) Cancer Res , vol.58 , Issue.19 , pp. 4453-4460
    • Fulda, S.1    Susin, S.A.2    Kroemer, G.3    Debatin, K.M.4
  • 28
    • 0033587708 scopus 로고    scopus 로고
    • Herpes simplex virus thymidine kinase/ ganciclovir-induced apoptosis involves ligand-independent death receptor aggregation and activation of caspases
    • Beltinger C, Fulda S, Kammertoens T, Meyer E, Uckert W, Debatin KM (1999) Herpes simplex virus thymidine kinase/ ganciclovir-induced apoptosis involves ligand-independent death receptor aggregation and activation of caspases. Proc Natl Acad Sci USA 96(15):8699-8704
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.15 , pp. 8699-8704
    • Beltinger, C.1    Fulda, S.2    Kammertoens, T.3    Meyer, E.4    Uckert, W.5    Debatin, K.M.6
  • 29
    • 85047682789 scopus 로고    scopus 로고
    • Taxol-induced apoptosis in human SKOV3 ovarian and MCF7 breast carcinoma cells is caspase-3 and caspase-9 independent
    • Ofir R, Seidman R, Rabinski T, Krup M, Yavelsky V, Weinstein Y et al (2002) Taxol-induced apoptosis in human SKOV3 ovarian and MCF7 breast carcinoma cells is caspase-3 and caspase-9 independent. Cell Death Differ 9(6):636-642
    • (2002) Cell Death Differ , vol.9 , Issue.6 , pp. 636-642
    • Ofir, R.1    Seidman, R.2    Rabinski, T.3    Krup, M.4    Yavelsky, V.5    Weinstein, Y.6
  • 30
    • 0037192631 scopus 로고    scopus 로고
    • Ganciclovir-induced apoptosis in HSV-1 thymidine kinase expressing cells: Critical role of DNA breaks, Bcl-2 decline and caspase-9 activation
    • Tomicic MT, Thust R, Kaina B (2002) Ganciclovir-induced apoptosis in HSV-1 thymidine kinase expressing cells: critical role of DNA breaks, Bcl-2 decline and caspase-9 activation. Oncogene 21(14):2141-2153
    • (2002) Oncogene , vol.21 , Issue.14 , pp. 2141-2153
    • Tomicic, M.T.1    Thust, R.2    Kaina, B.3
  • 31
    • 12244251385 scopus 로고    scopus 로고
    • Involvement of mitochondrial pathway in Taxol-induced apoptosis of human T24 bladder cancer cells
    • Yuan SY, Hsu SL, Tsai KJ, Yang CR (2002) Involvement of mitochondrial pathway in Taxol-induced apoptosis of human T24 bladder cancer cells. Urol Res 30(5):282-288
    • (2002) Urol Res , vol.30 , Issue.5 , pp. 282-288
    • Yuan, S.Y.1    Hsu, S.L.2    Tsai, K.J.3    Yang, C.R.4
  • 32
    • 0032508504 scopus 로고    scopus 로고
    • Enhanced phosphorylation of p53 by ATM in response to DNA damage
    • Banin S, Moyal L, Shieh S, Taya Y, Anderson CW, Chessa L et al (1998) Enhanced phosphorylation of p53 by ATM in response to DNA damage. Science 281(5383):1674-1677
    • (1998) Science , vol.281 , Issue.5383 , pp. 1674-1677
    • Banin, S.1    Moyal, L.2    Shieh, S.3    Taya, Y.4    Anderson, C.W.5    Chessa, L.6
  • 33
    • 0038637168 scopus 로고    scopus 로고
    • Neocarzinostatin induces an effective p53-dependent response in human papillomavirus-positive cervical cancer cells
    • Banuelos A, Reyes E, Ocadiz R, Alvarez E, Moreno M, Monroy A et al (2003) Neocarzinostatin induces an effective p53-dependent response in human papillomavirus-positive cervical cancer cells. J Pharmacol Exp Ther 306(2):671-680
    • (2003) J Pharmacol Exp Ther , vol.306 , Issue.2 , pp. 671-680
    • Banuelos, A.1    Reyes, E.2    Ocadiz, R.3    Alvarez, E.4    Moreno, M.5    Monroy, A.6
  • 34
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ (1999) BCL-2 family members and the mitochondria in apoptosis. Genes Dev 13(15):1899-1911
    • (1999) Genes Dev , vol.13 , Issue.15 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 35
    • 0343340396 scopus 로고    scopus 로고
    • Redox control of caspase-3 activity by thioredoxin and other reduced proteins
    • Baker A, Santos BD, Powis G (2000) Redox control of caspase-3 activity by thioredoxin and other reduced proteins. Biochem Biophys Res Commun 268(1):78-81
    • (2000) Biochem Biophys Res Commun , vol.268 , Issue.1 , pp. 78-81
    • Baker, A.1    Santos, B.D.2    Powis, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.