메뉴 건너뛰기




Volumn 7, Issue 5, 2012, Pages

MDA-7/IL-24 induces Bcl-2 denitrosylation and ubiquitin-degradation involved in cancer cell apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

2 (4 CARBOXYPHENYL) 4,4,5,5 TETRAMETHYLIMIDAZOLINE 1 OXYL 3 OXIDE; 26S PROTEASOME; AURANOFIN; CASPASE; CONDITIONALLY REPLICATING ADENOVIRUS; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 24; NITRIC OXIDE; PROTEASOME; PROTEIN BCL 2; SMALL INTERFERING RNA; THIOREDOXIN REDUCTASE 1; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84861313000     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037200     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 0029558740 scopus 로고
    • Subtraction hybridization identifies a novel melanoma differentiation associated gene, MDA-7, modulated during human melanoma differentiation, growth and progression
    • Jiang H, Lin JJ, Su ZZ, Goldstein NI, Fisher PB, (1995) Subtraction hybridization identifies a novel melanoma differentiation associated gene, MDA-7, modulated during human melanoma differentiation, growth and progression. Oncogene 11: 2477-2486.
    • (1995) Oncogene , vol.11 , pp. 2477-2486
    • Jiang, H.1    Lin, J.J.2    Su, Z.Z.3    Goldstein, N.I.4    Fisher, P.B.5
  • 2
    • 0029808333 scopus 로고    scopus 로고
    • The melanoma differentiation associated gene MDA-7 suppresses cancer cell growth
    • Jiang H, Su ZZ, Lin JJ, Goldstein NI, Young CSH, et al. (1996) The melanoma differentiation associated gene MDA-7 suppresses cancer cell growth. Proc Natl Acad Sci USA 93: 9160-9165.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9160-9165
    • Jiang, H.1    Su, Z.Z.2    Lin, J.J.3    Goldstein, N.I.4    Young, C.S.H.5
  • 4
    • 33745593993 scopus 로고    scopus 로고
    • MDA-7/IL-24: multifunctional cancer-specific apoptosis-inducing cytokine
    • Gupta P, Su ZZ, Lebedeva IV, Sarkar D, Sauane M, et al. (2006) MDA-7/IL-24: multifunctional cancer-specific apoptosis-inducing cytokine. Pharmacol Ther 111: 596-628.
    • (2006) Pharmacol Ther , vol.111 , pp. 596-628
    • Gupta, P.1    Su, Z.Z.2    Lebedeva, I.V.3    Sarkar, D.4    Sauane, M.5
  • 5
    • 0037468264 scopus 로고    scopus 로고
    • Melanoma differentiation associated gene-7, MDA-7/IL-24, selectively induces growth suppression, apoptosis and radiosensitization in malignant gliomas in a p53-independent manner
    • Su ZZ, Lebedeva IV, Sarkar D, Gopalkrishnan RV, Sauane M, et al. (2003) Melanoma differentiation associated gene-7, MDA-7/IL-24, selectively induces growth suppression, apoptosis and radiosensitization in malignant gliomas in a p53-independent manner. Oncogene 22: 1164-1180.
    • (2003) Oncogene , vol.22 , pp. 1164-1180
    • Su, Z.Z.1    Lebedeva, I.V.2    Sarkar, D.3    Gopalkrishnan, R.V.4    Sauane, M.5
  • 6
    • 1642383850 scopus 로고    scopus 로고
    • MDA-7 (IL-24) Inhibits growth and enhances radiosensitivity of glioma cells in vitro via JNK signaling
    • Yacoub A, Mitchell C, Lebedeva IV, Sarkar D, Su ZZ, et al. (2003) MDA-7 (IL-24) Inhibits growth and enhances radiosensitivity of glioma cells in vitro via JNK signaling. Cancer Biol Ther 2: 347-353.
    • (2003) Cancer Biol Ther , vol.2 , pp. 347-353
    • Yacoub, A.1    Mitchell, C.2    Lebedeva, I.V.3    Sarkar, D.4    Su, Z.Z.5
  • 7
    • 0346365376 scopus 로고    scopus 로고
    • Melanoma differentiation associated gene-7, MDA-7/interleukin-24, induces apoptosis in prostate cancer cells by promoting mitochondrial dysfunction and inducing reactive oxygen species
    • Lebedeva IV, Su ZZ, Sarkar D, Kitada S, Dent P, et al. (2003) Melanoma differentiation associated gene-7, MDA-7/interleukin-24, induces apoptosis in prostate cancer cells by promoting mitochondrial dysfunction and inducing reactive oxygen species. Cancer Res. 63: 8138-8144.
