메뉴 건너뛰기




Volumn 3, Issue 115, 2010, Pages

The role of the kinases RIP1 and RIP3 in TNF-induced necrosis

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; LIPOXYGENASE; OXIDOREDUCTASE; PHOSPHOLIPASE A2; PROTEIN RIP 1; PROTEIN RIP 3; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SPHINGOMYELIN PHOSPHODIESTERASE; TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; HRB PROTEIN, HUMAN; NUCLEOPORIN; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK3 PROTEIN, HUMAN; RNA BINDING PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN;

EID: 77953672526     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.3115re4     Document Type: Review
Times cited : (370)

References (103)
  • 1
    • 67349162130 scopus 로고    scopus 로고
    • Tumour necrosis factor and cancer
    • F. Balkwill, Tumour necrosis factor and cancer. Nat. Rev. Cancer 9, 361-371 (2009).
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 361-371
    • Balkwill, F.1
  • 4
    • 0000161413 scopus 로고
    • The treatment of malignant tumors by repeated inoculations of erysipelas: With a report of ten original cases
    • W. B. Coley, The treatment of malignant tumors by repeated inoculations of erysipelas: With a report of ten original cases. Am. J. Med. Sci. 105, 487-511 (1893).
    • (1893) Am. J. Med. Sci. , vol.105 , pp. 487-511
    • Coley, W.B.1
  • 6
    • 45349112005 scopus 로고
    • Cytokines as communication signals between leukocytes and endothelial cells
    • A. Mantovani, E. Dejana, Cytokines as communication signals between leukocytes and endothelial cells. Immunol. Today 10, 370-375 (1989).
    • (1989) Immunol. Today , vol.10 , pp. 370-375
    • Mantovani, A.1    Dejana, E.2
  • 7
    • 55849089267 scopus 로고    scopus 로고
    • Many cytokines are very useful therapeutic targets in disease
    • M. Feldmann, Many cytokines are very useful therapeutic targets in disease. J. Clin. Invest. 118, 3533-3536 (2008).
    • (2008) J. Clin. Invest. , vol.118 , pp. 3533-3536
    • Feldmann, M.1
  • 9
    • 70350719371 scopus 로고    scopus 로고
    • TNF-alpha as a therapeutic target in inflammatory diseases, ischemia-reperfusion injury and trauma
    • E. Esposito, S. Cuzzocrea, TNF-alpha as a therapeutic target in inflammatory diseases, ischemia-reperfusion injury and trauma. Curr. Med. Chem. 16, 3152-3167 (2009).
    • (2009) Curr. Med. Chem. , vol.16 , pp. 3152-3167
    • Esposito, E.1    Cuzzocrea, S.2
  • 10
    • 0023954297 scopus 로고
    • Cachectin (tumor necrosis factor): A macrophage hormone governing cellular metabolism and inflammatory response
    • B. Beutler, A. Cerami, Cachectin (tumor necrosis factor): A macrophage hormone governing cellular metabolism and inflammatory response. Endocr. Rev. 9, 57-66 (1988).
    • (1988) Endocr. Rev. , vol.9 , pp. 57-66
    • Beutler, B.1    Cerami, A.2
  • 11
    • 0033576675 scopus 로고    scopus 로고
    • More than one way to die: Apoptosis, necrosis and reactive oxygen damage
    • W. Fiers, R. Beyaert, W. Declercq, P. Vandenabeele, More than one way to die: Apoptosis, necrosis and reactive oxygen damage. Oncogene 18, 7719-7730 (1999).
    • (1999) Oncogene , vol.18 , pp. 7719-7730
    • Fiers, W.1    Beyaert, R.2    Declercq, W.3    Vandenabeele, P.4
  • 12
    • 0033188158 scopus 로고    scopus 로고
    • Regulation of tumor necrosis factor-induced, mitochondria- and reactive oxygen species-dependent cell death by the electron flux through the electron transport chain complex I
    • V. Goossens, G. Stangé, K. Moens, D. Pipeleers, J. Grooten, Regulation of tumor necrosis factor-induced, mitochondria- and reactive oxygen species-dependent cell death by the electron flux through the electron transport chain complex I. Antioxid. Redox Signal. 1, 285-295 (1999).
