메뉴 건너뛰기




Volumn 12, Issue 10, 2012, Pages 1350-1360

A novel spider peptide toxin suppresses tumor growth through dual signaling pathways

Author keywords

Apoptosis; Cell proliferation; Gene expression; Mitochondria; P27; Signal transduction; Spider peptide toxin; Tumor suppression

Indexed keywords

CASPASE 3; CYTOCHROME C; LYCOSIN 1; PROTEIN P19; PROTEIN P21; PROTEIN P27; SPIDER VENOM; UNCLASSIFIED DRUG;

EID: 84870187949     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/156652412803833643     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 33750873334 scopus 로고    scopus 로고
    • Spider toxins activate the capsaicin receptor to produce inflammatory pain
    • Siemens J, Lukacs V, Thyagarajan B, et al. Spider toxins activate the capsaicin receptor to produce inflammatory pain. Nature 2006; 444: 208-212.
    • (2006) Nature , vol.444 , pp. 208-212
    • Siemens, J.1    Lukacs, V.2    Thyagarajan, B.3
  • 2
    • 77953271751 scopus 로고    scopus 로고
    • A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
    • Valero JG, Sancey L, Kucharczak J, et al. A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell 2010; 141: 834-845.
    • (2010) Cell , vol.141 , pp. 834-845
    • Valero, J.G.1    Sancey, L.2    Kucharczak, J.3
  • 3
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • Alabi AA, Bahamonde MI, Jung HJ, Kim JI, Swartz KJ. Portability of paddle motif function and pharmacology in voltage sensors. Nature 2007; 450: 370-375.
    • (2007) Nature , vol.450 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 4
    • 3142580385 scopus 로고    scopus 로고
    • A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom
    • Lee, SY, MacKinnon R. A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature 2004; 430: 232-235.
    • (2004) Nature , vol.430 , pp. 232-235
    • Lee, S.Y.1    Mackinnon, R.2
  • 5
    • 35648975390 scopus 로고    scopus 로고
    • Tarantula toxins interact with voltage sensors within lipid membranes
    • Milescu M, Vobecky J, Roh SH, et al. Tarantula toxins interact with voltage sensors within lipid membranes. J Gen Physiol 2007; 130: 497-511.
    • (2007) J Gen Physiol , vol.130 , pp. 497-511
    • Milescu, M.1    Vobecky, J.2    Roh, S.H.3
  • 6
    • 3142652571 scopus 로고    scopus 로고
    • Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers
    • Suchyna TM, Tape SE, Koeppe RE, et al. Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature 2004; 430: 235-240.
    • (2004) Nature , vol.430 , pp. 235-240
    • Suchyna, T.M.1    Tape, S.E.2    Koeppe, R.E.3
  • 7
    • 34547502749 scopus 로고    scopus 로고
    • A tarantula peptideagainst pain via ASIC1a channels and opioid mechanisms
    • Mazzuca M, Heurteaux C, Alloui A, et al. A tarantula peptideagainst pain via ASIC1a channels and opioid mechanisms. Nat Neurosci 2007; 10: 943-945.
    • (2007) Nat Neurosci , vol.10 , pp. 943-945
    • Mazzuca, M.1    Heurteaux, C.2    Alloui, A.3
  • 8
    • 33845351490 scopus 로고    scopus 로고
    • Molecular diversification in spider venoms: A web of combinatorial peptide libraries
    • Escoubas P. Molecular diversification in spider venoms: a web of combinatorial peptide libraries. Mol Divers 2006; 10: 545-554.
    • (2006) Mol Divers , vol.10 , pp. 545-554
    • Escoubas, P.1
  • 9
    • 0345687964 scopus 로고    scopus 로고
    • Pharmacologically active spider peptide toxins
    • Corzo G, Escoubas P. Pharmacologically active spider peptide toxins. Cell Mol Life Sci 2003; 60: 2409-2426.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2409-2426
    • Corzo, G.1    Escoubas, P.2
  • 10
    • 0031941375 scopus 로고    scopus 로고
    • Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis
    • Yan L, Adams ME. Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis. J Biol Chem 1998; 273: 2059-2066.