    • (2003) Cancer Res , vol.63 , pp. 8138-8144
    • Lebedeva, I.V.1    Su, Z.Z.2    Sarkar, D.3    Kitada, S.4    Dent, P.5
  • 8
    • 0345732497 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL differentially protect human prostate cancer cells from induction of apoptosis by melanoma differentiation associated gene-7, MDA-7/IL-24
    • Lebedeva IV, Sarkar D, Su ZZ, Kitada S, Dent P, et al. (2003) Bcl-2 and Bcl-xL differentially protect human prostate cancer cells from induction of apoptosis by melanoma differentiation associated gene-7, MDA-7/IL-24. Oncogene 22: 8758-8773.
    • (2003) Oncogene , vol.22 , pp. 8758-8773
    • Lebedeva, I.V.1    Sarkar, D.2    Su, Z.Z.3    Kitada, S.4    Dent, P.5
  • 9
    • 28544435618 scopus 로고    scopus 로고
    • Is MDA-7/IL-24 a "magic bullet" for cancer?
    • Fisher PB, (2005) Is MDA-7/IL-24 a "magic bullet" for cancer? Cancer Res 65: 10128-10138.
    • (2005) Cancer Res , vol.65 , pp. 10128-10138
    • Fisher, P.B.1
  • 12
    • 0035964399 scopus 로고    scopus 로고
    • A combinatorial approach for selectively inducing programmed cell death in human pancreatic cancer cells
    • Su Z, Lebedeva IV, Gopalkrishnan RV, Goldstein NI, Stein CA, et al. (2001) A combinatorial approach for selectively inducing programmed cell death in human pancreatic cancer cells. Proc Natl Acad Sci U S A 98: 10332-10337.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10332-10337
    • Su, Z.1    Lebedeva, I.V.2    Gopalkrishnan, R.V.3    Goldstein, N.I.4    Stein, C.A.5
  • 13
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD, (1997) The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 14
    • 1842430458 scopus 로고    scopus 로고
    • Current strategies to target the anti-apoptotic Bcl-2 protein in cancer cells
    • Osford SM, Dallman CL, Johnson PW, Ganesan A, Packham G, (2004) Current strategies to target the anti-apoptotic Bcl-2 protein in cancer cells. Curr Med Chem 11: 1031-1039.
    • (2004) Curr Med Chem , vol.11 , pp. 1031-1039
    • Osford, S.M.1    Dallman, C.L.2    Johnson, P.W.3    Ganesan, A.4    Packham, G.5
  • 15
    • 33747497689 scopus 로고    scopus 로고
    • Targeting gene-virotherapy of cancer
    • Liu XY, Gu JF, (2006) Targeting gene-virotherapy of cancer. Cell Res 16: 25-30.
    • (2006) Cell Res , vol.16 , pp. 25-30
    • Liu, X.Y.1    Gu, J.F.2
  • 16
    • 33845932083 scopus 로고    scopus 로고
    • S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis
    • Azad N, Vallyathan V, Wang L, Tantishaiyakul V, Stehlik C, et al. (2006) S-nitrosylation of Bcl-2 inhibits its ubiquitin-proteasomal degradation. A novel antiapoptotic mechanism that suppresses apoptosis. J Biol Chem 281: 34124-34134.
    • (2006) J Biol Chem , vol.281 , pp. 34124-34134
    • Azad, N.1    Vallyathan, V.2    Wang, L.3    Tantishaiyakul, V.4    Stehlik, C.5
  • 17
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • Cory S, Adams JM, (2002) The Bcl2 family: regulators of the cellular life-or-death switch. Nat Rev Cancer 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 18
    • 0033974063 scopus 로고    scopus 로고
    • Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway
    • Breitschopf K, Haendeler J, Malchow P, Zeiher AM, Dimmeler S, (2000) Posttranslational modification of Bcl-2 facilitates its proteasome-dependent degradation: molecular characterization of the involved signaling pathway. Mol Cell Biol 20: 1886-1896.
