메뉴 건너뛰기




Volumn 162, Issue 5, 1999, Pages 2766-2774

A tailless Fas-FADD death-effector domain chimera is sufficient to execute Fas function in T cells but not B cells of MRL-lpr/lpr mice

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; FAS ANTIGEN;

EID: 0033106243     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (11)

References (52)
  • 1
    • 0028927607 scopus 로고
    • The Fas death factor
    • Nagata, S., and P. Golstein. 1995. The Fas death factor. Science 267:1449.
    • (1995) Science , vol.267 , pp. 1449
    • Nagata, S.1    Golstein, P.2
  • 2
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. 1997. Apoptosis by death factor. Cell 88:355.
    • (1997) Cell , vol.88 , pp. 355
    • Nagata, S.1
  • 3
    • 0026568919 scopus 로고
    • Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis
    • Watanabe, F. R., C. I. Brannan, N. G. Copeland, N. A. Jenkins, and S. Nagata. 1992. Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis. Nature 356:314.
    • (1992) Nature , vol.356 , pp. 314
    • Watanabe, F.R.1    Brannan, C.I.2    Copeland, N.G.3    Jenkins, N.A.4    Nagata, S.5
  • 6
    • 0031079805 scopus 로고    scopus 로고
    • Portrait of an executioner: The molecular mechanism of FAS/APO-1-induced apoptosis
    • Chinnaiyan, A. M., and V. M. Dixit. 1997. Portrait of an executioner: the molecular mechanism of FAS/APO-1-induced apoptosis. Sem. Immunol. 9:69.
    • (1997) Sem. Immunol. , vol.9 , pp. 69
    • Chinnaiyan, A.M.1    Dixit, V.M.2
  • 7
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of fas/ APO1 contains a sequence motif related to the death domain
    • Boldin, M. P., E. E. Varfolomeev, Z. Pancer, I. L. Mett, J. H. Camonis, and D. Wallach. 1995. A novel protein that interacts with the death domain of fas/ APO1 contains a sequence motif related to the death domain. J. Biol. Chem. 270:7795.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7795
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 8
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A. M., K. O'Rourke, M. Tewari, and V. M. Dixit. 1995. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81:505.
    • (1995) Cell , vol.81 , pp. 505
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 9
    • 0030001051 scopus 로고    scopus 로고
    • A mouse Fas-associated protein with homology to the human MortI/FADD protein is essential for Fas-induced apoptosis
    • Zhang, J., and A. Winoto. 1996. A mouse Fas-associated protein with homology to the human MortI/FADD protein is essential for Fas-induced apoptosis. Mol. Cell. Biol. 16:2756.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2756
    • Zhang, J.1    Winoto, A.2
  • 10
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • Stanger, B. Z., P. Leder, T.-H. Lee, E. Kim, and B. Seed. 1995. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 81:513.
    • (1995) Cell , vol.81 , pp. 513
    • Stanger, B.Z.1    Leder, P.2    Lee, T.-H.3    Kim, E.4    Seed, B.5
  • 11
    • 0029616220 scopus 로고
    • A Fas-associated protein factor, FAFI, potentiates Fas-mediated apoptosis
    • Chu, K., X. Niu, and L. T. Williams. 1995. A Fas-associated protein factor, FAFI, potentiates Fas-mediated apoptosis. Proc. Natl. Acad. Sci. USA 92:11894.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11894
    • Chu, K.1    Niu, X.2    Williams, L.T.3
  • 12
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura, T., L. Gong, T. Kamitani, T. Wada, I. Okura, C. F. Wei, H. M. Chang, and E. T. Yeh. 1996. Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J. Immunol. 157:4277.
    • (1996) J. Immunol. , vol.157 , pp. 4277
    • Okura, T.1    Gong, L.2    Kamitani, T.3    Wada, T.4    Okura, I.5    Wei, C.F.6    Chang, H.M.7    Yeh, E.T.8
  • 13
    • 0029963721 scopus 로고    scopus 로고
    • Association of human Fas (CD95) with a ubiquitin-conjugating enzyme (UBC-FAP)
    • Wright, D. A., B. Futcher, P. Ghosh, and R. S. Geha. 1996. Association of human Fas (CD95) with a ubiquitin-conjugating enzyme (UBC-FAP). J. Biol. Chem. 271:31037.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31037
    • Wright, D.A.1    Futcher, B.2    Ghosh, P.3    Geha, R.S.4
  • 14
    • 0031587883 scopus 로고    scopus 로고
    • Daxx, a novel Fas-binding protein that activates JNK and apoptosis
    • Yang, X., R. Khosravi-Far, H. Y. Chang, and D. Baltimore. 1997. Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89:1067.
