메뉴 건너뛰기




Volumn 14, Issue 1, 2003, Pages 67-77

Caspase- and serine protease-dependent apoptosis by the death domain of fadd in normal epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CASPASE; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 9; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; SERINE PROTEINASE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG;

EID: 0037237988     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-04-0207     Document Type: Article
Times cited : (38)

References (49)
  • 1
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi, A., and Dixit, V.M. (1998). Death receptors: signaling and modulation. Science 281, 1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 2
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activity of recombinant soluble Apo2 ligand
    • Ashkenazi, A. et al. (1999). Safety and antitumor activity of recombinant soluble Apo2 ligand. J. Clin. Invest. 104, 155-162.
    • (1999) J. Clin. Invest. , vol.104 , pp. 155-162
    • Ashkenazi, A.1
  • 3
    • 0034019382 scopus 로고    scopus 로고
    • In situ monitoring of caspase activation in hepatobiliary diseases
    • Bantel, H., Ruck, P., and Schulze-Osthoff, K. (2000). In situ monitoring of caspase activation in hepatobiliary diseases. Cell Death Differ. 7, 504-505.
    • (2000) Cell Death Differ. , vol.7 , pp. 504-505
    • Bantel, H.1    Ruck, P.2    Schulze-Osthoff, K.3
  • 4
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulin, C., Salvesen, G.S., and Oshima, R.G. (1997). Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. J. Cell Biol. 138, 1379-1394.
    • (1997) J. Cell Biol. , vol.138 , pp. 1379-1394
    • Caulin, C.1    Salvesen, G.S.2    Oshima, R.G.3
  • 5
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A.M., O'Rourke, K., Tewari, M., and Dixit, V.M. (1995). FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 81, 505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 6
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I
    • Coleman, M.L., Sahai, E.A., Yeo, M., Bosch, M., Dewar, A., and Olson, M.F. (2001). Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat. Cell Biol. 3, 339-345.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6
  • 7
    • 0034910509 scopus 로고    scopus 로고
    • Death receptor-induced apoptotic and necrotic cell death: Differential role of caspases and mitochondria
    • Denecker, G. et al. (2001). Death receptor-induced apoptotic and necrotic cell death: differential role of caspases and mitochondria. Cell Death Differ. 8, 829-840.
    • (2001) Cell Death Differ. , vol.8 , pp. 829-840
    • Denecker, G.1
  • 8
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L., and Wang, X. (2000). Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 9
    • 0034726959 scopus 로고    scopus 로고
    • The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program
    • Elliott, K., Ge, K., Du, W., and Prendergast, G.C. (2000). The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program. Oncogene 19, 4669-4684.
    • (2000) Oncogene , vol.19 , pp. 4669-4684
    • Elliott, K.1    Ge, K.2    Du, W.3    Prendergast, G.C.4
  • 11
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein, J.C., Waterhouse, N.J., Juin, P., Evan, G.I., and Green, D.R. (2000). The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2, 156-162.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5
  • 12
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green, D.R., and Evan, G.I. (2002). A matter of life and death. Cancer Cell 1, 19-30.
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 14
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D., and Weinberg, R.A. (2000). The hallmarks of cancer. Cell 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 15
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts IAP-caspase interaction
    • Hegde, R. et al. (2002). Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts IAP-caspase interaction. J. Biol. Chem. 277, 432-438.
    • (2002) J. Biol. Chem. , vol.277 , pp. 432-438
    • Hegde, R.1
  • 16
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M.O. (2000). The biochemistry of apoptosis. Nature 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 17
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation
    • Hsu, H., Xiong, J., and Goeddel, D.V. (1995). The TNF receptor 1-associated protein TRADD signals cell death and NF-kappa B activation. Cell 81, 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 18
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson, D.E. (2000). Noncaspase proteases in apoptosis. Leukemia 14, 1695-1703.