    • (1999) Antioxid. Redox Signal , vol.1 , pp. 285-295
    • Goossens, V.1    Stangé, G.2    Moens, K.3    Pipeleers, D.4    Grooten, J.5
  • 13
    • 58149464289 scopus 로고    scopus 로고
    • The Jekyll and Hyde functions of caspases
    • C. H. Yi, J. Yuan, The Jekyll and Hyde functions of caspases. Dev. Cell 16, 21-34 (2009).
    • (2009) Dev. Cell. , vol.16 , pp. 21-34
    • Yi, C.H.1    Yuan, J.2
  • 14
    • 33749178260 scopus 로고    scopus 로고
    • Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response
    • N. Festjens, T. Vanden Berghe, P. Vandenabeele, Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response. Biochim. Biophys. Acta 1757, 1371-1387 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1    Berghe, T.V.2    Vandenabeele, P.3
  • 17
    • 0031282499 scopus 로고    scopus 로고
    • Tumour necrosis factorinduced necrosis versus anti-Fas-induced apoptosis in L929 cells
    • D. Vercammen, P. Vandenabeele, R. Beyaert, W. Declercq, W. Fiers, Tumour necrosis factorinduced necrosis versus anti-Fas-induced apoptosis in L929 cells. Cytokine 9, 801-808 (1997).
    • (1997) Cytokine , vol.9 , pp. 801-808
    • Vercammen, D.1    Vandenabeele, P.2    Beyaert, R.3    Declercq, W.4    Fiers, W.5
  • 19
    • 0347065342 scopus 로고    scopus 로고
    • A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses
    • F. K. Chan, J. Shisler, J. G. Bixby, M. Felices, L. Zheng, M. Appel, J. Orenstein, B. Moss, M. J. Lenardo, A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses. J. Biol. Chem. 278, 51613-51621 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51613-51621
    • Chan, F.K.1    Shisler, J.2    Bixby, J.G.3    Felices, M.4    Zheng, L.5    Appel, M.6    Orenstein, J.7    Moss, B.8    Lenardo, M.J.9
  • 21
    • 0033970831 scopus 로고    scopus 로고
    • Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/caspase-8 death signaling pathway
    • S. Balachandran, P. C. Roberts, T. Kipperman, K. N. Bhalla, R. W. Compans, D. R. Archer, G. N. Barber, Alpha/beta interferons potentiate virus-induced apoptosis through activation of the FADD/caspase-8 death signaling pathway. J. Virol. 74, 1513-1523 (2000).
    • (2000) J. Virol. , vol.74 , pp. 1513-1523
    • Balachandran, S.1    Roberts, P.C.2    Kipperman, T.3    Bhalla, K.N.4    Compans, R.W.5    Archer, D.R.6    Barber, G.N.7
  • 22
    • 0036715377 scopus 로고    scopus 로고
    • Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA
    • M. Kalai, G. Van Loo, T. Vanden Berghe, A. Meeus, W. Burm, X. Saelens, P. Vandenabeele, Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA. Cell Death Differ. 9, 981-994 (2002).
    • (2002) Cell. Death Differ , vol.9 , pp. 981-994
    • Kalai, M.1    Van Loo, G.2    Berghe, T.V.3    Meeus, A.4    Burm, W.5    Saelens, X.6    Vandenabeele, P.7
  • 23
    • 29644433629 scopus 로고    scopus 로고
    • NF-kappaB protects macrophages from lipopolysaccharide induced cell death: The role of caspase 8 and receptor-interacting protein
    • Y. Ma, V. Temkin, H. Liu, R. M. Pope, NF-kappaB protects macrophages from lipopolysaccharide induced cell death: The role of caspase 8 and receptor-interacting protein. J. Biol. Chem. 280, 41827-41834 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 41827-41834
    • Ma, Y.1    Temkin, V.2    Liu, H.3    Pope, R.M.4
  • 26
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: Crucial integrators of cellular stress
    • E. Meylan, J. Tschopp, The RIP kinases: Crucial integrators of cellular stress. Trends Biochem. Sci. 30, 151-159 (2005).
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 27
    • 33847051539 scopus 로고    scopus 로고
    • RIP1, a kinase on the crossroads of a cell's decision to live or die
    • N. Festjens, T. Vanden Berghe, S. Cornelis, P. Vandenabeele, RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ. 14, 400-410 (2007).
