메뉴 건너뛰기




Volumn 43, Issue 3, 1999, Pages 245-252

Recruitment of apoptotic cysteine proteases (caspases) in influenza virus-induced cell death

Author keywords

Apoptosis; Caspase; Influenza virus

Indexed keywords

CASPASE; CYSTEINE PROTEINASE; FAS ANTIGEN;

EID: 0033041585     PISSN: 03855600     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1348-0421.1999.tb02400.x     Document Type: Article
Times cited : (72)

References (47)
  • 2
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson, S., Davis, D.L., Dahlback, H., Jornvall, H., and Russell, D.W. 1989. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264: 8222-8229.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 4
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death
    • Boldin, M.P., Goncharov, T.M., Goltsev, Y.V., and Wallach, D. 1996. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell 85: 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 6
    • 0026344133 scopus 로고
    • Prevention of apoptosis by a baculovirus gene during infection of insect cells
    • Clem, R.J., Fechheimer, M., and Miller, L.K. 1991. Prevention of apoptosis by a baculovirus gene during infection of insect cells. Science 254: 1388-1390.
    • (1991) Science , vol.254 , pp. 1388-1390
    • Clem, R.J.1    Fechheimer, M.2    Miller, L.K.3
  • 7
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen, G.M. 1997. Caspases: the executioners of apoptosis. Biochem. J. 326: 1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 8
    • 0029664969 scopus 로고    scopus 로고
    • An interleukin-1β converting enzyme-like protease is a key component of fasmediated apoptosis
    • Darmon, A.J., and Bleackley, R.C. 1996. An interleukin-1β converting enzyme-like protease is a key component of Fasmediated apoptosis. J. Biol. Chem. 271: 21699-21702.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21699-21702
    • Darmon, A.J.1    Bleackley, R.C.2
  • 9
    • 0029022365 scopus 로고
    • Involvement of an ICE-like protease in Fas-mediated apoptosis
    • Enari, M., Hug, H., and Nagata, S. 1995. Involvement of an ICE-like protease in Fas-mediated apoptosis. Nature 375: 78-81.
    • (1995) Nature , vol.375 , pp. 78-81
    • Enari, M.1    Hug, H.2    Nagata, S.3
  • 10
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S. 1998. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391: 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 11
    • 0028265818 scopus 로고
    • Programmed cell death (apoptosis) in human monocyte infected by influenza A virus
    • Fesq, H., Bacher, M., Nain, M., and Gemsa, D. 1994. Programmed cell death (apoptosis) in human monocyte infected by influenza A virus. Immunobiology 190: 175-182.
    • (1994) Immunobiology , vol.190 , pp. 175-182
    • Fesq, H.1    Bacher, M.2    Nain, M.3    Gemsa, D.4
  • 12
    • 0031872125 scopus 로고    scopus 로고
    • Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells
    • Fujimoto, I., Takizawa, T., Ohba, Y., and Nakanishi, Y. 1998. Co-expression of Fas and Fas-ligand on the surface of influenza virus-infected cells. Cell Death Differ. 5: 426-431.
    • (1998) Cell Death Differ. , vol.5 , pp. 426-431
    • Fujimoto, I.1    Takizawa, T.2    Ohba, Y.3    Nakanishi, Y.4
  • 14
    • 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., Borner, C., and Michell, M.R. 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    Borner, C.6    Michell, M.R.7
  • 16
    • 0028278094 scopus 로고
    • Apoptosis: A mechanism of cell killing by influenza A and B viruses
    • Hinshaw, V.G., Olsen, C.W., Dybdahl-Sissoko, N., and Evans, D. 1994. Apoptosis: a mechanism of cell killing by influenza A and B viruses. J. Virol. 68: 3667-3673.
    • (1994) J. Virol. , vol.68 , pp. 3667-3673
    • Hinshaw, V.G.1    Olsen, C.W.2    Dybdahl-Sissoko, N.3    Evans, D.4
  • 17
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson, M.D., Weil, M., and Raff, M.C. 1997. Programmed cell death in animal development. Cell 88: 347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 18
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 β-converting enzyme
    • Kumar, S., Kinoshita, M., Noda, M., Copeland, N.G., and Jenkins, N.A. 1994. Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 β-converting enzyme. Genes Dev. 8: 1613-1626.
    • (1994) Genes Dev. , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 21
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • Martin, S.J., and Green, D.R. 1995. Protease activation during apoptosis: death by a thousand cuts? Cell 82: 349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 22
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homologue of C. elegans cell death gene ced-3
    • Miura, M., Zhu, H., Rotello, R., Hartwieg, E.A., and Yuan, J. 1993. Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homologue of C. elegans cell death gene ced-3. Cell 75: 653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 23
    • 0029114963 scopus 로고
    • Tumor necrosis factor-induced apoptosis is mediated by a crmA-sensitive cell death pathway
    • Miura, M., Friedlander, R.M., and Yuan, J. 1995. Tumor necrosis factor-induced apoptosis is mediated by a crmA-sensitive cell death pathway. Proc. Natl. Acad. Sci. U.S.A. 92: 8318-8322.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8318-8322
    • Miura, M.1    Friedlander, R.M.2    Yuan, J.3
  • 26
