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Volumn 16, Issue 1, 2005, Pages 101-108

Bovine herpesvirus VP22 induces apoptosis in neuroblastoma cells by upregulating the expression ratio of Bax to Bcl-2

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; HERPESVIRUS VECTOR; PROTEIN BAX; PROTEIN BCL 2; PROTEIN VP22;

EID: 13844253349     PISSN: 10430342     EISSN: None     Source Type: Journal    
DOI: 10.1089/hum.2005.16.101     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0031566154 scopus 로고    scopus 로고
    • Possible involvement of Bcl-2 pathway in retinoid X receptor α-induced apoptosis of HL-60 cells
    • AGARWAL, N., and MEHTA, K. (1997). Possible involvement of Bcl-2 pathway in retinoid X receptor α-induced apoptosis of HL-60 cells. Biochem. Biophys. Res. Commun. 230, 251-253.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 251-253
    • Agarwal, N.1    Mehta, K.2
  • 2
    • 0032519426 scopus 로고    scopus 로고
    • Increased apoptosis of T cell subsets in aging humans: Altered expression of Fas (CD95), Fas ligand, Bcl-2. and Bax
    • AGGARWAL, S., and GUPTA, S. (1998). Increased apoptosis of T cell subsets in aging humans: Altered expression of Fas (CD95), Fas ligand, Bcl-2. and Bax. J. Immunol. 160, 1627-1637.
    • (1998) J. Immunol. , vol.160 , pp. 1627-1637
    • Aggarwal, S.1    Gupta, S.2
  • 5
    • 0001737927 scopus 로고
    • The structure and assembly of herpes viruses
    • J.R. Harris and R.W. Home, eds. (Academic Press, New York)
    • DARGAN, D. (1986). The structure and assembly of herpes viruses. In Viral Structure. J.R. Harris and R.W. Home, eds. (Academic Press, New York) pp. 359-437.
    • (1986) Viral Structure , pp. 359-437
    • Dargan, D.1
  • 6
    • 0031471203 scopus 로고    scopus 로고
    • Intercellular trafficking and protein delivery by a herpesvirus structural protein
    • ELLIOTT, G., and O'HARE, P. (1997). Intercellular trafficking and protein delivery by a herpesvirus structural protein. Cell 88, 223-233.
    • (1997) Cell , vol.88 , pp. 223-233
    • Elliott, G.1    O'Hare, P.2
  • 7
    • 0032922213 scopus 로고    scopus 로고
    • Intercellular trafficking of VP22-GFP fusion proteins
    • ELLIOTT, G., and O'HARE, P. (1999a). Intercellular trafficking of VP22-GFP fusion proteins. Gene Ther. 6, 149-151.
    • (1999) Gene Ther. , vol.6 , pp. 149-151
    • Elliott, G.1    O'Hare, P.2
  • 8
    • 0032928070 scopus 로고    scopus 로고
    • Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection
    • ELLIOTT, G., and O'HARE, P. (1999b). Live-cell analysis of a green fluorescent protein-tagged herpes simplex virus infection. J. Virol. 73, 4110-4119.
    • (1999) J. Virol. , vol.73 , pp. 4110-4119
    • Elliott, G.1    O'Hare, P.2
  • 9
    • 0035836609 scopus 로고    scopus 로고
    • Ability of the Tat basic domain and VP22 to mediate cell binding, but not membrane translocation of the diphtheria toxin A-fragment
    • FALNES, P.O., WESCHE, J., and OLSNES, S. (2001). Ability of the Tat basic domain and VP22 to mediate cell binding, but not membrane translocation of the diphtheria toxin A-fragment. Biochemistry 40, 4349-4358.
    • (2001) Biochemistry , vol.40 , pp. 4349-4358
    • Falnes, P.O.1    Wesche, J.2    Olsnes, S.3
  • 10
    • 0031786954 scopus 로고    scopus 로고
    • Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells
    • FANG, B., XU, B., KOCH, P., and ROTH, J.A. (1998). Intercellular trafficking of VP22-GFP fusion proteins is not observed in cultured mammalian cells. Gene Ther. 5, 1420-1424.
    • (1998) Gene Ther. , vol.5 , pp. 1420-1424
    • Fang, B.1    Xu, B.2    Koch, P.3    Roth, J.A.4
  • 12
    • 0016264832 scopus 로고
    • Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains
    • HEINE, J.W., HONESS, R.W., CASSAI, E., and ROIZMAN, B. (1974). Proteins specified by herpes simplex virus. XII. The virion polypeptides of type 1 strains. J. Virol. 14, 640-651.