    • (2007) Cell. Death Differ , vol.14 , pp. 400-410
    • Festjens, N.1    Berghe, T.V.2    Cornelis, S.3    Vandenabeele, P.4
  • 29
    • 84954358195 scopus 로고    scopus 로고
    • Necroptosis contributes to the NMDA-induced excitotoxicity in rat's cultured cortical neurons
    • Y. Li, X. Yang, C. Ma, J. Qiao, C. Zhang, Necroptosis contributes to the NMDA-induced excitotoxicity in rat's cultured cortical neurons. Neurosci. Lett. 447, 120-123 (2008).
    • (2008) Neurosci. Lett. , vol.447 , pp. 120-123
    • Li, Y.1    Yang, X.2    Ma, C.3    Qiao, J.4    Zhang, C.5
  • 30
    • 34250748014 scopus 로고    scopus 로고
    • Shikonin circumvents cancer drug resistance by induction of a necroptotic death
    • W. Han, L. Li, S. Qiu, Q. Lu, Q. Pan, Y. Gu, J. Luo, X. Hu, Shikonin circumvents cancer drug resistance by induction of a necroptotic death. Mol. Cancer Ther. 6, 1641-1649 (2007).
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 1641-1649
    • Han, W.1    Li, L.2    Qiu, S.3    Lu, Q.4    Pan, Q.5    Gu, Y.6    Luo, J.7    Hu, X.8
  • 31
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • F. K. Chan, H. J. Chun, L. Zheng, R. M. Siegel, K. L. Bui, M. J. Lenardo, A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 288, 2351-2354 (2000).
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.1    Chun, H.J.2    Zheng, L.3    Siegel, R.M.4    Bui, K.L.5    Lenardo, M.J.6
  • 32
    • 0030447483 scopus 로고    scopus 로고
    • The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex
    • H. B. Shu, M. Takeuchi, D. V. Goeddel, The tumor necrosis factor receptor 2 signal transducers TRAF2 and c-IAP1 are components of the tumor necrosis factor receptor 1 signaling complex. Proc. Natl. Acad. Sci. U. S. A. 93, 13973-13978 (1996).
    • (1996) Proc. Natl. Acad. Sci. U. S. A , vol.93 , pp. 13973-13978
    • Shu, H.B.1    Takeuchi, M.2    Goeddel, D.V.3
  • 33
    • 0029595282 scopus 로고
    • The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
    • M. Rothe, M. G. Pan, W. J. Henzel, T. M. Ayres, D. V. Goeddel, The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins. Cell 83, 1243-1252 (1995).
    • (1995) Cell. , vol.83 , pp. 1243-1252
    • Rothe, M.1    Pan, M.G.2    Henzel, W.J.3    Ayres, T.M.4    Goeddel, D.V.5
  • 34
    • 68949086679 scopus 로고    scopus 로고
    • Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2
    • R. A. Csomos, G. F. Brady, C. S. Duckett, Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2. J. Biol. Chem. 284, 20531-20539 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 20531-20539
    • Csomos, R.A.1    Brady, G.F.2    Duckett, C.S.3
  • 36
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • C. K. Ea, L. Deng, Z. P. Xia, G. Pineda, Z. J. Chen, Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol. Cell 22, 245-257 (2006).
    • (2006) Mol. Cell. , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3    Pineda, G.4    Chen, Z.J.5
  • 40
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • O. Micheau, J. Tschopp, Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114, 181-190 (2003).
    • (2003) Cell. , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 42
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • S. He, L. Wang, L. Miao, T. Wang, F. Du, L. Zhao, X. Wang, Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 137, 1100-1111 (2009).
    • (2009) Cell. , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6    Wang, X.7
  • 43
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Y. S. Cho, S. Challa, D. Moquin, R. Genga, T. D. Ray, M. Guildford, F. K. Chan, Phosphorylation driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 137, 1112-1123 (2009).
    • (2009) Cell. , vol.137 , pp. 1112-1123
    • Cho, Y.S.1    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6    Chan, F.K.7
  • 44
    • 77449150629 scopus 로고    scopus 로고
    • CYLD: A tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
    • S. C. Sun, CYLD: A tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes. Cell Death Differ. 17, 25-34 (2010).
    • (2010) Cell. Death Differ , vol.17 , pp. 25-34
    • Sun, S.C.1
  • 45
    • 62849093368 scopus 로고    scopus 로고
    • Death receptor signal transducers: Nodes of coordination in immune signaling networks
    • N. S. Wilson, V. Dixit, A. Ashkenazi, Death receptor signal transducers: Nodes of coordination in immune signaling networks. Nat. Immunol. 10, 348-355 (2009).