    • (1997) Cell , vol.89 , pp. 1067
    • Yang, X.1    Khosravi-Far, R.2    Chang, H.Y.3    Baltimore, D.4
  • 15
    • 0032525052 scopus 로고    scopus 로고
    • Phosphorylation of FADD/MORTI and Fas by kinases that associate with the membrane-proximal cytoplasmic domain of Fas
    • Kennedy, N. J., and R. C. Budd. 1998. Phosphorylation of FADD/MORTI and Fas by kinases that associate with the membrane-proximal cytoplasmic domain of Fas. J. Immunol. 160:4881.
    • (1998) J. Immunol. , vol.160 , pp. 4881
    • Kennedy, N.J.1    Budd, R.C.2
  • 16
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato, T., S. Irie, S. Kitada, and J. C. Reed. 1995. FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 268:411.
    • (1995) Science , vol.268 , pp. 411
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 17
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/ CD95) associated proteins form a death-inducing signaling complex (DISC) with the receptor
    • Kischkel, F. C., S. Hellbardt, I. Behrmann, M. Germer, M. Pawlita, P. H. Krammer, and M. E. Peter. 1995. Cytotoxicity-dependent APO-1 (Fas/ CD95) associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J. 14:5579.
    • (1995) EMBO J. , vol.14 , pp. 5579
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3    Germer, M.4    Pawlita, M.5    Krammer, P.H.6    Peter, M.E.7
  • 19
    • 0032546387 scopus 로고    scopus 로고
    • Absence of Fas-mediated apoptosis and T cell receptor-induced proliferation in FADD-deficient mice
    • Zhang, J., D. Cado, A. Chen, N. H. Kabra, and A. Winoto. 1998. Absence of Fas-mediated apoptosis and T cell receptor-induced proliferation in FADD-deficient mice. Nature 392:296.
    • (1998) Nature , vol.392 , pp. 296
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 22
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H., H.-B. Shu, M.-G. Pan, and D. V. Goeddel. 1996. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 84:299.
    • (1996) Cell , vol.84 , pp. 299
    • Hsu, H.1    Shu, H.-B.2    Pan, M.-G.3    Goeddel, D.V.4
  • 24
    • 0000046089 scopus 로고
    • A human β-actin expression vector system directs high-level accumulation of antisense transcripts
    • Gunning, P., J. Leavitt, G. Muscat, S. Y. Ng, and L. Kedes. 1987. A human β-actin expression vector system directs high-level accumulation of antisense transcripts. Proc. Natl. Acad. Sci. USA 84:4831.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4831
    • Gunning, P.1    Leavitt, J.2    Muscat, G.3    Ng, S.Y.4    Kedes, L.5
  • 25
    • 0025119207 scopus 로고
    • Dissection of thymocyte signaling pathways by in vivo expression of pertussis toxin ADP-ribosyltransferase
    • Chaffin, K. E., C. R. Beals, T. M. Wilkie, K. A. Forbush, M. I. Simon, and R. M. Perlmutter. 1990. Dissection of thymocyte signaling pathways by in vivo expression of pertussis toxin ADP-ribosyltransferase. EMBO J. 9:3821.
    • (1990) EMBO J. , vol.9 , pp. 3821
    • Chaffin, K.E.1    Beals, C.R.2    Wilkie, T.M.3    Forbush, K.A.4    Simon, M.I.5    Perlmutter, R.M.6
  • 26
  • 27
    • 0026756135 scopus 로고
    • Cloning of gt box-binding proteins: A novel sp1 multigene family regulating T-cell receptor gene expression
    • Kingsley, C., and A. Winoto. 1992. Cloning of GT box-binding proteins: a novel Sp1 multigene family regulating T-cell receptor gene expression. Mol. Cell. Biol. 12:4251.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4251
    • Kingsley, C.1    Winoto, A.2
  • 28
    • 0030789734 scopus 로고    scopus 로고
    • Adjacent DNA elements dominantly restrict the ubiquitous activity of a novel chromatin-opening region to specific tissues
    • Ortiz, B. D., D. Cado, V. Chen, P. W. Diaz, and A. Winoto. 1997. Adjacent DNA elements dominantly restrict the ubiquitous activity of a novel chromatin-opening region to specific tissues. EMBO J. 16:5037.