    • (2000) Mol Cell Biol , vol.20 , pp. 1886-1896
    • Breitschopf, K.1    Haendeler, J.2    Malchow, P.3    Zeiher, A.M.4    Dimmeler, S.5
  • 19
    • 1442359881 scopus 로고    scopus 로고
    • Bcl-2 family members: integrators of survival and death signals in physiology and pathology
    • Schinzel A, Kaufmann T, Borner C, (2004) Bcl-2 family members: integrators of survival and death signals in physiology and pathology. Biochim Biophys Acta 1644 (2-3): 95-105.
    • (2004) Biochim Biophys Acta , vol.1644 , Issue.2-3 , pp. 95-105
    • Schinzel, A.1    Kaufmann, T.2    Borner, C.3
  • 20
    • 42049103183 scopus 로고    scopus 로고
    • Regulation of Bcl-2 family proteins by posttranslational modifications
    • Kutuk O, Letai A, (2008) Regulation of Bcl-2 family proteins by posttranslational modifications. Curr Mol Med 8 (2): 102-18.
    • (2008) Curr Mol Med , vol.8 , Issue.2 , pp. 102-118
    • Kutuk, O.1    Letai, A.2
  • 21
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC, (2001) Nitrosylation. the prototypic redox-based signaling mechanism. Cell 106: 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 22
    • 0028349156 scopus 로고
    • Nitric oxide synthases in mammals
    • Knowles RG, Moncada S, (1994) Nitric oxide synthases in mammals. Biochem J 298: 249-258.
    • (1994) Biochem J , vol.298 , pp. 249-258
    • Knowles, R.G.1    Moncada, S.2
  • 23
    • 77951627581 scopus 로고    scopus 로고
    • Nitric oxide-mediated bcl-2 stabilization potentiates malignant transformation of human lung epithelial cells
    • Azad N, Iyer AK, Wang L, Lu Y, Medan D, et al. (2010) Nitric oxide-mediated bcl-2 stabilization potentiates malignant transformation of human lung epithelial cells. Am J Respir Cell Mol Biol 42: 578-585.
    • (2010) Am J Respir Cell Mol Biol , vol.42 , pp. 578-585
    • Azad, N.1    Iyer, A.K.2    Wang, L.3    Lu, Y.4    Medan, D.5
  • 24
    • 0034485823 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase and nitrotyrosine in human metastatic melanoma tumors correlate with poor survival
    • Ekmekcioglu S, Ellerhorst J, Smid CM, Prieto VG, Munsell M, et al. (2000) Inducible nitric oxide synthase and nitrotyrosine in human metastatic melanoma tumors correlate with poor survival. Clin Cancer Res 6: 4768-4775.
    • (2000) Clin Cancer Res , vol.6 , pp. 4768-4775
    • Ekmekcioglu, S.1    Ellerhorst, J.2    Smid, C.M.3    Prieto, V.G.4    Munsell, M.5
  • 25
    • 0141576591 scopus 로고    scopus 로고
    • Negative association of melanoma differentiation-associated gene (MDA-7) and inducible nitric oxide synthase (iNOS) in human melanoma: MDA-7 regulates iNOS expression in melanoma cells
    • Ekmekcioglu S, Ellerhorst JA, Mumm JB, Zheng M, Broemeling L, et al. (2003) Negative association of melanoma differentiation-associated gene (MDA-7) and inducible nitric oxide synthase (iNOS) in human melanoma: MDA-7 regulates iNOS expression in melanoma cells. Mol Cancer Ther 2: 9-17.
    • (2003) Mol Cancer Ther , vol.2 , pp. 9-17
    • Ekmekcioglu, S.1    Ellerhorst, J.A.2    Mumm, J.B.3    Zheng, M.4    Broemeling, L.5
  • 27
    • 33745685863 scopus 로고    scopus 로고
    • Nitric oxide regulates cell sensitivity to cisplatin-induced apoptosis through S-nitrosylation and inhibition of Bcl-2 ubiquitination
    • Chanvorachote P, Nimmannit U, Stehlik C, Wang L, Jiang BH, et al. (2006) Nitric oxide regulates cell sensitivity to cisplatin-induced apoptosis through S-nitrosylation and inhibition of Bcl-2 ubiquitination. Cancer Res 66: 6353-6360.