    • (2009) Nat. Immunol. , vol.10 , pp. 348-355
    • Wilson, N.S.1    Dixit, V.2    Ashkenazi, A.3
  • 46
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • L. Wang, F. Du, X. Wang, TNF-alpha induces two distinct caspase-8 activation pathways. Cell 133, 693-703 (2008).
    • (2008) Cell. , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 47
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • S. Feng, Y. Yang, Y. Mei, L. Ma, D. E. Zhu, N. Hoti, M. Castanares, M. Wu, Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell. Signal. 19, 2056-2067 (2007).
    • (2007) Cell. Signal , vol.19 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 49
    • 1642299768 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation
    • Y. Lin, S. Choksi, H. M. Shen, Q. F. Yang, G. M. Hur, Y. S. Kim, J. H. Tran, S. A. Nedospasov, Z. G. Liu, Tumor necrosis factor-induced nonapoptotic cell death requires receptor-interacting protein-mediated cellular reactive oxygen species accumulation. J. Biol. Chem. 279, 10822-10828 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 10822-10828
    • Lin, Y.1    Choksi, S.2    Shen, H.M.3    Yang, Q.F.4    Hur, G.M.5    Kim, Y.S.6    Tran, J.H.7    Nedospasov, S.A.8    Liu, Z.G.9
  • 51
    • 50149089360 scopus 로고    scopus 로고
    • The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors
    • Y. L. Pobezinskaya, Y. S. Kim, S. Choksi, M. J. Morgan, T. Li, C. Liu, Z. Liu, The function of TRADD in signaling through tumor necrosis factor receptor 1 and TRIF-dependent Toll-like receptors. Nat. Immunol. 9, 1047-1054 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 1047-1054
    • Pobezinskaya, Y.L.1    Kim, Y.S.2    Choksi, S.3    Morgan, M.J.4    Li, T.5    Liu, C.6    Liu, Z.7
  • 52
    • 57649181391 scopus 로고    scopus 로고
    • Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway
    • J. Hitomi, D. E. Christofferson, A. Ng, J. Yao, A. Degterev, R. J. Xavier, J. Yuan, Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway. Cell 135, 1311-1323 (2008).
    • (2008) Cell. , vol.135 , pp. 1311-1323
    • Hitomi, J.1    Christofferson, D.E.2    Ng, A.3    Yao, J.4    Degterev, A.5    Xavier, R.J.6    Yuan, J.7
  • 53
    • 65549085701 scopus 로고    scopus 로고
    • Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling
    • Z. Jin, Y. Li, R. Pitti, D. Lawrence, V. C. Pham, J. R. Lill, A. Ashkenazi, Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling. Cell 137, 721-735 (2009).
    • (2009) Cell. , vol.137 , pp. 721-735
    • Jin, Z.1    Li, Y.2    Pitti, R.3    Lawrence, D.4    Pham, V.C.5    Lill, J.R.6    Ashkenazi, A.7
  • 54
    • 69449095860 scopus 로고    scopus 로고
    • Caspases and kinases in a death grip
    • M. Kurokawa, S. Kornbluth, Caspases and kinases in a death grip. Cell 138, 838-854 (2009).
    • (2009) Cell. , vol.138 , pp. 838-854
    • Kurokawa, M.1    Kornbluth, S.2
  • 55
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • D.-W. Zhang, J. Shao, J. Lin, N. Zhang, B.-J. Lu, S.-C. Lin, M.-Q. Dong, J. Han, RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325, 332-336 (2009).
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.-W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.-J.5    Lin, S.-C.6    Dong, M.-Q.7    Han, J.8
  • 56
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • T. H. Lee, J. Shank, N. Cusson, M. A. Kelliher, The kinase activity of Rip1 is not required for tumor necrosis factor-alpha-induced IkappaB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279, 33185-33191 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 33185-33191
    • Lee, T.H.1    Shank, J.2    Cusson, N.3    Kelliher, M.A.4
  • 57
    • 0842304221 scopus 로고    scopus 로고
    • Kinase RIP3 is dispensable for normal NF-kappa Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4
    • K. Newton, X. Sun, V. M. Dixit, Kinase RIP3 is dispensable for normal NF-kappa Bs, signaling by the B-cell and T-cell receptors, tumor necrosis factor receptor 1, and Toll-like receptors 2 and 4. Mol. Cell. Biol. 24, 1464-1469 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1464-1469
    • Newton, K.1    Sun, X.2    Dixit, V.M.3
  • 59
    • 0029090167 scopus 로고
    • Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity
    • V. Goossens, J. Grooten, K. De Vos, W. Fiers, Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity. Proc. Natl. Acad. Sci. U. S. A. 92, 8115-8119 (1995).