    • (1997) EMBO J. , vol.16 , pp. 5037
    • Ortiz, B.D.1    Cado, D.2    Chen, V.3    Diaz, P.W.4    Winoto, A.5
  • 29
    • 0028446580 scopus 로고
    • A locus control region in the T cell receptor α/δ locus
    • Diaz, P., D. Cado, and A. Winoto. 1994. A locus control region in the T cell receptor α/δ locus. Immunity 1:207.
    • (1994) Immunity , vol.1 , pp. 207
    • Diaz, P.1    Cado, D.2    Winoto, A.3
  • 30
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • Gavrieli, Y., Y. Sherman, and S. A. Ben-Sasson. 1992. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119:493.
    • (1992) J. Cell Biol. , vol.119 , pp. 493
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 31
    • 0028102478 scopus 로고
    • Cleavage of poly (ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y. A., S. H. Kaufmann, S. Desnoyers, G. G. Poirier, and W. C. Earnshaw. 1994. Cleavage of poly (ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371:346.
    • (1994) Nature , vol.371 , pp. 346
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 33
    • 0032522665 scopus 로고    scopus 로고
    • Transgenic expression of Fas in T cells blocks lymphoproliferation but not autoimmune disease in MRL-lpr mice
    • Fukuyama, H., M. Adachi, S. Suematsu, K. Miwa, T. Suda, N. Yoshida, and S. Nagata. 1998. Transgenic expression of Fas in T cells blocks lymphoproliferation but not autoimmune disease in MRL-lpr mice. J. Immunol. 160:3805.
    • (1998) J. Immunol. , vol.160 , pp. 3805
    • Fukuyama, H.1    Adachi, M.2    Suematsu, S.3    Miwa, K.4    Suda, T.5    Yoshida, N.6    Nagata, S.7
  • 34
    • 0025875259 scopus 로고
    • Lpr and gld: Single gene models of systemic autoimmunity and lymphoproliferative disease
    • Cohen, P. L., and R. A. Eisenberg. 1991. Lpr and gld: single gene models of systemic autoimmunity and lymphoproliferative disease. Annu. Rev. Immunol. 9:243.
    • (1991) Annu. Rev. Immunol. , vol.9 , pp. 243
    • Cohen, P.L.1    Eisenberg, R.A.2
  • 36
    • 0030002562 scopus 로고    scopus 로고
    • Restriction of the TCR repertoire inhibits the development of memory T cells and prevents autoimmunity in lpr mice
    • Perkins, D. L., J. A. Listman, A. Marshak-Rothstein, W. Kozlow, V. R. Kelley, P. W. Finn, and I. J. Rimm. 1996. Restriction of the TCR repertoire inhibits the development of memory T cells and prevents autoimmunity in lpr mice. J. Immunol. 156:4961.
    • (1996) J. Immunol. , vol.156 , pp. 4961
    • Perkins, D.L.1    Listman, J.A.2    Marshak-Rothstein, A.3    Kozlow, W.4    Kelley, V.R.5    Finn, P.W.6    Rimm, I.J.7
  • 37
    • 0028985378 scopus 로고
    • + T cells but normal autoantibody production in lpr/lpr mice lacking major histocompatibility complex class I molecules
    • + T cells but normal autoantibody production in lpr/lpr mice lacking major histocompatibility complex class I molecules. Eur. J. Immunol. 25:37.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 37
    • Ohteki, T.1    Iwamoto, M.2    Izui, S.3    MacDonald, H.R.4
  • 38
    • 0028206729 scopus 로고
    • Correction of accelerated autoimmune disease by early replacement of the mutated lpr gene with the normal Fas apoptosis gene in the T cells of transgenic MRL-lpr/lpr mice
    • Wu, J., T. Zhou, J. Zhang, J. He, W. C. Gause, and J. D. Mountz. 1994. Correction of accelerated autoimmune disease by early replacement of the mutated lpr gene with the normal Fas apoptosis gene in the T cells of transgenic MRL-lpr/lpr mice. Proc. Natl. Acad. Sci. USA 91:2344.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2344
    • Wu, J.1    Zhou, T.2    Zhang, J.3    He, J.4    Gause, W.C.5    Mountz, J.D.6
  • 39
    • 0026715951 scopus 로고
    • Inhibition of abnormal t cell development and autoimmunity in gld mice by transgenic T cell receptor β chain
    • Yui, K., A. Bhandoola, M. Z. Radic, S. Komori, M. Katsumata, and M. I. Greene. 1992. Inhibition of abnormal T cell development and autoimmunity in gld mice by transgenic T cell receptor β chain. Eur. J. Immunol. 22:1693.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 1693
    • Yui, K.1    Bhandoola, A.2    Radic, M.Z.3    Komori, S.4    Katsumata, M.5    Greene, M.I.6
  • 40
    • 0032532008 scopus 로고    scopus 로고
    • Thymic expression of the transcription factor Nur77 rescues the T cell but not the B cell abnormality of gld/gld mice
    • Chan, F. K.-M., A. Chen, and A. Winoto. 1998. Thymic expression of the transcription factor Nur77 rescues the T cell but not the B cell abnormality of gld/gld mice. J. Immunol. 161:4252.
