메뉴 건너뛰기




Volumn 80, Issue 13, 2007, Pages 1189-1197

ACTX-8, a cytotoxic l-amino acid oxidase isolated from Agkistrodon acutus snake venom, induces apoptosis in Hela cervical cancer cells

Author keywords

ACTX 8; Apoptosis; Bcl 2 family; Cytotoxin; l amino acid oxidase (LAO); Mitochondria

Indexed keywords

ACTX 8; ALANYLASPARTYLASPARTYLARGINYLASPARAGINYLPROLYLLEUCYL GLUTAMYLGLUTAMYLPHENYLALANYLARGINYLGLUTAMYLASPARAGINYL ASPARAGINYLTYROSYLGLUTAMYLGLUTAMYLPHENYLALANYLLEUCINE; ANTINEOPLASTIC AGENT; CASPASE; CASPASE INHIBITOR; CYTOCHROME C; DNA FRAGMENT; PHOSPHATIDYLSERINE; PROTEIN; PROTEIN BAD; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 33847299416     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2006.12.024     Document Type: Article
Times cited : (61)

References (39)
  • 1
    • 0034671997 scopus 로고    scopus 로고
    • Isolation, structural, and functional characterization of an apoptosis-inducing l-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom
    • Ali S.A., Stoeva S., Abbasi A., Alam J.M., Kaved R., Faigle M., Neumeister B., and Voelter W. Isolation, structural, and functional characterization of an apoptosis-inducing l-amino acid oxidase from leaf-nosed viper (Eristocophis macmahoni) snake venom. Archives of Biochemistry and Biophysics 384 2 (2000) 216-226
    • (2000) Archives of Biochemistry and Biophysics , vol.384 , Issue.2 , pp. 216-226
    • Ali, S.A.1    Stoeva, S.2    Abbasi, A.3    Alam, J.M.4    Kaved, R.5    Faigle, M.6    Neumeister, B.7    Voelter, W.8
  • 2
    • 33745812087 scopus 로고    scopus 로고
    • Mechanism of cell death induction by l-amino acid oxidase, a major component of ophidian venom
    • Ander S.R., Kommoju P.R., Draxl S., Murkovic M., Macheroux P., Ghisla S., and Ferrando-Mav E. Mechanism of cell death induction by l-amino acid oxidase, a major component of ophidian venom. Apoptosis 11 8 (2006) 1439-1451
    • (2006) Apoptosis , vol.11 , Issue.8 , pp. 1439-1451
    • Ander, S.R.1    Kommoju, P.R.2    Draxl, S.3    Murkovic, M.4    Macheroux, P.5    Ghisla, S.6    Ferrando-Mav, E.7
  • 3
    • 0034811108 scopus 로고    scopus 로고
    • Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis
    • Bae J., Hsu S.Y., Leo C.P., Zell K., and Hsueh A.J. Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis. Apoptosis 6 5 (2001) 319-330
    • (2001) Apoptosis , vol.6 , Issue.5 , pp. 319-330
    • Bae, J.1    Hsu, S.Y.2    Leo, C.P.3    Zell, K.4    Hsueh, A.J.5
  • 5
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • Cory S., and Adams J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nature Reviews. Cancer 2 9 (2002) 647-656
    • (2002) Nature Reviews. Cancer , vol.2 , Issue.9 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 7
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 2 (2004) 205-219
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 9
    • 3442898222 scopus 로고    scopus 로고
    • Apoptosis via the B cell antigen receptor requires Bax translocation and involves mitochondrial depolarization, cytochrome c release, and caspase-9 activation
    • Eldering E., Mackus W.J., Derks I.A., Evers L.M., Beuling E., Teeling P., Lens S.M., van Oers M.H., and van Lier R.A. Apoptosis via the B cell antigen receptor requires Bax translocation and involves mitochondrial depolarization, cytochrome c release, and caspase-9 activation. European Journal of Immunology 34 7 (2004) 1950-1960
    • (2004) European Journal of Immunology , vol.34 , Issue.7 , pp. 1950-1960
    • Eldering, E.1    Mackus, W.J.2    Derks, I.A.3    Evers, L.M.4    Beuling, E.5    Teeling, P.6    Lens, S.M.7    van Oers, M.H.8    van Lier, R.A.9
  • 10
    • 0033385980 scopus 로고    scopus 로고
    • Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs
    • Fontaine E., and Bernardi P. Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs. Journal of Bioenergetics and Biomembranes 31 4 (1999) 335-345
    • (1999) Journal of Bioenergetics and Biomembranes , vol.31 , Issue.4 , pp. 335-345
    • Fontaine, E.1    Bernardi, P.2
  • 11
    • 0034669944 scopus 로고    scopus 로고
    • Deoxyadenosine analogues induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria
    • Genini D., Adachi S., Chao Q., Rose D.W., Carrera C.J., Cottam H.B., Carson D.A., and Leoni L.M. Deoxyadenosine analogues induce programmed cell death in chronic lymphocytic leukemia cells by damaging the DNA and by directly affecting the mitochondria. Blood 96 10 (2000) 3537-3543
    • (2000) Blood , vol.96 , Issue.10 , pp. 3537-3543
    • Genini, D.1    Adachi, S.2    Chao, Q.3    Rose, D.W.4    Carrera, C.J.5    Cottam, H.B.6    Carson, D.A.7    Leoni, L.M.8
  • 12
    • 0033179760 scopus 로고    scopus 로고
    • Bcl-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., and Korsmeyer S.J. Bcl-2 family members and the mitochondria in apoptosis. Genes and Development 13 15 (1999) 1899-1911
    • (1999) Genes and Development , vol.13 , Issue.15 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 13
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G., and Reed J.C. Mitochondrial control of cell death. Nature Medicine 6 5 (2000) 513-519
    • (2000) Nature Medicine , vol.6 , Issue.5 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 14
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitizer or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A., Bassik M.C., Walensky L.D., Sorcinelli M.D., Weiler S., and Korsmeyer S.J. Distinct BH3 domains either sensitizer or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cells 2 23 (2002) 183-192
    • (2002) Cancer Cells , vol.2 , Issue.23 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 16
    • 0030916417 scopus 로고    scopus 로고
    • DEF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X., Zou H., Slaughter C., and Wang X. DEF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89 2 (1997) 175-184
    • (1997) Cell , vol.89 , Issue.2 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 20
    • 0033198217 scopus 로고    scopus 로고
    • BAX translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, BCL-2, and caspases
    • Putcha G.V., Deshmukh M., and Johoson Jr. E.M. BAX translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, BCL-2, and caspases. Journal of Neuroscience 19 17 (1999) 7476-7485
    • (1999) Journal of Neuroscience , vol.19 , Issue.17 , pp. 7476-7485
    • Putcha, G.V.1    Deshmukh, M.2    Johoson Jr., E.M.3
  • 21
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H., Enari M., and Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391 6662 (1998) 96-99
    • (1998) Nature , vol.391 , Issue.6662 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 22
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S., Narita M., and Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 6735 (1999) 483-487
    • (1999) Nature , vol.399 , Issue.6735 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 23
    • 0030580287 scopus 로고    scopus 로고
    • Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell
    • Skulachev V.P. Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Letters 397 1 (1996) 7-10
    • (1996) FEBS Letters , vol.397 , Issue.1 , pp. 7-10
    • Skulachev, V.P.1
  • 24
  • 26
    • 0037376232 scopus 로고    scopus 로고
    • Apoptotic effect in the glioma cells induced by specific protein extracted from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to oxidative stress
    • Sun L.K., Yoshii Y., Hyodo A., Tsurushima H., Saito A., Harakuni T., Li Y.P., Kariya K., Nozaki M., and Morine N. Apoptotic effect in the glioma cells induced by specific protein extracted from Okinawa Habu (Trimeresurus flavoviridis) venom in relation to oxidative stress. Toxicology In Vitro 17 2 (2003) 169-177