    • (1995) Proc. Natl. Acad. Sci. U. S. A , vol.92 , pp. 8115-8119
    • Goossens, V.1    Grooten, J.2    De Vos, K.3    Fiers, W.4
  • 60
    • 0026713818 scopus 로고
    • Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation
    • K. Schulze-Osthoff, A. C. Bakker, B. Vanhaesebroeck, R. Beyaert, W. A. Jacob, W. Fiers, Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation. J. Biol. Chem. 267, 5317-5323 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 5317-5323
    • Schulze-Osthoff, K.1    Bakker, A.C.2    Vanhaesebroeck, B.3    Beyaert, R.4    Jacob, W.A.5    Fiers, W.6
  • 61
    • 34249820757 scopus 로고    scopus 로고
    • TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death
    • Y. S. Kim, M. J. Morgan, S. Choksi, Z. G. Liu, TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death. Mol. Cell 26, 675-687 (2007).
    • (2007) Mol. Cell. , vol.26 , pp. 675-687
    • Kim, Y.S.1    Morgan, M.J.2    Choksi, S.3    Liu, Z.G.4
  • 64
    • 5444269110 scopus 로고    scopus 로고
    • The cellular fate of glucose and its relevance in type 2 diabetes
    • C. Bouché, S. Serdy, C. R. Kahn, A. B. Goldfine, The cellular fate of glucose and its relevance in type 2 diabetes. Endocr. Rev. 25, 807-830 (2004).
    • (2004) Endocr. Rev. , vol.25 , pp. 807-830
    • Bouché, C.1    Serdy, S.2    Kahn, C.R.3    Goldfine, A.B.4
  • 66
    • 33750608704 scopus 로고    scopus 로고
    • Glutamine: A Trojan horse in ammonia neurotoxicity
    • J. Albrecht, M. D. Norenberg, Glutamine: A Trojan horse in ammonia neurotoxicity. Hepatology 44, 788-794 (2006).
    • (2006) Hepatology , vol.44 , pp. 788-794
    • Albrecht, J.1    Norenberg, M.D.2
  • 67
    • 0030028069 scopus 로고    scopus 로고
    • The oxidative metabolism of glutamine. A modulator of reactive oxygen intermediate-mediated cytotoxicity of tumor necrosis factor in L929 fibrosarcoma cells
    • V. Goossens, J. Grooten, W. Fiers, The oxidative metabolism of glutamine. A modulator of reactive oxygen intermediate-mediated cytotoxicity of tumor necrosis factor in L929 fibrosarcoma cells. J. Biol. Chem. 271, 192-196 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 192-196
    • Goossens, V.1    Grooten, J.2    Fiers, W.3
  • 68
    • 36849056027 scopus 로고    scopus 로고
    • The cardioprotective effect of necrostatin requires the cyclophilin-D component of the mitochondrial permeability transition pore
    • S. Y. Lim, S. M. Davidson, M. M. Mocanu, D. M. Yellon, C. C. Smith, The cardioprotective effect of necrostatin requires the cyclophilin-D component of the mitochondrial permeability transition pore. Cardiovasc. Drugs Ther. 21, 467-469 (2007).
    • (2007) Cardiovasc. Drugs Ther. , vol.21 , pp. 467-469
    • Lim, S.Y.1    Davidson, S.M.2    Mocanu, M.M.3    Yellon, D.M.4    Smith, C.C.5
  • 70
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal
    • S. A. Phillips, P. J. Thornalley, The formation of methylglyoxal from triose phosphates. Investigation using a specific assay for methylglyoxal. Eur. J. Biochem. 212, 101-105 (1993).
    • (1993) Eur. J. Biochem. , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 71
    • 0037154172 scopus 로고    scopus 로고
    • Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE
    • F. Van Herreweghe, J. Mao, F. W. Chaplen, J. Grooten, K. Gevaert, J. Vandekerckhove, K. Vancompernolle, Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE. Proc. Natl. Acad. Sci. U. S. A. 99, 949-954 (2002).
