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Volumn 93, Issue 5, 2011, Pages 941-947

Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom

Author keywords

Cell cycle; L amino acid oxidase; Parasiticidal and bactericidal effects

Indexed keywords

AMINO ACID OXIDASE; BATROXLAAO; BATROXOBIN; FLUORESCENT DYE; HYDROGEN PEROXIDE; UNCLASSIFIED DRUG;

EID: 79953885089     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.01.009     Document Type: Article
Times cited : (53)

References (48)
  • 1
    • 0014216389 scopus 로고
    • On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase
    • V. Massey, B. Curti, On the reaction mechanism of Crotalus adamanteus L-amino acid oxidase, J. Biol. Chem. 242 (1967) 1259-1264.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1259-1264
    • Massey, V.1    Curti, B.2
  • 3
    • 33646113547 scopus 로고    scopus 로고
    • L-amino acid oxidases and lactate dehydrogenase
    • G.S. Bailey (Ed.) Alaken Inc, Fort Collins, C.O
    • N.H. Tan, L-amino acid oxidases and lactate dehydrogenase. in: G.S. Bailey (Ed.), Enzynmes from Snake Venom. Alaken Inc, Fort Collins, C.O, 1998, pp. 579-598.
    • (1998) Enzynmes from Snake Venom , pp. 579-598
    • Tan, N.H.1
  • 4
    • 0037145809 scopus 로고    scopus 로고
    • Antimicrobial action of achacin is mediated by L-amino acid oxidase activity
    • DOI 10.1016/S0014-5793(02)03608-6, PII S0014579302036086
    • T. Ehara, S. Kitajima, N. Kanzawa, T. Tamiya, T. Tsuchiya, Antimicrobial action of achacin is mediated by L-amino acid oxidase activity, FEBS Lett. 531 (2002) 509-512. (Pubitemid 35336077)
    • (2002) FEBS Letters , vol.531 , Issue.3 , pp. 509-512
    • Ehara, T.1    Kitajima, S.2    Kanzawa, N.3    Tamiya, T.4    Tsuchiya, T.5
  • 5
    • 24344500872 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of APIT, a new L-amino acid oxidase from Aplysia punctata
    • D. Butzke, R. Hurwitz, B. Thiede, S. Goedert, T. Rudel, Cloning and biochemical characterization of APIT, a new L-amino acid oxidase from Aplysia punctata, Toxicon 46 (2005) 479-489.
    • (2005) Toxicon , vol.46 , pp. 479-489
    • Butzke, D.1    Hurwitz, R.2    Thiede, B.3    Goedert, S.4    Rudel, T.5
  • 6
    • 0036234815 scopus 로고    scopus 로고
    • Snake venom L-amino acid oxidases
    • DOI 10.1016/S0041-0101(02)00102-2, PII S0041010102001022
    • X.Y. Du, K.J. Clemetson, Snake venom L-amino acid oxidases, Toxicon 40 (2002) 659-665. (Pubitemid 34439228)
    • (2002) Toxicon , vol.40 , Issue.6 , pp. 659-665
    • Du, X.-Y.1    Clemetson, K.J.2
  • 9
    • 0030570468 scopus 로고    scopus 로고
    • Identification of the snake venom substance that induces apoptosis
    • S.M. Suhr, D.S. Kim, Identification of the snake venom substance that induces apoptosis, Biochem. Biophys. Res. Commun. 224 (1996) 134-139.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 134-139
    • Suhr, S.M.1    Kim, D.S.2
  • 10
    • 0030910602 scopus 로고    scopus 로고
    • Apoxin I, a novel apoptosis-inducing factor with Lamino acid oxidase activity purified from Western diamondback rattlesnake venom
    • S. Torii, M. Naito, T. Tsuruo, Apoxin I, a novel apoptosis-inducing factor with Lamino acid oxidase activity purified from Western diamondback rattlesnake venom, J. Biol. Chem. 272 (1997) 9539-9542.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9539-9542
    • Torii, S.1    Naito, M.2    Tsuruo, T.3
  • 11
    • 0034724181 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of apoxin I, a snake venom-derived apoptosis-inducing factor with L-amino acid oxidase activity
    • S. Torii, K. Yamane, T. Mashima, N. Haga, K. Yamamoto, J.W. Fox, M. Naito, T. Tsuruo, Molecular cloning and functional analysis of apoxin I, a snake venom-derived apoptosis-inducing factor with L-amino acid oxidase activity, Biochemistry 39 (2000) 3197-3205.
