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Volumn 60, Issue 7, 2000, Pages 1818-1823

Inhibitor of apoptosis protein hILP undergoes caspase-mediated cleavage during T lymphocyte apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 7; CYTOKINE RESPONSE MODIFIER A; ENZYME INHIBITOR; ETOPOSIDE; FAS ANTIGEN; INHIBITOR OF APOPTOSIS PROTEIN; PROTEIN BCL 2; PROTEIN HILP; STAUROSPORINE; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG;

EID: 0034032963     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (73)

References (38)
  • 1
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen, G. M. Caspases: the executioners of apoptosis. Biochem. J., 326: 1-16, 1997.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 2
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Washington DC
    • Thornberry, N. A., and Lazebnik, Y. Caspases: enemies within. Science (Washington DC), 281: 1312-1316, 1998.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 3
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X., Chang, H. Y., and Baltimore, D. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell, 1: 319-325, 1998.
    • (1998) Mol. Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 4
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHα1) death signal
    • Martin, D. A., Siegel, R. M., Zheng, L., and Lenardo, M. J. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHα1) death signal. J. Biol. Chem., 273: 4345-4349, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 7
    • 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. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death. Cell, 85: 803-815, 1996.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 8
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiate an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiate an apoptotic protease cascade. Cell, 91: 479-489, 1997.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 9
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., and Wang, X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell, 86: 147-157, 1996.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 11
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Washington DC
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmeyer, D. D. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science (Washington DC), 275: 1132-1136, 1997.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 12
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-21. release of cytochrome c from mitochondria blocked
    • Washington DC
    • Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T. I., Jones, D.P., and Wang, X. Prevention of apoptosis by Bcl-21. release of cytochrome c from mitochondria blocked. Science (Washington DC), 275: 1129-1132, 1997.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.I.7    Jones, D.P.8    Wang, X.9
  • 15
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Henzel, W. J., Liu, X., Lutschg, A., and Wang, X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell, 90: 405-413, 1997.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 17
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins: Suppressors of apoptosis
    • Deveraux, Q. L., and Reed, J. C. IAP family proteins: suppressors of apoptosis. Genes Dev., 13: 239-252, 1999.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 19
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy, N., Deveraux, Q. L., Takahashi, R., Salvesen, G. S., and Reed, J. C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases EMBO J., 16: 6914-6925, 1997.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 20
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux, Q. L., Takahashi, R., Salvesen, G. S., and Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature (Lond.), 388: 300-304, 1997.
    • (1997) Nature (Lond.) , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 23
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme
    • Ray, C. A., Black, R. A., Kronheim, S. R., Greenstreet, T. A., Sleath, P. R., Salvesen, G. S., and Pickup, D. J. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1β converting enzyme. Cell, 69: 597-604, 1992.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 25
    • 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. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J. Biol. Chem., 272: 7797-7800, 1997.
    • (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
  • 26