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 949-954
    • Van Herreweghe, F.1    Mao, J.2    Chaplen, F.W.3    Grooten, J.4    Gevaert, K.5    Vandekerckhove, J.6    Vancompernolle, K.7
  • 72
    • 53849092368 scopus 로고    scopus 로고
    • Dicarbonyls linked to damage in the powerhouse: Glycation of mitochondrial proteins and oxidative stress
    • N. Rabbani, P. J. Thornalley, Dicarbonyls linked to damage in the powerhouse: Glycation of mitochondrial proteins and oxidative stress. Biochem. Soc. Trans. 36, 1045-1050 (2008).
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1045-1050
    • Rabbani, N.1    Thornalley, P.J.2
  • 75
    • 0036022402 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase-1 cleavage during apoptosis: An update
    • C. Soldani, A. I. Scovassi, Poly (ADP-ribose) polymerase-1 cleavage during apoptosis: An update. Apoptosis 7, 321-328 (2002).
    • (2002) Apoptosis , vol.7 , pp. 321-328
    • Soldani, C.1    Scovassi, A.I.2
  • 76
    • 63849124057 scopus 로고    scopus 로고
    • The molecular "Jekyll and Hyde" duality of PARP1 in cell death and cell survival
    • P. O. Hassa, The molecular "Jekyll and Hyde" duality of PARP1 in cell death and cell survival. Front. Biosci. 14, 72-111 (2009).
    • (2009) Front. Biosci. , vol.14 , pp. 72-111
    • Hassa, P.O.1
  • 77
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: Chromatin modulation, enhancer-binding, coregulation, and insulation
    • W. L. Kraus, Transcriptional control by PARP-1: Chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 20, 294-302 (2008).
    • (2008) Curr. Opin. Cell. Biol. , vol.20 , pp. 294-302
    • Kraus, W.L.1
  • 78
    • 0036196425 scopus 로고    scopus 로고
    • Activation and caspasemediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling
    • M. Los, M. Mozoluk, D. Ferrari, A. Stepczynska, C. Stroh, A. Renz, Z. Herceg, Z. Q. Wang, K. Schulze-Osthoff, Activation and caspasemediated inhibition of PARP: A molecular switch between fibroblast necrosis and apoptosis in death receptor signaling. Mol. Biol. Cell 13, 978-988 (2002).
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 978-988
    • Los, M.1    Mozoluk, M.2    Ferrari, D.3    Stepczynska, A.4    Stroh, C.5    Renz, A.6    Herceg, Z.7    Wang, Z.Q.8    Schulze-Osthoff, K.9
  • 79
    • 2442624618 scopus 로고    scopus 로고
    • Poly (ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition
    • C. C. Alano, W. Ying, R. A. Swanson, Poly (ADP-ribose) polymerase-1-mediated cell death in astrocytes requires NAD+ depletion and mitochondrial permeability transition. J. Biol. Chem. 279, 18895-18902 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 18895-18902
    • Alano, C.C.1    Ying, W.2    Swanson, R.A.3
  • 80
    • 33646827842 scopus 로고    scopus 로고
    • Poly (ADPribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation
    • Y. Xu, S. Huang, Z. G. Liu, J. Han, Poly (ADPribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation. J. Biol. Chem. 281, 8788-8795 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8788-8795
    • Xu, Y.1    Huang, S.2    Liu, Z.G.3    Han, J.4
  • 81
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • M. Leist, B. Single, A. F. Castoldi, S. Kühnle, P. Nicotera, Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis. J. Exp. Med. 185, 1481-1486 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kühnle, S.4    Nicotera, P.5
  • 82
    • 0033563776 scopus 로고    scopus 로고
    • Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis
    • M. Leist, B. Single, H. Naumann, E. Fava, B. Simon, S. Kühnle, P. Nicotera, Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis. Exp. Cell Res. 249, 396-403 (1999).
    • (1999) Exp. Cell. Res. , vol.249 , pp. 396-403
    • Leist, M.1    Single, B.2    Naumann, H.3    Fava, E.4    Simon, B.5    Kühnle, S.6    Nicotera, P.7
  • 83
    • 33644763298 scopus 로고    scopus 로고
    • Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis
    • V. Temkin, Q. Huang, H. Liu, H. Osada, R. M. Pope, Inhibition of ADP/ATP exchange in receptor-interacting protein-mediated necrosis. Mol. Cell. Biol. 26, 2215-2225 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2215-2225
    • Temkin, V.1    Huang, Q.2    Liu, H.3    Osada, H.4    Pope, R.M.5
  • 84
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase A2 structure/function, mechanism, and signaling
    • J. E. Burke, E. A. Dennis, Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res. 50 (suppl.), S237-S242 (2009).