    • (1974) J. Virol. , vol.14 , pp. 640-651
    • Heine, J.W.1    Honess, R.W.2    Cassai, E.3    Roizman, B.4
  • 13
    • 0033119372 scopus 로고    scopus 로고
    • BCL-2 gene family and the regulation of programmed cell death
    • KORSMEYER, S.J. (1999). BCL-2 gene family and the regulation of programmed cell death. Cancer Res. 59(7 Suppl.), 1693s-1700s.
    • (1999) Cancer Res. , vol.59 , Issue.7 SUPPL.
    • Korsmeyer, S.J.1
  • 15
    • 0029942344 scopus 로고    scopus 로고
    • Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles
    • LESLIE, J., RIXON, F.J., and MCLAUCHLAN, J. (1996). Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles. Virology 220, 60-68.
    • (1996) Virology , vol.220 , pp. 60-68
    • Leslie, J.1    Rixon, F.J.2    Mclauchlan, J.3
  • 16
    • 0030744392 scopus 로고    scopus 로고
    • Study of immunogenicity and virulence of bovine herpesvirus 1 mutants deficient in the UL49 homolog, UL49.5 homolog and dUTPase genes in cattle
    • LIANG, X., CHOW, B., and BABIUK, L.A. (1997). Study of immunogenicity and virulence of bovine herpesvirus 1 mutants deficient in the UL49 homolog, UL49.5 homolog and dUTPase genes in cattle. Vaccine 15, 1057-1064.
    • (1997) Vaccine , vol.15 , pp. 1057-1064
    • Liang, X.1    Chow, B.2    Babiuk, L.A.3
  • 17
    • 0035287755 scopus 로고    scopus 로고
    • VP22 enhanced intercellular trafficking of HSV thymidine kinase reduced the level of ganciclovir needed to cause suicide cell death
    • LIU, C.S., KONG, B., XIA, H.H., ELLEM, K.A., and WEI, M.Q. (2001). VP22 enhanced intercellular trafficking of HSV thymidine kinase reduced the level of ganciclovir needed to cause suicide cell death. J. Gene Med. 3, 145-152.
    • (2001) J. Gene Med. , vol.3 , pp. 145-152
    • Liu, C.S.1    Kong, B.2    Xia, H.H.3    Ellem, K.A.4    Wei, M.Q.5
  • 18
    • 0034910022 scopus 로고    scopus 로고
    • Is VP22 nuclear homing an artifact?
    • LUNDBERG, M., and JOHANSSON, M. (2001). Is VP22 nuclear homing an artifact? [Letter]. Nat. Biotechnol. 19, 713-714.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 713-714
    • Lundberg, M.1    Johansson, M.2
  • 19
    • 0035805581 scopus 로고    scopus 로고
    • Particle formation by a conserved domain of the herpes simplex virus protein VP22 facilitating protein and nucleic acid delivery
    • NORMAND, N., VAN LEEUWEN, H., and O'HARE, P. (2001). Particle formation by a conserved domain of the herpes simplex virus protein VP22 facilitating protein and nucleic acid delivery. J. Biol. Chem. 276, 15042-15050.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15042-15050
    • Normand, N.1    Van Leeuwen, H.2    O'Hare, P.3
  • 20
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • OLTVAI, Z.N., MILLIMAN, C.L., and KORSMEYER, S.J. (1993). Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74, 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 21
    • 0031953510 scopus 로고    scopus 로고
    • Intercellular delivery of functional p53 by the herpesvirus protein VP22
    • PHELAN, A., ELLIOTT, G., and O'HARE, P. (1998). Intercellular delivery of functional p53 by the herpesvirus protein VP22. Nat. Biotechnol. 16, 440-443.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 440-443
    • Phelan, A.1    Elliott, G.2    O'Hare, P.3
  • 22
    • 0032775897 scopus 로고    scopus 로고
    • Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection
    • POMERANZ, L.E., and BLAHO, J.A. (1999). Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection. J. Virol. 73, 6769-6781.
    • (1999) J. Virol. , vol.73 , pp. 6769-6781
    • Pomeranz, L.E.1    Blaho, J.A.2
  • 23
    • 0344142396 scopus 로고    scopus 로고
    • Emerging roles of caspase-3 in apoptosis
    • PORTER, A.G., and JANICKE, R.U. (1999). Emerging roles of caspase-3 in apoptosis. Cell Death Differ. 6, 99-104.