    • (1998) J Biol Chem , vol.273 , pp. 2059-2066
    • Yan, L.1    Adams, M.E.2
  • 11
    • 0037192798 scopus 로고    scopus 로고
    • Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae)
    • Kuhn-Nentwig L, Muller J, Schaller J, Walz A, Dathe M, Nentwig W. Cupiennin 1, a new family of highly basic antimicrobial peptides in the venom of the spider Cupiennius salei (Ctenidae). J Biol Chem 2002; 277: 11208-11216.
    • (2002) J Biol Chem , vol.277 , pp. 11208-11216
    • Kuhn-Nentwig, L.1    Muller, J.2    Schaller, J.3    Walz, A.4    Dathe, M.5    Nentwig, W.6
  • 12
    • 0037189567 scopus 로고    scopus 로고
    • Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins
    • Corzo G, Villegas E, Gómez-Lagunas F, Possani LD, Belokoneva OS, Nakajima T. Oxyopinins, large amphipathic peptides isolated from the venom of the wolf spider Oxyopes kitabensis with cytolytic properties and positive insecticidal cooperativity with spider neurotoxins. J Biol Chem 2002; 277: 23627-23637.
    • (2002) J Biol Chem , vol.277 , pp. 23627-23637
    • Corzo, G.1    Villegas, E.2    Gómez-Lagunas, F.3    Possani, L.D.4    Belokoneva, O.S.5    Nakajima, T.6
  • 13
    • 33746351784 scopus 로고    scopus 로고
    • Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity
    • Kozlov SA, Vassilevski AA, Feofanov AV, Surovoy AY, Karpunin DV, Grishin EV. Latarcins, antimicrobial and cytolytic peptides from the venom of the spider Lachesana tarabaevi (Zodariidae) that exemplify biomolecular diversity. J Biol Chem 2006; 281: 20983-20992.
    • (2006) J Biol Chem , vol.281 , pp. 20983-20992
    • Kozlov, S.A.1    Vassilevski, A.A.2    Feofanov, A.V.3    Surovoy, A.Y.4    Karpunin, D.V.5    Grishin, E.V.6
  • 14
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • Brown KL, Hancock RE. Cationic host defense (antimicrobial) peptides. Curr Opin Immunol 2006; 18: 24-30.
    • (2006) Curr Opin Immunol , vol.18 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.2
  • 15
    • 33845373254 scopus 로고    scopus 로고
    • Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumor cell membranes
    • Dennison SR, Whittaker M, Harris F, Phoenix DA. Anticancer alpha-helical peptides and structure/function relationships underpinning their interactions with tumor cell membranes. Curr Protein Pept Sci 2006; 7: 487-499.
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 487-499
    • Dennison, S.R.1    Whittaker, M.2    Harris, F.3    Phoenix, D.A.4
  • 16
    • 79951826260 scopus 로고    scopus 로고
    • Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells
    • Fadnes B, Uhlin-Hansen L, Lindin I, Rekdal Ø. Bax-derived membrane-active peptides act as potent and direct inducers of apoptosis in cancer cells. J Cell Sci 2011; 124: 556-564.
    • (2011) J Cell Sci , vol.124 , pp. 556-564
    • Fadnes, B.1    Uhlin-Hansen, L.2    Lindin, I.3    Rekdal, Ø.4
  • 17
    • 0035503496 scopus 로고    scopus 로고
    • A proapoptotic peptide for the treatment of solid tumors
    • Mai JC, Mi Z, Kim SH, Ng B, Robbins PD. A proapoptotic peptide for the treatment of solid tumors. Cancer Res 2001; 61: 7709-7712.
    • (2001) Cancer Res , vol.61 , pp. 7709-7712
    • Mai, J.C.1    Mi, Z.2    Kim, S.H.3    Ng, B.4    Robbins, P.D.5
  • 18
    • 0035940401 scopus 로고    scopus 로고
    • Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells
    • Kanovsky M, Raffo A, Drew L, et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc Natl Acad Sci USA 2001; 98: 12438-12443.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12438-12443
    • Kanovsky, M.1    Raffo, A.2    Drew, L.3
  • 19
    • 65949122547 scopus 로고    scopus 로고
    • Suppression of human solid tumor growth in mice by intratumor and systemic inoculation of histidine-rich and pH-dependent host defense- like lytic peptides