    • (2006) Cancer Res , vol.66 , pp. 6353-6360
    • Chanvorachote, P.1    Nimmannit, U.2    Stehlik, C.3    Wang, L.4    Jiang, B.H.5
  • 28
    • 0032473496 scopus 로고    scopus 로고
    • Alphaviruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivation of Bcl-2
    • Grandgirard D, Studer E, Monney L, Belser T, Fellay I, et al. (1998) Alphaviruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivation of Bcl-2. EMBO J 17: 1268-1278.
    • (1998) EMBO J , vol.17 , pp. 1268-1278
    • Grandgirard, D.1    Studer, E.2    Monney, L.3    Belser, T.4    Fellay, I.5
  • 29
    • 0345732497 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-x(L) differentially protect human prostate cancer cells from induction of apoptosis by melanoma differentiation associated gene-7, MDA-7/IL-24
    • Lebedeva IV, Sarkar D, Su ZZ, Kitada S, Dent P, et al. (2003) Bcl-2 and Bcl-x(L) differentially protect human prostate cancer cells from induction of apoptosis by melanoma differentiation associated gene-7, MDA-7/IL-24. Oncogene 22: 8758-8773.
    • (2003) Oncogene , vol.22 , pp. 8758-8773
    • Lebedeva, I.V.1    Sarkar, D.2    Su, Z.Z.3    Kitada, S.4    Dent, P.5
  • 30
    • 45449104968 scopus 로고    scopus 로고
    • Killing of human melanoma cells induced by activation of class I interferon-regulated signaling pathways via MDA-7/IL-24
    • Ekmekcioglu S, Mumm JB, Udtha M, Chada S, Grimm EA, (2008) Killing of human melanoma cells induced by activation of class I interferon-regulated signaling pathways via MDA-7/IL-24. Cytokine 43 (1): 34-44.
    • (2008) Cytokine , vol.43 , Issue.1 , pp. 34-44
    • Ekmekcioglu, S.1    Mumm, J.B.2    Udtha, M.3    Chada, S.4    Grimm, E.A.5
  • 31
    • 0036939057 scopus 로고    scopus 로고
    • Nitrosylation: the next phosphorylation?
    • Mannick JB, Schonhoff CM, (2002) Nitrosylation: the next phosphorylation? Arch Biochem Biophys 408 (1): 1-6.
    • (2002) Arch Biochem Biophys , vol.408 , Issue.1 , pp. 1-6
    • Mannick, J.B.1    Schonhoff, C.M.2
  • 32
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: enzymatic mechanisms and cellular functions
    • Benhar M, Forrester MT, Stamler JS, (2009) Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat Rev Mol Cell Biol 10: 721-732.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 33
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar M, Forrester MT, Hess DT, Stamler JS, (2008) Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 320: 1050-1054.
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 34
    • 34347268109 scopus 로고    scopus 로고
    • Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress
    • Forrester MT, Foster MW, Stamler JS, (2007) Assessment and application of the biotin switch technique for examining protein S-nitrosylation under conditions of pharmacologically induced oxidative stress. J Biol Chem 282: 13977-13983.
    • (2007) J Biol Chem , vol.282 , pp. 13977-13983
    • Forrester, M.T.1    Foster, M.W.2    Stamler, J.S.3
  • 36
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B by S-nitrosylation
    • Marshall HE, Stamler JS, (2001) Inhibition of NF-kappa B by S-nitrosylation. Biochemistry 40: 1688-1693.
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 37
    • 0035798544 scopus 로고    scopus 로고
    • TNFalpha and oxLDL reduce protein S-nitrosylation in endothelial cells
    • Hoffmann J, Haendeler J, Zeiher AM, Dimmeler S, (2001) TNFalpha and oxLDL reduce protein S-nitrosylation in endothelial cells. J Biol Chem 276: 41383-41387.
    • (2001) J Biol Chem , vol.276 , pp. 41383-41387
    • Hoffmann, J.1    Haendeler, J.2    Zeiher, A.M.3    Dimmeler, S.4
  • 38
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, et al. (2004) S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304: 1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5
  • 39
    • 14844300857 scopus 로고    scopus 로고
    • S-nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance
    • Yasukawa T, Tokunaga E, Ota H, Sugita H, Martyn JA, et al. (2005) S-nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance. J Biol Chem 280: 7511-7518.
    • (2005) J Biol Chem , vol.280 , pp. 7511-7518
    • Yasukawa, T.1    Tokunaga, E.2    Ota, H.3    Sugita, H.4    Martyn, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.