    • (1999) Cell Death Differ. , vol.6 , pp. 99-104
    • Porter, A.G.1    Janicke, R.U.2
  • 24
    • 1842484010 scopus 로고    scopus 로고
    • Bovine herpesvirus tegument protein VP22 enhances thymidine kinase/ganciclovir suicide gene therapy for neuroblastomas compared with herpes simplex virus VP22
    • QIU, Z., HARMS, J.S., ZHU, J., and SPLITTER, G.A. (2004). Bovine herpesvirus tegument protein VP22 enhances thymidine kinase/ganciclovir suicide gene therapy for neuroblastomas compared with herpes simplex virus VP22. J. Virol. 78, 4224-4233.
    • (2004) J. Virol. , vol.78 , pp. 4224-4233
    • Qiu, Z.1    Harms, J.S.2    Zhu, J.3    Splitter, G.A.4
  • 25
    • 0034872766 scopus 로고    scopus 로고
    • Bovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization
    • REN, X., HARMS, J.S., and SPLITTER, G.A. (2001). Bovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization. J. Virol. 75, 8251-8258.
    • (2001) J. Virol. , vol.75 , pp. 8251-8258
    • Ren, X.1    Harms, J.S.2    Splitter, G.A.3
  • 26
    • 0036870648 scopus 로고    scopus 로고
    • Efficient translocation and apoptosis induction by adenovirus encoded VP22-p53 fusion protein in human tumor cells in vitro
    • ROY, I., HOLLE, L., SONG, W., HOLLE, E., WAGNER, T., and YU, X. (2002). Efficient translocation and apoptosis induction by adenovirus encoded VP22-p53 fusion protein in human tumor cells in vitro. Anticancer Res. 22, 3185-3189.
    • (2002) Anticancer Res. , vol.22 , pp. 3185-3189
    • Roy, I.1    Holle, L.2    Song, W.3    Holle, E.4    Wagner, T.5    Yu, X.6
  • 27
    • 0015253192 scopus 로고
    • Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion
    • SPEAR, P.G., and ROIZMAN, B. (1972). Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion. J. Virol. 9, 143-159.
    • (1972) J. Virol. , vol.9 , pp. 143-159
    • Spear, P.G.1    Roizman, B.2
  • 28
    • 0001860050 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly and envelopment
    • W. Chiu, R.M. Burnett, and R.L. Carcea, eds. (Oxford University Press, New York)
    • STEVEN, A.C., and SPEAR, P.G. (1997). Herpesvirus capsid assembly and envelopment. In Structural Biology of Viruses. W. Chiu, R.M. Burnett, and R.L. Carcea, eds. (Oxford University Press, New York) pp. 312-351.
    • (1997) Structural Biology of Viruses , pp. 312-351
    • Steven, A.C.1    Spear, P.G.2
  • 29
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • THORNBERRY, N.A., and LAZEBNIK, Y. (1998). Caspases: Enemies within. Science 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 32
    • 0037295437 scopus 로고    scopus 로고
    • Intercellular trafficking and enhanced in vivo antitumour activity of a non-virally delivered p27-VP22 fusion protein
    • ZAVAGLIA, D., FAVROT, M.C., EYMIN, B., TENAUD, C., and COLL, J.L. (2003). Intercellular trafficking and enhanced in vivo antitumour activity of a non-virally delivered p27-VP22 fusion protein. Gene Ther. 10, 314-325.
    • (2003) Gene Ther. , vol.10 , pp. 314-325
    • Zavaglia, D.1    Favrot, M.C.2    Eymin, B.3    Tenaud, C.4    Coll, J.L.5
  • 33
    • 0036267436 scopus 로고    scopus 로고
    • VP22-mediated intercellular transport of p53 in hepatoma cells in vitro and in vivo
    • ZENDER, L., KUHNEL, F., KOCK, R., MANNS, M., and KUBICKA, S. (2002a). VP22-mediated intercellular transport of p53 in hepatoma cells in vitro and in vivo. Cancer Gene Ther. 9, 489-496.
    • (2002) Cancer Gene Ther. , vol.9 , pp. 489-496
    • Zender, L.1    Kuhnel, F.2    Kock, R.3    Manns, M.4    Kubicka, S.5
  • 35
    • 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. (1999). An APAF-1 cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274, 11549-11556.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.