    • Arik M, Fink A, Shai Y. Suppression of human solid tumor growth in mice by intratumor and systemic inoculation of histidine-rich and pH-dependent host defense- like lytic peptides. Cancer Res 2009; 69: 3458-3463.
    • (2009) Cancer Res , vol.69 , pp. 3458-3463
    • Arik, M.1    Fink, A.2    Shai, Y.3
  • 20
    • 0032819838 scopus 로고    scopus 로고
    • Anti-cancer activity of targeted pro-apoptotic peptides
    • Ellerby HM, Arap W, Ellerby LM, et al. Anti-cancer activity of targeted pro-apoptotic peptides. Nat Med 1999; 5: 1032-1038.
    • (1999) Nat Med , vol.5 , pp. 1032-1038
    • Ellerby, H.M.1    Arap, W.2    Ellerby, L.M.3
  • 21
    • 84866550518 scopus 로고    scopus 로고
    • The PP2A-Aαgene is regulated by multiple transcriptional factors including Ets-1, SP1/SP3, and RXRα/α
    • Liu J, Ji WK, Sun SM, et al. The PP2A-Aαgene is regulated by multiple transcriptional factors including Ets-1, SP1/SP3, and RXRα/α. Curr Mol Med 2012; 12: 982-994.
    • (2012) Curr Mol Med , vol.12 , pp. 982-994
    • Liu, J.1    Ji, W.K.2    Sun, S.M.3
  • 22
    • 84866529773 scopus 로고    scopus 로고
    • The tumor suppressor p53 directly regulates c-Maf and Prox-1 to control lens differentiation
    • Liu F-Y, Tang X-C, Deng M, et al. The tumor suppressor p53 directly regulates c-Maf and Prox-1 to control lens differentiation. Curr Mol Med 2012; 12: 917-928.
    • (2012) Curr Mol Med , vol.12 , pp. 917-928
    • Liu, F.-Y.1    Tang, X.-C.2    Deng, M.3
  • 23
    • 84866526095 scopus 로고    scopus 로고
    • The p53-Bak apoptotic signaling axis plays an essential role in regulating differentiation of the ocular lens
    • Deng M, Chen P, Liu F-Y, et al. The p53-Bak apoptotic signaling axis plays an essential role in regulating differentiation of the ocular lens. Curr Mol Med 2012; 12: 901-916.
    • (2012) Curr Mol Med , vol.12 , pp. 901-916
    • Deng, M.1    Chen, P.2    Liu, F.-Y.3
  • 24
    • 84862939518 scopus 로고    scopus 로고
    • α-Crystallins interact with caspase-3 and Bax to guard mouse lens development
    • Hu W-F, Gong L, Cao Z, et al. α-Crystallins interact with caspase-3 and Bax to guard mouse lens development. Curr Mol Med 2012; 12: 177-187.
    • (2012) Curr Mol Med , vol.12 , pp. 177-187
    • Hu, W.-F.1    Gong, L.2    Cao, Z.3
  • 25
    • 33646835102 scopus 로고    scopus 로고
    • Function and solution structure of Huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena
    • Liu Z, Dai J, Dai L, et al. Function and solution structure of Huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena. J Biol Chem 2006; 281: 8628-8635.
    • (2006) J Biol Chem , vol.281 , pp. 8628-8635
    • Liu, Z.1    Dai, J.2    Dai, L.3
  • 26
    • 0001439249 scopus 로고    scopus 로고
    • Structureactivity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell- penetrating ability of buforin II
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structureactivity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell- penetrating ability of buforin II. Proc Natl Acad Sci USA 2000; 97: 8245-8250.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 27
    • 42949170340 scopus 로고    scopus 로고
    • Protein phosphatase-2A is a target of epigallocatechin-3- gallate and modulates p53-bak apoptotic pathway
    • Qin J, Chen HG, Yan Q, et al. Protein phosphatase-2A is a target of epigallocatechin-3- gallate and modulates p53-bak apoptotic pathway. Cancer Res 2008; 68: 4150-4162.
    • (2008) Cancer Res , vol.68 , pp. 4150-4162
    • Qin, J.1    Chen, H.G.2    Yan, Q.3
  • 28
    • 24344508124 scopus 로고    scopus 로고
    • Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alphaB-crystallin through inhibition of RAS activation
    • Li DW, Liu JP, Mao YW, et al. Calcium-activated RAF/MEK/ERK signaling pathway mediates p53-dependent apoptosis and is abrogated by alphaB-crystallin through inhibition of RAS activation. Mol Biol Cell 2005; 16: 4437-4453.