    • (2000) Biochemistry , vol.39 , pp. 3197-3205
    • Torii, S.1    Yamane, K.2    Mashima, T.3    Haga, N.4    Yamamoto, K.5    Fox, J.W.6    Naito, M.7    Tsuruo, T.8
  • 13
    • 0028045984 scopus 로고
    • Purification and characterization of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation
    • Z.Y. Li, T.F. Yu, E.C. Lian, Purification and characterization of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation, Toxicon 32 (1994) 1348-1358.
    • (1994) Toxicon , vol.32 , pp. 1348-1358
    • Li, Z.Y.1    Yu, T.F.2    Lian, E.C.3
  • 14
    • 0036910432 scopus 로고    scopus 로고
    • L-amino acid oxidase from Trimeresurus jerdonii snake venom: Purification, characterization, platelet aggregation-inducing and antibacterial effects
    • Q.M. Lu, Q. Wei, Y. Jin, J.F. Wei, W.Y. Wang, Y.L. Xiong, L-amino acid oxidase from Trimeresurus jerdonii snake venom: purification, characterization, platelet aggregation-inducing and antibacterial effects, J. Nat. Toxins 11 (2002) 345-352. (Pubitemid 36029240)
    • (2002) Journal of Natural Toxins , vol.11 , Issue.4 , pp. 345-352
    • Lu, Q.-M.1    Wei, Q.2    Jin, Y.3    Wei, J.-F.4    Wang, W.-Y.5    Xiong, Y.-L.6
  • 17
    • 0033567358 scopus 로고    scopus 로고
    • Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: Preliminary crystallographic data
    • DOI 10.1006/abbi.1999.1287
    • D.H. Souza, L.M. Eugenio, J.E. Fletcher, M.S. Jiang, R.C. Garratt, G. Oliva, H.S. Selistre-de-Araujo, Isolation and structural characterization of a cytotoxic L-amino acid oxidase from Agkistrodon contortrix laticinctus snake venom: preliminary crystallographic data, Arch. Biochem. Biophys. 368 (1999) 285-290. (Pubitemid 29406553)
    • (1999) Archives of Biochemistry and Biophysics , vol.368 , Issue.2 , pp. 285-290
    • Souza, D.H.F.1    Eugenio, L.M.2    Fletcher, J.E.3    Jiang, M.-S.4    Garratt, R.C.5    Oliva, G.6    Selistre-de-Araujo, H.S.7
  • 18
    • 77649187050 scopus 로고    scopus 로고
    • Biochemical, functional and structural characterization of Akbu-LAAO: A novel snake venom Lamino acid oxidase from Agkistrodon blomhoffii ussurensis
    • M.Z. Sun, C. Guo, Y. Tian, D. Chen, F.T. Greenaway, S. Liu, Biochemical, functional and structural characterization of Akbu-LAAO: a novel snake venom Lamino acid oxidase from Agkistrodon blomhoffii ussurensis, Biochimie 92 (2010) 343-349.
    • (2010) Biochimie , vol.92 , pp. 343-349
    • Sun, M.Z.1    Guo, C.2    Tian, Y.3    Chen, D.4    Greenaway, F.T.5    Liu, S.6
  • 20
    • 68949161833 scopus 로고    scopus 로고
    • Purification and characterization of a new L-amino acid oxidase from Daboia russellii siamensis venom
    • S.R. Zhong, Y. Jin, J.B. Wu, Y.H. Jia, G.L. Xu, G.C. Wang, Y.L. Xiong, Q.M. Lu, Purification and characterization of a new L-amino acid oxidase from Daboia russellii siamensis venom, Toxicon 54 (2009) 763-771.