    • (2003) Toxicology In Vitro , vol.17 , Issue.2 , pp. 169-177
    • Sun, L.K.1    Yoshii, Y.2    Hyodo, A.3    Tsurushima, H.4    Saito, A.5    Harakuni, T.6    Li, Y.P.7    Kariya, K.8    Nozaki, M.9    Morine, N.10
  • 30
    • 0030865679 scopus 로고    scopus 로고
    • The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-alpha receptors
    • Uddin S., Fish E.N., Sher D., Gardziola C., Colamonici O.R., Kellum M., Pitha P.M., White M.F., and Platanias L.C. The IRS-pathway operates distinctively from the Stat-pathway in hematopoietic cells and transduces common and distinct signals during engagement of the insulin or interferon-alpha receptors. Blood 90 7 (1997) 2574-2582
    • (1997) Blood , vol.90 , Issue.7 , pp. 2574-2582
    • Uddin, S.1    Fish, E.N.2    Sher, D.3    Gardziola, C.4    Colamonici, O.R.5    Kellum, M.6    Pitha, P.M.7    White, M.F.8    Platanias, L.C.9
  • 33
    • 0036053357 scopus 로고    scopus 로고
    • An anti-GD2 monoclonal antibody enhances apoptotic effectors of anticancer drugs against small cell lung cancer cells via JNK (c-Jun terminal kinase) activation
    • Yoshida S., Kawaguchi H., Sato S., Ueda R., and Furukawa K. An anti-GD2 monoclonal antibody enhances apoptotic effectors of anticancer drugs against small cell lung cancer cells via JNK (c-Jun terminal kinase) activation. Japanese Journal of Cancer Research 93 7 (2002) 816-824
    • (2002) Japanese Journal of Cancer Research , vol.93 , Issue.7 , pp. 816-824
    • Yoshida, S.1    Kawaguchi, H.2    Sato, S.3    Ueda, R.4    Furukawa, K.5
  • 35
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14.3.3 not Bcl-xL
    • Zha J., Harada H., Yang E., Jockel J., and Korsmeyer S.J. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14.3.3 not Bcl-xL. Cell 87 4 (1996) 619-628
    • (1996) Cell , vol.87 , Issue.4 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 36
    • 12344308486 scopus 로고    scopus 로고
    • Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel l-amino acid oxidase with cell apoptosis-inducing activity from Agkistrodon Halys pallas venom
    • Zhang H., Teng M., Niu L., Wang Y., Wang Y., Liu Q., Huang Q., Hao Q., Dong Y., and Liu P. Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel l-amino acid oxidase with cell apoptosis-inducing activity from Agkistrodon Halys pallas venom. Acta Crystallographica. Section D, Biological Crystallography 60 5 (2004) 974-977
    • (2004) Acta Crystallographica. Section D, Biological Crystallography , vol.60 , Issue.5 , pp. 974-977
    • Zhang, H.1    Teng, M.2    Niu, L.3    Wang, Y.4    Wang, Y.5    Liu, Q.6    Huang, Q.7    Hao, Q.8    Dong, Y.9    Liu, P.10
  • 37
    • 18144425416 scopus 로고    scopus 로고
    • Purification and characterization of cytotoxins from Agkistrodon acutus venom and their anticancer activity
    • Zhang L., Li H., and Wu W.T. Purification and characterization of cytotoxins from Agkistrodon acutus venom and their anticancer activity. Journal of Chinese Pharmaceutical Sciences 13 2 (2004) 97-102
    • (2004) Journal of Chinese Pharmaceutical Sciences , vol.13 , Issue.2 , pp. 97-102
    • Zhang, L.1    Li, H.2    Wu, W.T.3
  • 38
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M., and Szabò I. The mitochondrial permeability transition. Biochimica et Biophysica Acta 1241 2 (1995) 139-176
    • (1995) Biochimica et Biophysica Acta , vol.1241 , Issue.2 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2
  • 39
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H., Li Y., Liu X., and Wang X. An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. Journal of Biological Chemistry 274 15 (1999) 11549-11556
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.