    • (2005) Mol Biol Cell , vol.16 , pp. 4437-4453
    • Li, D.W.1    Liu, J.P.2    Mao, Y.W.3
  • 29
    • 0035900776 scopus 로고    scopus 로고
    • Human Bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-induced apoptosis throughdown- regulation of the alphaB-crystallin gene
    • Mao YW, Xiang H, Wang J, Korsmeyer S, Reddan J, Li DW. Human Bcl-2 gene attenuates the ability of rabbit lens epithelial cells against H2O2-induced apoptosis throughdown- regulation of the alphaB-crystallin gene. J Biol Chem 2001; 276: 43435-43445.
    • (2001) J Biol Chem , vol.276 , pp. 43435-43445
    • Mao, Y.W.1    Xiang, H.2    Wang, J.3    Korsmeyer, S.4    Reddan, J.5    Li, D.W.6
  • 30
    • 77955711839 scopus 로고    scopus 로고
    • Protein phosphatase-1 regulates Akt1 signal transduction pathway to control gene expression, cell survival and differentiation
    • Xiao L, Gong L, Yuan D, et al. Protein phosphatase-1 regulates Akt1 signal transduction pathway to control gene expression, cell survival and differentiation. Cell Death Differ 2010; 17: 1448-1462.
    • (2010) Cell Death Differ , vol.17 , pp. 1448-1462
    • Xiao, L.1    Gong, L.2    Yuan, D.3
  • 31
  • 32
    • 79958213430 scopus 로고    scopus 로고
    • Knockdown of Akt1 promotes Akt2 upregulation and resistance to oxidative stress-induced apoptosis through control of multiple signaling pathways
    • Zhang L, Sun S, Zhou J, et al. Knockdown of Akt1 promotes Akt2 upregulation and resistance to oxidative stress-induced apoptosis through control of multiple signaling pathways. Antioxid Redox Signal 2011; 15: 1-17.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1-17
    • Zhang, L.1    Sun, S.2    Zhou, J.3
  • 33
    • 78650462563 scopus 로고    scopus 로고
    • Sumoylation activates the transcriptional activity of Pax-6, an important transcription factor for eye and brain development
    • Yan Q, Gong L, Deng M, et al. Sumoylation activates the transcriptional activity of Pax-6, an important transcription factor for eye and brain development. Proc Natl Acad Sci USA 2012; 107: 21034-21039.
    • (2012) Proc Natl Acad Sci USA , vol.107 , pp. 21034-21039
    • Yan, Q.1    Gong, L.2    Deng, M.3
  • 34
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev 2001; 15: 2922-2933.
    • (2001) Genes Dev , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 35
    • 28444491105 scopus 로고    scopus 로고
    • Mechanisms of apoptosis through structural biology
    • Yan N, Shi Y. Mechanisms of apoptosis through structural biology. Annu Rev Cell Dev Biol 2005; 21: 35-56.
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 35-56
    • Yan, N.1    Shi, Y.2
  • 37
    • 41149150219 scopus 로고    scopus 로고
    • The Cdk inhibitor p27 in human cancer: Prognostic potential and relevance to anticancer therapy
    • Chu IM, Hengst L, Slingerland JM. The Cdk inhibitor p27 in human cancer: prognostic potential and relevance to anticancer therapy. Nat Rev Cancer 2008; 8: 253-267.
    • (2008) Nat Rev Cancer , vol.8 , pp. 253-267
    • Chu, I.M.1    Hengst, L.2    Slingerland, J.M.3
  • 38
    • 79952075874 scopus 로고    scopus 로고
    • Spider-venom peptides as therapeutics
    • Saez NJ, Senff S, Jensen JE, et al. Spider-venom peptides as therapeutics. Toxins (Basel) 2010; 2: 2851-2871.
    • (2010) Toxins (Basel) , vol.2 , pp. 2851-2871
    • Saez, N.J.1    Senff, S.2    Jensen, J.E.3
  • 39
    • 1442349929 scopus 로고    scopus 로고
    • De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis
    • Budnik BA, Olsen JV, Egorov TA, et al. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. J Mass Spectrom 2004; 39: 193-201.
    • (2004) J Mass Spectrom , vol.39 , pp. 193-201
    • Budnik, B.A.1    Olsen, J.V.2    Egorov, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.