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 19
    • 0031753981 scopus 로고    scopus 로고
    • Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line
    • Jones, B., Roberts, P.J., Faubion, W.A., Kominami, E., and Gores, G.J. (1998). Cystatin A expression reduces bile salt-induced apoptosis in a rat hepatoma cell line. Am. J. Physiol. 275, G723-G730.
    • (1998) Am. J. Physiol. , vol.275
    • Jones, B.1    Roberts, P.J.2    Faubion, W.A.3    Kominami, E.4    Gores, G.J.5
  • 20
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist, M., and Jaattela, M. (2001a). Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell. Biol. 2, 589-598.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 21
    • 0035038613 scopus 로고    scopus 로고
    • Triggering of apoptosis by cathepsins
    • Leist, M., and Jaattela, M. (2001b). Triggering of apoptosis by cathepsins. Cell Death Differ. 8, 324-326.
    • (2001) Cell Death Differ. , vol.8 , pp. 324-326
    • Leist, M.1    Jaattela, M.2
  • 22
    • 0034682890 scopus 로고    scopus 로고
    • Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3
    • Li, H. et al. (2000). Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3. Science 289, 1159-1164.
    • (2000) Science , vol.289 , pp. 1159-1164
    • Li, H.1
  • 23
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L.Y., Luo, X., and Wang, X. (2001). Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412, 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 24
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S.M., Ahmad, M., Alnemri, E.S., and Wang, X. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
    • (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
  • 25
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo, X., Budihardjo, I., Zou, H., Slaughter, C., and Wang, X. (1998). Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94, 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 26
    • 0037016707 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif
    • Martins, L.M. et al. (2002). The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a Reaper-like motif. J. Biol. Chem. 277, 439-444.
    • (2002) J. Biol. Chem. , vol.277 , pp. 439-444
    • Martins, L.M.1
  • 27
    • 0031033274 scopus 로고    scopus 로고
    • Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes. DNA damage, or the Bcl-2 homologue Bak
    • McCarthy, N.J., Whyte, M.K., Gilbert, C.S., and Evan, G.I. (1997). Inhibition of Ced-3/ICE-related proteases does not prevent cell death induced by oncogenes, DNA damage, or the Bcl-2 homologue Bak. J. Cell Biol. 136, 215-227.
    • (1997) J. Cell Biol. , vol.136 , pp. 215-227
    • McCarthy, N.J.1    Whyte, M.K.2    Gilbert, C.S.3    Evan, G.I.4
  • 28
    • 0035135471 scopus 로고    scopus 로고
    • Measurement of caspase activity in individual cells reveals differences in the kinetics of caspase activation between cells
    • Morgan, M.J., and Thorburn, A. (2001). Measurement of caspase activity in individual cells reveals differences in the kinetics of caspase activation between cells. Cell Death Differ. 8, 38-43.
    • (2001) Cell Death Differ. , vol.8 , pp. 38-43
    • Morgan, M.J.1    Thorburn, A.2
  • 29
    • 0034743157 scopus 로고    scopus 로고
    • An apoptosis signaling pathway induced by the death domain of FADD selectively kills normal but not cancerous prostate epithelial cells
    • Morgan, M.J., Thorburn, J., Thomas, L., Maxwell, T., Brothman, A.R., and Thorburn, A. (2001). An apoptosis signaling pathway induced by the death domain of FADD selectively kills normal but not cancerous prostate epithelial cells. Cell Death Differ. 8, 696-705.
    • (2001) Cell Death Differ. , vol.8 , pp. 696-705
    • Morgan, M.J.1    Thorburn, J.2    Thomas, L.3    Maxwell, T.4    Brothman, A.R.5    Thorburn, A.6
  • 30
    • 85047697089 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) triggers apoptosis in normal prostate epithelial cells
    • Nesterov, A., Ivashchenko, Y., and Kraft, A.S. (2002). Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) triggers apoptosis in normal prostate epithelial cells. Oncogene 21, 1135-1140.