    • (2009) Toxicon , vol.54 , pp. 763-771
    • Zhong, S.R.1    Jin, Y.2    Wu, J.B.3    Jia, Y.H.4    Xu, G.L.5    Wang, G.C.6    Xiong, Y.L.7    Lu, Q.M.8
  • 21
    • 74549185818 scopus 로고    scopus 로고
    • Novel L-amino acid oxidase with antibacterial activity against methicillin-resistant Staphylococcus aureus isolated from epidermal mucus of the flounder Platichthys stellatus
    • K. Kasai, T. Ishikawa, T. Komata, K. Fukuchi, M. Chiba, H. Nozaka, T. Nakamura, T. Sato, T. Miura, Novel L-amino acid oxidase with antibacterial activity against methicillin-resistant Staphylococcus aureus isolated from epidermal mucus of the flounder Platichthys stellatus, FEBS J. 277 (2010) 453-\465.
    • (2010) FEBS J. , vol.277
    • Kasai, K.1    Ishikawa, T.2    Komata, T.3    Fukuchi, K.4    Chiba, M.5    Nozaka, H.6    Nakamura, T.7    Sato, T.8    Miura, T.9
  • 23
  • 24
    • 41149094512 scopus 로고    scopus 로고
    • Regulation of DNA repair throughout the cell cycle
    • DOI 10.1038/nrm2351, PII NRM2351
    • D. Branzei, M. Foiani, Regulation of DNA repair throughout the cell cycle, Nat. Rev. Mol. Cell. Biol. 9 (2008) 297-308. (Pubitemid 351430844)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.4 , pp. 297-308
    • Branzei, D.1    Foiani, M.2
  • 25
    • 79953854502 scopus 로고    scopus 로고
    • Development of in vitro susceptibility testing and quality control parameters. Approved Guideline
    • NCCLS National Committee for Clinical Laboratory Standards second ed. Wayne, Pa
    • NCCLS (2001), In National Committee for Clinical Laboratory Standards. Development of in vitro susceptibility testing and quality control parameters. Approved Guideline, second ed. NCCLS document M23-A2, Wayne, Pa.
    • (2001) NCCLS Document M23-A2
  • 26
    • 0035992072 scopus 로고    scopus 로고
    • Resazurin microtiter assay plate: Simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis
    • DOI 10.1128/AAC.46.8.2720-2722.2002
    • J.C. Palomino, A. Martin, M. Camacho, H. Guerra, J. Swings, F. Portaels, Resazurin microtiter assay plate: simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis, Antimicrobial Agents Chemother. 46 (2002) 2720-2722. (Pubitemid 34793497)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.8 , pp. 2720-2722
    • Palomino, J.-C.1    Martin, A.2    Camacho, M.3    Guerra, H.4    Swings, J.5    Portaels, F.6
  • 29
    • 0033661713 scopus 로고    scopus 로고
    • Setting of a colorimetric method to determine the viability of Trypanosoma cruzi epimastigotes
    • S. Muelas-Serrano, J.J. Nogal-Ruiz, A. Gómez-Barrio, Setting of a colorimetric method to determine the viability of Trypanosoma cruzi epimastigotes, Parasitol. Res. 86 (2000) 999-1002.
    • (2000) Parasitol. Res. , vol.86 , pp. 999-1002
    • Muelas-Serrano, S.1    Nogal-Ruiz, J.J.2    Gómez-Barrio, A.3
  • 30
    • 0004419163 scopus 로고    scopus 로고
    • Apoptotic and necrotic cell death are both induced by electroporation in HL60 human promyeloid leukaemia cells
    • J. Piñero, M. López-Baena, T. Ortis, F. Cortés, Apoptotic and necrotic cell death are both induced by electroporation in HL60 human promyeloid leukaemia cells, Apoptosis 2 (1997) 330-336.