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. 1997. Apoptosis by death factor. Cell 88: 355-365.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 27
    • 7344226810 scopus 로고
    • Regulation of apoptosis in virus-infected cells
    • Nakanishi, Y. 1995. Regulation of apoptosis in virus-infected cells. Tiss. Cult. Res. Commun. 14: 1739-1746.
    • (1995) Tiss. Cult. Res. Commun. , vol.14 , pp. 1739-1746
    • Nakanishi, Y.1
  • 29
    • 0029656251 scopus 로고    scopus 로고
    • bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation
    • Olsen, C.W., Kehren, J.C., Dybdahl-Sissoko, N.R., and Hinshaw, V.S. 1996. bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation. J. Virol. 70: 663-666.
    • (1996) J. Virol. , vol.70 , pp. 663-666
    • Olsen, C.W.1    Kehren, J.C.2    Dybdahl-Sissoko, N.R.3    Hinshaw, V.S.4
  • 30
    • 2642667881 scopus 로고
    • Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases
    • Pickup, D.J., Ink, B.S., Hu, W., Ray, C.A., and Joklik, W.K. 1986. Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc. Natl. Acad. Sci. U.S.A. 83: 7698-7702.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 7698-7702
    • Pickup, D.J.1    Ink, B.S.2    Hu, W.3    Ray, C.A.4    Joklik, W.K.5
  • 31
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira, H., Enari, M., and Nagata, S. 1998. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391: 96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 33
    • 0030002801 scopus 로고    scopus 로고
    • Benzyloxycarbonyl-Val-Ala-ASP (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32
    • Slee, E.A., Zhu, H., Chow, S.C., MacFarlane, M., Nicholson, D.W., and Cohen, G.M. 1996. Benzyloxycarbonyl-Val-Ala-ASP (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32. Biochem. J. 315: 21-24.
    • (1996) Biochem. J. , vol.315 , pp. 21-24
    • Slee, E.A.1    Zhu, H.2    Chow, S.C.3    MacFarlane, M.4    Nicholson, D.W.5    Cohen, G.M.6
  • 34
    • 0027382362 scopus 로고
    • Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells
    • Takizawa, T., Matsukawa, S., Higuchi, Y., Nakamura, S., Nakanishi, Y., and Fukuda, R. 1993. Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells. J. Gen. Virol. 74: 2347-2355.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2347-2355
    • Takizawa, T.1    Matsukawa, S.2    Higuchi, Y.3    Nakamura, S.4    Nakanishi, Y.5    Fukuda, R.6
  • 35
    • 0029063283 scopus 로고
    • Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon
    • Takizawa, T., Fukuda, R., Miyawaki, T., Ohashi, K., and Nakanishi, Y. 1995. Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon. Virology 209: 288-296.
    • (1995) Virology , vol.209 , pp. 288-296
    • Takizawa, T.1    Fukuda, R.2    Miyawaki, T.3    Ohashi, K.4    Nakanishi, Y.5
  • 37
    • 0031041172 scopus 로고    scopus 로고
    • Regulation of apoptosis by viral gene products
    • Teodoro, J.G., and Branton, P.E. 1997. Regulation of apoptosis by viral gene products. J. Virol. 71: 1739-1746.
    • (1997) J. Virol. , vol.71 , pp. 1739-1746
    • Teodoro, J.G.1    Branton, P.E.2
  • 38
    • 0028873964 scopus 로고
    • Fas-and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product
    • Tewari, M., and Dixit, V.M. 1995. Fas-and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product. J. Biol. Chem. 270: 3255-3260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 39
    • 0028990125 scopus 로고
    • Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari, M., Quan, L.T., O'Rourke, K., Desnoyers, S., Zeng, Z., Beidler, D.R., Poirier, G.G., Salvesen, G.S., and Dixit, V.M. 1995. Yama/CPP32β, a mammalian homolog of CED-3, is a crmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 43
    • 0028978241 scopus 로고
    • Transcription stimulation of the Fas-encoding gene by nuclear factor for interleukin-6 expression upon influenza virus infection
    • Wada, N., Matsumura, M., Ohba, Y., Kobayashi, N., Takizawa, T., and Nakanishi, Y. 1995. Transcription stimulation of the Fas-encoding gene by nuclear factor for interleukin-6 expression upon influenza virus infection. J. Biol. Chem. 270: 18007-18012.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18007-18012
    • Wada, N.1    Matsumura, M.2    Ohba, Y.3    Kobayashi, N.4    Takizawa, T.5    Nakanishi, Y.6
  • 44
  • 45
    • 0030903882 scopus 로고    scopus 로고
    • C-terminal mutation of G protein β subunit affects differentially extra-cellular signal-regulated kinase and c-Jun N-terminal kinase pathways in human embryonal kidney 293 cells
    • Yamauchi, J., Kaziro, Y., and Itoh, H. 1997. C-terminal mutation of G protein β subunit affects differentially extra-cellular signal-regulated kinase and c-Jun N-terminal kinase pathways in human embryonal kidney 293 cells. J. Biol. Chem. 272: 7602-7607.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7602-7607
    • Yamauchi, J.1    Kaziro, Y.2    Itoh, H.3
  • 46
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang, X., Khosravi-Far, R., Chang, H.Y., and Baltimore, D. 1997. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89: 1067-1076.
    • (1997) Cell , vol.89 , pp. 1067-1076
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 47
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA. Analysis of five caspases
    • Zhou, Q., Snipas, S., Orth, K., Muzio, M., Dixit, V.M., and Salvesen, G.S. 1997. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J. Biol. Chem. 272: 7797-7800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.