메뉴 건너뛰기




Volumn 335, Issue 2, 2005, Pages 575-583

The apoptosis inhibitory domain of FE65-like protein 1 regulates both apoptotic and caspase-independent programmed cell death mediated by tumor necrosis factor

Author keywords

Apoptosis; Caspase independent programmed cell death; Ceramide; FE65 like; Tumor necrosis factor

Indexed keywords

ANTIOXIDANT; BUTYLATED HYDROXYANISOLE; CASPASE; CERAMIDE; COMPLEMENTARY DNA; PROTEIN FE65; REACTIVE OXYGEN METABOLITE; SPHINGOLIPID; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR;

EID: 23744459810     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.125     Document Type: Article
Times cited : (4)

References (31)
  • 1
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • M. Leist, and M. Jäättelä Four deaths and a funeral: from caspases to alternative mechanisms Nat. Rev. Mol. Cell Biol. 2 2001 589 598
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jäättelä, M.2
  • 2
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • R.W. Johnstone, A.A. Ruefli, and S.W. Lowe Apoptosis: a link between cancer genetics and chemotherapy Cell 108 2002 153 164
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 3
    • 2442480795 scopus 로고    scopus 로고
    • Multiple cell death pathways as regulators of tumour initiation and progression
    • M. Jäättelä Multiple cell death pathways as regulators of tumour initiation and progression Oncogene 23 2004 2746 2756
    • (2004) Oncogene , vol.23 , pp. 2746-2756
    • Jäättelä, M.1
  • 4
    • 0037386245 scopus 로고    scopus 로고
    • Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2
    • A. Cauwels, B. Janssen, A. Waeytens, C. Cuvelier, and P. Brouckaert Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2 Nat. Immunol. 4 2003 387 393
    • (2003) Nat. Immunol. , vol.4 , pp. 387-393
    • Cauwels, A.1    Janssen, B.2    Waeytens, A.3    Cuvelier, C.4    Brouckaert, P.5
  • 5
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • M. Jäättelä, and J. Tschopp Caspase-independent cell death in T lymphocytes Nat. Immunol. 4 2003 416 423
    • (2003) Nat. Immunol. , vol.4 , pp. 416-423
    • Jäättelä, M.1    Tschopp, J.2
  • 10
    • 0034637510 scopus 로고    scopus 로고
    • Sensitization to death receptor cytotoxicity by inhibition of Fas-associated death domain protein (FADD)/caspase signaling-requirement of cell cycle progression
    • S. Lüschen, S. Ussat, G. Scherer, D. Kabelitz, and S. Adam-Klages Sensitization to death receptor cytotoxicity by inhibition of Fas-associated death domain protein (FADD)/caspase signaling-requirement of cell cycle progression J. Biol. Chem. 275 2000 24670 24678
    • (2000) J. Biol. Chem. , vol.275 , pp. 24670-24678
    • Lüschen, S.1    Ussat, S.2    Scherer, G.3    Kabelitz, D.4    Adam-Klages, S.5
  • 12
    • 0034610019 scopus 로고    scopus 로고
    • Characterization of an apoptosis inhibitory domain at the C-termini of FE65-like protein
    • H. Cao, N. Pratt, J. Mattison, Y. Zhao, and N.S. Chang Characterization of an apoptosis inhibitory domain at the C-termini of FE65-like protein Biochem. Biophys. Res. Commun. 276 2000 843 850
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 843-850
    • Cao, H.1    Pratt, N.2    Mattison, J.3    Zhao, Y.4    Chang, N.S.5
  • 13
    • 16844374267 scopus 로고    scopus 로고
    • Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPalpha pathway in primates
    • Q. Hu, L. Wang, Z. Yang, B.H. Cool, G. Zitnik, and G.M. Martin Endoproteolytic cleavage of FE65 converts the adaptor protein to a potent suppressor of the sAPPalpha pathway in primates J. Biol. Chem. 280 2005 12548 12558
    • (2005) J. Biol. Chem. , vol.280 , pp. 12548-12558
    • Hu, Q.1    Wang, L.2    Yang, Z.3    Cool, B.H.4    Zitnik, G.5    Martin, G.M.6
  • 14
    • 0037144438 scopus 로고    scopus 로고
    • Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression
    • P. Bruni, G. Minopoli, T. Brancaccio, M. Napolitano, R. Faraonio, N. Zambrano, U. Hansen, and T. Russo Fe65, a ligand of the Alzheimer's beta-amyloid precursor protein, blocks cell cycle progression by down-regulating thymidylate synthase expression J. Biol. Chem. 277 2002 35481 35488
    • (2002) J. Biol. Chem. , vol.277 , pp. 35481-35488
    • Bruni, P.1    Minopoli, G.2    Brancaccio, T.3    Napolitano, M.4    Faraonio, R.5    Zambrano, N.6    Hansen, U.7    Russo, T.8
  • 15
    • 0032519711 scopus 로고    scopus 로고
    • Fe65L2: A new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein
    • A. Duilio, R. Faraonio, G. Minopoli, N. Zambrano, and T. Russo Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein Biochem. J. 330 1998 513 519
    • (1998) Biochem. J. , vol.330 , pp. 513-519
    • Duilio, A.1    Faraonio, R.2    Minopoli, G.3    Zambrano, N.4    Russo, T.5
  • 16
    • 0032489554 scopus 로고    scopus 로고
    • TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase
    • R. Schwandner, K. Wiegmann, K. Bernardo, D. Kreder, and M. Krönke TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase J. Biol. Chem. 273 1998 5916 5922
    • (1998) J. Biol. Chem. , vol.273 , pp. 5916-5922
    • Schwandner, R.1    Wiegmann, K.2    Bernardo, K.3    Kreder, D.4    Krönke, M.5
  • 18
    • 0036537553 scopus 로고    scopus 로고
    • Feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65 and beta-amyloid precursor protein genes, are involved in the same pathway that controls nematode pharyngeal pumping
    • N. Zambrano, M. Bimonte, S. Arbucci, D. Gianni, T. Russo, and P. Bazzicalupo feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65 and beta-amyloid precursor protein genes, are involved in the same pathway that controls nematode pharyngeal pumping J. Cell Sci. 115 2002 1411 1422
    • (2002) J. Cell Sci. , vol.115 , pp. 1411-1422
    • Zambrano, N.1    Bimonte, M.2    Arbucci, S.3    Gianni, D.4    Russo, T.5    Bazzicalupo, P.6
  • 19
    • 0036844981 scopus 로고    scopus 로고
    • Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains
    • H. Tanahashi, and T. Tabira Characterization of an amyloid precursor protein-binding protein Fe65L2 and its novel isoforms lacking phosphotyrosine-interaction domains Biochem. J. 367 2002 687 695
    • (2002) Biochem. J. , vol.367 , pp. 687-695
    • Tanahashi, H.1    Tabira, T.2
  • 20
    • 0032493814 scopus 로고    scopus 로고
    • The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1
    • N. Zambrano, G. Minopoli, P. de Candia, and T. Russo The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1 J. Biol. Chem. 273 1998 20128 20133
    • (1998) J. Biol. Chem. , vol.273 , pp. 20128-20133
    • Zambrano, N.1    Minopoli, G.2    De Candia, P.3    Russo, T.4
  • 21
    • 2542423595 scopus 로고    scopus 로고
    • The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling
    • M.S. Perkinton, C.L. Standen, K.F. Lau, S. Kesavapany, H.L. Byers, M. Ward, D.M. McLoughlin, and C.C. Miller The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling J. Biol. Chem. 279 2004 22084 22091
    • (2004) J. Biol. Chem. , vol.279 , pp. 22084-22091
    • Perkinton, M.S.1    Standen, C.L.2    Lau, K.F.3    Kesavapany, S.4    Byers, H.L.5    Ward, M.6    McLoughlin, D.M.7    Miller, C.C.8
  • 23
    • 0018349752 scopus 로고
    • Stimulation of RNA synthesis in L-929 cells by rabbit tumor necrosis factor
    • J.M. Ostrove, and G.E. Gifford Stimulation of RNA synthesis in L-929 cells by rabbit tumor necrosis factor Proc. Soc. Exp. Biol. Med. 160 1979 354 358
    • (1979) Proc. Soc. Exp. Biol. Med. , vol.160 , pp. 354-358
    • Ostrove, J.M.1    Gifford, G.E.2
  • 26
    • 0346461445 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase reduces TNF-induced activation of NF-kappaB, elicits caspase activity, and enhances cytotoxicity
    • S. Lüschen, G. Scherer, S. Ussat, H. Ungefroren, and S. Adam-Klages Inhibition of p38 mitogen-activated protein kinase reduces TNF-induced activation of NF-kappaB, elicits caspase activity, and enhances cytotoxicity Exp. Cell. Res. 293 2004 196 206
    • (2004) Exp. Cell. Res. , vol.293 , pp. 196-206
    • Lüschen, S.1    Scherer, G.2    Ussat, S.3    Ungefroren, H.4    Adam-Klages, S.5
  • 27
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • O. Micheau, and J. Tschopp Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes Cell 114 2003 181 190
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 30
    • 0031919157 scopus 로고    scopus 로고
    • Regulation of ceramide production and apoptosis
    • R.N. Kolesnick, and M. Krönke Regulation of ceramide production and apoptosis Annu. Rev. Physiol. 60 1998 643 665
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 643-665
    • Kolesnick, R.N.1    Krönke, M.2
  • 31
    • 0028468309 scopus 로고
    • The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts
    • R. Hurwitz, K. Ferlinz, and K. Sandhoff The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts Biol. Chem. Hoppe-Seyler 375 1994 447 450
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 447-450
    • Hurwitz, R.1    Ferlinz, K.2    Sandhoff, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.