    • (1997) Apoptosis , vol.2 , pp. 330-336
    • Piñero, J.1    López-Baena, M.2    Ortis, T.3    Cortés, F.4
  • 32
    • 33845918428 scopus 로고    scopus 로고
    • Molecular cloning, expression and purification of l-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma
    • DOI 10.1016/j.pep.2006.09.016, PII S1046592806003068
    • P.R. Kommuju, P. Macheroux, S. Ghisla, Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma, Protein Exp. Purif. 52 (2007) 89-95. (Pubitemid 46038758)
    • (2007) Protein Expression and Purification , vol.52 , Issue.1 , pp. 89-95
    • Kommoju, P.R.1    Macheroux, P.2    Ghisla, S.3
  • 33
    • 0025784241 scopus 로고
    • Antibacterial effects of different snake venoms: Purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom
    • B.G. Stiles, F.W. Sexton, S.A. Weinstein, Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom, Toxicon 29 (1991) 1129-1141.
    • (1991) Toxicon , vol.29 , pp. 1129-1141
    • Stiles, B.G.1    Sexton, F.W.2    Weinstein, S.A.3
  • 34
    • 0033033686 scopus 로고    scopus 로고
    • Comparison of the apoptotic pathways induced by Lamino acid oxidase and hydrogen peroxide
    • S.M. Suhr, D.S. Kim, Comparison of the apoptotic pathways induced by Lamino acid oxidase and hydrogen peroxide, J. Biochem. 125 (1999) 305-309.
    • (1999) J. Biochem. , vol.125 , pp. 305-309
    • Suhr, S.M.1    Kim, D.S.2
  • 35
    • 79953885227 scopus 로고    scopus 로고
    • Anticancer effect of Lycium barbarum polysaccharides on colon cancer cells involves G0/G1 phase arrest
    • PMID: 20066520
    • F. Mao, B. Xiao, Z. Jiang, J. Zhao, X. Huang, J. Guo, Anticancer effect of Lycium barbarum polysaccharides on colon cancer cells involves G0/G1 phase arrest, Med. Oncol. (2010) PMID: 20066520.
    • (2010) Med. Oncol.
    • Mao, F.1    Xiao, B.2    Jiang, Z.3    Zhao, J.4    Huang, X.5    Guo, J.6
  • 36
    • 0030458544 scopus 로고    scopus 로고
    • Antioxidant defense in parasitic protozoa
    • R.K. Mehlotra, Antioxidant defense in parasitic protozoa, Crit. Rev. Microbiol. 22 (1996) 295-314.
    • (1996) Crit. Rev. Microbiol. , vol.22 , pp. 295-314
    • Mehlotra, R.K.1
  • 39
    • 42449138183 scopus 로고    scopus 로고
    • Isolation and characterization of ACTX-6: A cytotoxic L-amino acid oxidase from Agkistrodon acutus snake venom
    • DOI 10.1080/14786410701592679, PII 792204380
    • L. Zhang, W.T. Wu, Isolation and characterization of ACTX-6: a cytotoxic Lamino acid oxidase from Agkistrodon acutus snake venom, Nat. Prod. Res. 22 (2008) 554-563. (Pubitemid 351560237)
    • (2008) Natural Product Research , vol.22 , Issue.6 , pp. 554-563
    • Zhang, L.1    Wu, W.T.2
  • 40
    • 0034671997 scopus 로고    scopus 로고
    • Isolation, structural and a functional characterization of an apoptosis inducing L-amino acid oxidase from Leaf-nosed viper (Eristocophis macmahoni) snake venom
    • S.A. Ali, S. Stoeva, A. Abbase, J.M. Alan, R. Kayed, M. Faigle, B. Neumeister, W. Voelter, Isolation, structural and a functional characterization of an apoptosis inducing L-amino acid oxidase from Leaf-nosed viper (Eristocophis macmahoni) snake venom, Arch. Biochem. Biophys. 384 (2000) 216-226.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 216-226
    • Ali, S.A.1    Stoeva, S.2    Abbase, A.3    Alan, J.M.4    Kayed, R.5    Faigle, M.6    Neumeister, B.7    Voelter, W.8
  • 41
    • 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
    • DOI 10.1016/0014-5793(96)00989-1, PII S0014579396009891
    • V.P. Skulachev, Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell, FEBS Lett. 397 (1996) 7-10. (Pubitemid 26380163)
    • (1996) FEBS Letters , vol.397 , Issue.1 , pp. 7-10
    • Skulachev, V.P.1
  • 42
    • 0037174142 scopus 로고    scopus 로고
    • Programmed death in yeast as adaptation?