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Burke, J.E.1    Dennis, E.A.2
  • 85
    • 0026100924 scopus 로고
    • Tumournecrosis factor-mediated cytotoxicity is correlated with phospholipase-A2 activity, but not with arachidonic acid release per se
    • P. Suffys, R. Beyaert, D. De Valck, B. Vanhaesebroeck, F. Van Roy, W. Fiers, Tumournecrosis factor-mediated cytotoxicity is correlated with phospholipase-A2 activity, but not with arachidonic acid release per se. Eur. J. Biochem. 195, 465-475 (1991).
    • (1991) Eur. J. Biochem. , vol.195 , pp. 465-475
    • Suffys, P.1    Beyaert, R.2    De Valck, D.3    Vanhaesebroeck, B.4    Van Roy, F.5    Fiers, W.6
  • 86
    • 0034671967 scopus 로고    scopus 로고
    • Resistance to TNF-induced cytotoxicity correlates with an abnormal cleavage of cytosolic phospholipase A2
    • N. E. El Mahdani, M. Ameyar, Z. Cai, O. Colard, J. Masliah, S. Chouaib, Resistance to TNF-induced cytotoxicity correlates with an abnormal cleavage of cytosolic phospholipase A2. J. Immunol. 165, 6756-6761 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 6756-6761
    • El Mahdani, N.E.1    Ameyar, M.2    Cai, Z.3    Colard, O.4    Masliah, J.5    Chouaib, S.6
  • 87
    • 0036249657 scopus 로고    scopus 로고
    • 15-lipoxygenase-1: A prooxidant enzyme
    • T. Schewe, 15-lipoxygenase-1: A prooxidant enzyme. Biol. Chem. 383, 365-374 (2002).
    • (2002) Biol. Chem. , vol.383 , pp. 365-374
    • Schewe, T.1
  • 88
    • 54949137644 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death
    • P. Boya, G. Kroemer, Lysosomal membrane permeabilization in cell death. Oncogene 27, 6434-6451 (2008).
    • (2008) Oncogene , vol.27 , pp. 6434-6451
    • Boya, P.1    Kroemer, G.2
  • 89
    • 0037386245 scopus 로고    scopus 로고
    • Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2
    • DOI 10.1038/ni914
    • A. Cauwels, B. Janssen, A. Waeytens, C. Cuvelier, P. Brouckaert, Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2. Nat. Immunol. 4, 387-393 (2003). (Pubitemid 36432323)
    • (2003) Nature Immunology , vol.4 , Issue.4 , pp. 387-393
    • Cauwels, A.1    Janssen, B.2    Waeytens, A.3    Cuvelier, C.4    Brouckaert, P.5
  • 90
    • 0347363475 scopus 로고    scopus 로고
    • PLA2 activity is required for nuclear shrinkage in caspase independent caspase independent cell death
    • K. Shinzawa, Y. Tsujimoto, PLA2 activity is required for nuclear shrinkage in caspase independent caspase independent cell death. J. Cell Biol. 163, 1219-1230 (2003).
    • (2003) J. Cell. Biol. , vol.163 , pp. 1219-1230
    • Shinzawa, K.1    Tsujimoto, Y.2
  • 91
    • 33646589316 scopus 로고    scopus 로고
    • Sphingolipid signaling and redox regulation
    • J. S. Won, I. Singh, Sphingolipid signaling and redox regulation. Free Radic. Biol. Med. 40, 1875-1888 (2006).
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1875-1888
    • Won, J.S.1    Singh, I.2
  • 93
    • 33646589316 scopus 로고    scopus 로고
    • Sphingolipid signaling and redox regulation
    • J. S. Won, I. Singh, Sphingolipid signaling and redox regulation. Free Radic. Biol. Med. 40, 1875-1888 (2006).