    • (2002) Oncogene , vol.21 , pp. 1135-1140
    • Nesterov, A.1    Ivashchenko, Y.2    Kraft, A.S.3
  • 31
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D.W. (1999). Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6, 1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 34
    • 0032535018 scopus 로고    scopus 로고
    • Fas-mediated apoptosis in human prostatic carcinoma cell lines occurs via activation of caspase-8 and caspase-7
    • Rokhlin, O.W., Glover, R.A., and Cohen, M.B. (1998). Fas-mediated apoptosis in human prostatic carcinoma cell lines occurs via activation of caspase-8 and caspase-7. Cancer Res. 58, 5870-5875.
    • (1998) Cancer Res. , vol.58 , pp. 5870-5875
    • Rokhlin, O.W.1    Glover, R.A.2    Cohen, M.B.3
  • 35
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen, G.S., and Dixit, V.M. (1999). Caspase activation: the induced-proximity model. Proc. Natl. Acad. Sci. USA 96, 10964-10967.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 36
  • 37
    • 0035075597 scopus 로고    scopus 로고
    • Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
    • Sebbagh, M., Renvoize, C., Hamelin, J., Riche, N., Bertoglio, J., and Breard, J. (2001). Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat. Cell Biol. 3, 346-352.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 346-352
    • Sebbagh, M.1    Renvoize, C.2    Hamelin, J.3    Riche, N.4    Bertoglio, J.5    Breard, J.6
  • 38
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis: Cleavage of bid, not Pro-caspases, is the most likely route
    • Stoka, V. et al. (2001). Lysosomal protease pathways to apoptosis: cleavage of bid, not Pro-caspases, is the most likely route. J. Biol. Chem. 276, 3149-3157.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3149-3157
    • Stoka, V.1
  • 39
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S.A. et al. (1999). Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397, 441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 40
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, htra2, is released from the mitochondria and interacts with xiap, inducing cell death
    • Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., and Takahashi, R. (2001). A serine protease, htra2, is released from the mitochondria and interacts with xiap, inducing cell death. Mol. Cell 8, 613-621.
    • (2001) Mol. Cell. , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 41
    • 0037072933 scopus 로고    scopus 로고
    • Regulation of FADD death domain interactions by the death effector domain identified by a modified reverse two hybrid screen
    • Thomas, L., Stillman, D., and Thorburn, A. (2002). Regulation of FADD death domain interactions by the death effector domain identified by a modified reverse two hybrid screen. J. Biol. Chem. 277, 34343-34348.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34343-34348
    • Thomas, L.1    Stillman, D.2    Thorburn, A.3
  • 42
    • 0033198121 scopus 로고    scopus 로고
    • Germinal center B cell apoptosis requires both caspase and cathepsin activity
    • van Eijk, M., and de Groot, C. (1999). Germinal center B cell apoptosis requires both caspase and cathepsin activity. J. Immunol. 163, 2478-2482.
    • (1999) J. Immunol. , vol.163 , pp. 2478-2482
    • Van Eijk, M.1    De Groot, C.2
  • 43
    • 18244386261 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity
    • van Loo, G. et al. (2002). The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity. Cell Death Differ. 9, 20-26.
    • (2002) Cell Death Differ. , vol.9 , pp. 20-26
    • Van Loo, G.1
  • 46
  • 47
    • 0037016686 scopus 로고    scopus 로고
    • HtrA2 promotes cell death through its serine protease activity and its ability to antagonise inhibitor of apoptosis proteins
    • Verhagen, A.M et al. (2002). HtrA2 promotes cell death through its serine protease activity and its ability to antagonise inhibitor of apoptosis proteins. J. Biol. Chem. 277, 445-454.
    • (2002) J. Biol. Chem. , vol.277 , pp. 445-454
    • Verhagen, A.M.1
  • 49
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak, H. et al. (1999). Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat. Med. 5, 157-163.
    • (1999) Nat. Med. , vol.5 , pp. 157-163
    • Walczak, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.