    • 0029793621 scopus 로고    scopus 로고
    • Apoptotic suppression by baculovirus P35 involves cleavage by and inhibition of a virus-induced CED-3/ICE-like protease
    • Bertin, J., Mendrysa, S. M., LaCount, D. J., Gaur, S., Krebs, J. F., Armstrong, R. C., Tomaselli, K. J., and Friesen, P. D. Apoptotic suppression by baculovirus P35 involves cleavage by and inhibition of a virus-induced CED-3/ICE-like protease. J. Virol., 70: 6251-6259, 1996.
    • (1996) J. Virol. , vol.70 , pp. 6251-6259
    • Bertin, J.1    Mendrysa, S.M.2    LaCount, D.J.3    Gaur, S.4    Krebs, J.F.5    Armstrong, R.C.6    Tomaselli, K.J.7    Friesen, P.D.8
  • 27
    • 0029056059 scopus 로고
    • Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein
    • Xue, D., and Horvitz, H. R. Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein. Nature (Lond.), 377: 248-251, 1995.
    • (1995) Nature (Lond.) , vol.377 , pp. 248-251
    • Xue, D.1    Horvitz, H.R.2
  • 28
    • 0028168514 scopus 로고
    • Inhibition of interleukin-1β converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition
    • Komiyama, T., Ray, C. A., Pickup, D. J., Howard, A. D., Thomberry, N. A., Peterson, E. P., and Salvesen, G. Inhibition of interleukin-1β converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J. Biol. Chem., 269: 19331-19337, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19331-19337
    • Komiyama, T.1    Ray, C.A.2    Pickup, D.J.3    Howard, A.D.4    Thomberry, N.A.5    Peterson, E.P.6    Salvesen, G.7
  • 29
    • 0033521529 scopus 로고    scopus 로고
    • XIAP. a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway
    • Yamaguchi, K., Nagai, S., Ninomiya-Tsuji, J., Nishita, M., Tamai, K., Irie, K., Ueno, N., Nishida, E., Shibuya, H., and Matsumoto, K. XIAP. a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway. EMBO J., 18: 179-187, 1999.
    • (1999) EMBO J. , vol.18 , pp. 179-187
    • Yamaguchi, K.1    Nagai, S.2    Ninomiya-Tsuji, J.3    Nishita, M.4    Tamai, K.5    Irie, K.6    Ueno, N.7    Nishida, E.8    Shibuya, H.9    Matsumoto, K.10
  • 31
    • 0030943468 scopus 로고    scopus 로고
    • Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ice protease family
    • Dou, Q. P., An, B., Antoku, K., and Johnson, D. E. Fas stimulation induces RB dephosphorylation and proteolysis that is blocked by inhibitors of the ICE protease family. J. Cell. Biochem., 64: 586-594, 1997.
    • (1997) J. Cell. Biochem. , vol.64 , pp. 586-594
    • Dou, Q.P.1    An, B.2    Antoku, K.3    Johnson, D.E.4
  • 32
    • 0033534465 scopus 로고    scopus 로고
    • Regulation of fas-ligand expression during activation-induced cell death in T lymphocytes via nuclear factor κB
    • Kasibhatla, S., Genestier, L., and Green, D. R. Regulation of fas-ligand expression during activation-induced cell death in T lymphocytes via nuclear factor κB. J. Biol. Chem., 274: 987-992, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 987-992
    • Kasibhatla, S.1    Genestier, L.2    Green, D.R.3
  • 34
    • 0032102258 scopus 로고    scopus 로고
    • Lymphocyte apoptosis induced by Fas ligand-expressing ovarian carcinoma cells: Implications for altered expression of TcR in tumor-associated lymphocytes
    • Rabinowich, H., Reichert, T. E., Kashii, Y., Gastman, B. R., Bell, M. C., and Whiteside, T. L. Lymphocyte apoptosis induced by Fas ligand-expressing ovarian carcinoma cells: implications for altered expression of TcR in tumor-associated lymphocytes. J. Clin. Investig., 101: 2579-2588, 1998.
    • (1998) J. Clin. Investig. , vol.101 , pp. 2579-2588
    • Rabinowich, H.1    Reichert, T.E.2    Kashii, Y.3    Gastman, B.R.4    Bell, M.C.5    Whiteside, T.L.6
  • 36
    • 0032546453 scopus 로고    scopus 로고
    • Involvement of Bcl-2 cleavage in the acceleration of VP-16-induced U937 cell apoptosis
    • Fujita, N., and Tsuruo, T. Involvement of Bcl-2 cleavage in the acceleration of VP-16-induced U937 cell apoptosis. Biochem. Biophys. Res. Commun., 246: 484-488, 1998.
    • (1998) Biochem. Biophys. Res. Commun. , vol.246 , pp. 484-488
    • Fujita, N.1    Tsuruo, T.2
  • 38
    • 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 Michel, M. R. Alphaviruses induce apoptosis in Bcl-2-overexpressing cells: evidence for a caspase-mediated, proteolytic inactivation of Bcl-2. EMBO J., 17: 1268-1278, 1998.
    • (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    Michel, M.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.