    • V.P. Skulachev, Programmed death in yeast as adaptation? FEBS Lett. 528 (2000) 23-26.
    • (2000) FEBS Lett. , vol.528 , pp. 23-26
    • Skulachev, V.P.1
  • 43
    • 67649404608 scopus 로고    scopus 로고
    • Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom
    • J.F. Wei, H.W. Yang, X.L. Wei, L.Y. Qiao, W.Y. Wang, S.H. He, Purification, characterization and biological activities of the L-amino acid oxidase from Bungarus fasciatus snake venom, Toxicon 54 (2009) 262-271.
    • (2009) Toxicon , vol.54 , pp. 262-271
    • Wei, J.F.1    Yang, H.W.2    Wei, X.L.3    Qiao, L.Y.4    Wang, W.Y.5    He, S.H.6
  • 44
    • 33646110520 scopus 로고    scopus 로고
    • Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom
    • M. Samel, H. Vija, G. Rönnholm, J. Siigur, N. Kalkkinen, E. Siigur, Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom, Biochim. Biophys. Acta 1764 (2006) 707-714.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 707-714
    • Samel, M.1    Vija, H.2    Rönnholm, G.3    Siigur, J.4    Kalkkinen, N.5    Siigur, E.6
  • 45
    • 33748275681 scopus 로고    scopus 로고
    • The p53 tumor suppressor participates in multiple cell cycle checkpoints
    • L.E. Giono, J.J. Manfredi, The p53 tumor suppressor participates in multiple cell cycle checkpoints, J. Cell. Physiol. 209 (2006) 13-20.
    • (2006) J. Cell. Physiol. , vol.209 , pp. 13-20
    • Giono, L.E.1    Manfredi, J.J.2
  • 46
    • 0028171292 scopus 로고
    • G1 phase progression: Cycling on cue
    • DOI 10.1016/0092-8674(94)90540-1
    • C.J. Sherr, G1 phase progression: cycling on cue, Cell 79 (1994) 551-555. (Pubitemid 24363798)
    • (1994) Cell , vol.79 , Issue.4 , pp. 551-555
    • Sherr, C.J.1
  • 47
    • 72449125362 scopus 로고    scopus 로고
    • Apoptosis induction in human leukemic cells by a novel protein Bengalin, isolated from Indian black scorpion venom: Through mitochondrial pathway and inhibition of heat shock proteins
    • S.D. Gupta, A. Gomes, A. Debnath, A. Saha, A. Gomes, Apoptosis induction in human leukemic cells by a novel protein Bengalin, isolated from Indian black scorpion venom: through mitochondrial pathway and inhibition of heat shock proteins, Chem. Biol. Interact. 183 (2010) 293-303.
    • (2010) Chem. Biol. Interact. , vol.183 , pp. 293-303
    • Gupta, S.D.1    Gomes, A.2    Debnath, A.3    Saha, A.4    Gomes, A.5
  • 48
    • 67349191484 scopus 로고    scopus 로고
    • Apoptosis of human hepatocellular carcinoma cell (HepG2) induced by cardiotoxin III through S-phase arrest
    • X. Chen, P. Lv, J. Liu, K. Xu, Apoptosis of human hepatocellular carcinoma cell (HepG2) induced by cardiotoxin III through S-phase arrest, Exp. Toxicol. Pathol. 61 (2009) 307-315.
    • (2009) Exp. Toxicol. Pathol. , vol.61 , pp. 307-315
    • Chen, X.1    Lv, P.2    Liu, J.3    Xu, K.4


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