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1875-1888
    • Won, J.S.1    Singh, I.2
  • 94
    • 0035201812 scopus 로고    scopus 로고
    • Resistance to tumor necrosis factor-induced cell death mediated by PMCA4 deficiency
    • DOI 10.1128/MCB.21.24.8276-8288.2001
    • K. Ono, X. Wang, J. Han, Resistance to tumor necrosis factor-induced cell death mediated by PMCA4 deficiency. Mol. Cell. Biol. 21, 8276-8288 (2001). (Pubitemid 33108589)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.24 , pp. 8276-8288
    • Ono, K.1    Wang, X.2    Han, J.3
  • 95
    • 0037223288 scopus 로고    scopus 로고
    • Susceptibility of lysosomes to rupture is a determinant for plasma membrane disruption in tumor necrosis factor alpha-induced cell death
    • K. Ono, S. O. Kim, J. Han, Susceptibility of lysosomes to rupture is a determinant for plasma membrane disruption in tumor necrosis factor alpha-induced cell death. Mol. Cell. Biol. 23, 665-676 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 665-676
    • Ono, K.1    Kim, S.O.2    Han, J.3
  • 96
    • 47849120473 scopus 로고    scopus 로고
    • Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
    • F. Meissner, K. Molawi, A. Zychlinsky, Superoxide dismutase 1 regulates caspase-1 and endotoxic shock. Nat. Immunol. 9, 866-872 (2008).
    • (2008) Nat. Immunol. , vol.9 , pp. 866-872
    • Meissner, F.1    Molawi, K.2    Zychlinsky, A.3
  • 97
    • 53849136625 scopus 로고    scopus 로고
    • Viral subversion of apoptotic enzymes: Escape from death row
    • S. M. Best, Viral subversion of apoptotic enzymes: Escape from death row. Annu. Rev. Microbiol. 62, 171-192 (2008).
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 171-192
    • Best, S.M.1
  • 98
    • 0030722084 scopus 로고    scopus 로고
    • Antiviral activity of tumor necrosis factor (TNF) is mediated via p55 and p75 TNF receptors
    • J. Ruby, H. Bluethmann, J. J. Peschon, Antiviral activity of tumor necrosis factor (TNF) is mediated via p55 and p75 TNF receptors. J. Exp. Med. 186, 1591-1596 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1591-1596
    • Ruby, J.1    Bluethmann, H.2    Peschon, J.J.3
  • 100
    • 47749133767 scopus 로고    scopus 로고
    • Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1
    • J. W. Upton, W. J. Kaiser, E. S. Mocarski, Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1. J. Biol. Chem. 283, 16966-16970 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 16966-16970
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 101
    • 42949111649 scopus 로고    scopus 로고
    • Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein
    • C. Mack, A. Sickmann, D. Lembo, W. Brune, Inhibition of proinflammatory and innate immune signaling pathways by a cytomegalovirus RIP1-interacting protein. Proc. Natl. Acad. Sci. U. S. A. 105, 3094-3099 (2008).
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , pp. 3094-3099
    • Mack, C.1    Sickmann, A.2    Lembo, D.3    Brune, W.4
  • 102
    • 77953856662 scopus 로고    scopus 로고
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr
    • Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P, Pro; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; W, Trp; and Y, Tyr.
  • 103
    • 77953821408 scopus 로고    scopus 로고
    • Acknowledgments: We thank A. Bredan for editing and N. Takahashi for critically reading the manuscript. We apologize to the many authors whose original work could not be cited due to reference limitations. Funding: This research has been supported by VIB, Ghent University, Framework Programme 6 FP6 ApopTrain, MRTN-CT-035624; FP6 Epistem, LSHB-CT-2005-019067; Apo-Sys FP7-200767, IAP 6/18, Research Foundation Flanders FWO-Vlaanderen 3G.0218.06 and G.0226.09 and Flemish Special Research Fund-Concerted Research Actions BOFGOA 12.0505.02. T. V. B. holds a grant of the FWO and P. V. holds a Methusalem grant from the Flemish Government
    • Acknowledgments: We thank A. Bredan for editing and N. Takahashi for critically reading the manuscript. We apologize to the many authors whose original work could not be cited due to reference limitations. Funding: This research has been supported by VIB, Ghent University, Framework Programme 6 (FP6) ApopTrain, MRTN-CT-035624; FP6 Epistem, LSHB-CT-2005-019067; Apo-Sys FP7-200767, IAP 6/18, Research Foundation Flanders (FWO-Vlaanderen) (3G.0218.06 and G.0226.09) and Flemish Special Research Fund-Concerted Research Actions BOFGOA 12.0505.02. T. V. B. holds a grant of the FWO and P. V. holds a Methusalem grant from the Flemish Government.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.