    • (1998) J. Immunol. , vol.161 , pp. 4252
    • Chan, F.K.-M.1    Chen, A.2    Winoto, A.3
  • 41
    • 0030592564 scopus 로고    scopus 로고
    • Expansion or elimination of B cells in vivo: Dual roles for CD40- and fas (CD95)-ligands modulated by the b cell antigen receptor
    • Rathmell, J. C., S. E. Townsend, J. C. Xu, R. A. Flavell, and C. C. Goodnow. 1996. Expansion or elimination of B cells in vivo: dual roles for CD40- and fas (CD95)-ligands modulated by the B cell antigen receptor. Cell 87:319.
    • (1996) Cell , vol.87 , pp. 319
    • Rathmell, J.C.1    Townsend, S.E.2    Xu, J.C.3    Flavell, R.A.4    Goodnow, C.C.5
  • 45
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORTI/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin, M. P., T. M. Goncharov, Y. V. Goltsev, and D. Wallach. 1996. Involvement of MACH, a novel MORTI/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85:803.
    • (1996) Cell , vol.85 , pp. 803
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 47
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X. L., H. Y. Chang, and D. Baltimore. 1998. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1:319.
    • (1998) Mol. Cell , vol.1 , pp. 319
    • Yang, X.L.1    Chang, H.Y.2    Baltimore, D.3
  • 48
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACH α 1) death signal
    • Martin, D. A., R. M. Siegel, L. X. Zheng, and M. J. Lenardo. 1998. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACH α 1) death signal. J. Biol. Chem. 273:4345.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4345
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.X.3    Lenardo, M.J.4
  • 50
    • 0030293508 scopus 로고    scopus 로고
    • Apoptosis of mouse naive T cells induced by recombinant soluble Fas ligand and activation-induced resistance to Fas ligand
    • Suda, T., M. Tanaka, K. Miwa, and S. Nagata. 1996. Apoptosis of mouse naive T cells induced by recombinant soluble Fas ligand and activation-induced resistance to Fas ligand. J. Immunol. 157:3918.
    • (1996) J. Immunol. , vol.157 , pp. 3918
    • Suda, T.1    Tanaka, M.2    Miwa, K.3    Nagata, S.4
  • 51
    • 0027183703 scopus 로고
    • Activation interferes with the APO-1 pathway in mature human T cells
    • Klas, C., K. M. Debatin, R. R. Jonker, and P. H. Krammer. 1993. Activation interferes with the APO-1 pathway in mature human T cells. Int. Immunol. 5:625.
    • (1993) Int. Immunol. , vol.5 , pp. 625
    • Klas, C.1    Debatin, K.M.2    Jonker, R.R.3    Krammer, P.H.4
  • 52
    • 17544398702 scopus 로고    scopus 로고
    • Biochemical mechanisms of IL-2-regulated Fas-mediated T cell apoptosis
    • Refaeli, Y., L. V. Parijs, C. A. London, J. Tschopp, and A. K. Abbas. 1998. Biochemical mechanisms of IL-2-regulated Fas-mediated T cell apoptosis. Immunity 8:615.
    • (1998) Immunity , vol.8 , pp. 615
    • Refaeli, Y.1    Parijs, L.V.2    London, C.A.3    Tschopp, J.4    Abbas, A.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.