메뉴 건너뛰기




Volumn 1783, Issue 2, 2008, Pages 297-311

S100A8/9 induces cell death via a novel, RAGE-independent pathway that involves selective release of Smac/DIABLO and Omi/HtrA2

Author keywords

Bcl2 protein family; Cancer regression; Drp1; Mitochondrial fission; Receptor for advanced glycated endproducts (RAGE); S100 calgranulin; XIAP

Indexed keywords

ADVANCED GLYCATION END PRODUCT; APOPTOSIS INDUCING FACTOR; CALGRANULIN A; CALGRANULIN B; CYTOCHROME C; DYNAMIN I; ENDONUCLEASE G; PROTEIN BAD; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN BNIP3; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; SERINE PROTEINASE OMI;

EID: 38349040141     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.10.015     Document Type: Article
Times cited : (112)

References (64)
  • 1
    • 3042740431 scopus 로고    scopus 로고
    • Mechanism of apoptosis induced by S100A8/A9 in colon cancer cell lines: the role of ROS and the effect of metal ions
    • Ghavami S., Kerkhoff C., Los M., Hashemi M., Sorg C., and Karami-Tehrani F. Mechanism of apoptosis induced by S100A8/A9 in colon cancer cell lines: the role of ROS and the effect of metal ions. J. Leukoc. Biol. 76 (2004) 169-175
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 169-175
    • Ghavami, S.1    Kerkhoff, C.2    Los, M.3    Hashemi, M.4    Sorg, C.5    Karami-Tehrani, F.6
  • 2
    • 0023815341 scopus 로고
    • Neutrophil death as a defence mechanism against Candida albicans infections
    • McNamara M.P., Wiessner J.H., Collins-Lech C., Hahn B.L., and Sohnle P.G. Neutrophil death as a defence mechanism against Candida albicans infections. Lancet 2 (1988) 1163-1165
    • (1988) Lancet , vol.2 , pp. 1163-1165
    • McNamara, M.P.1    Wiessner, J.H.2    Collins-Lech, C.3    Hahn, B.L.4    Sohnle, P.G.5
  • 4
    • 0032435515 scopus 로고    scopus 로고
    • Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)
    • Kerkhoff C., Klempt M., and Sorg C. Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Biochem. Biophys. Acta 1448 (1998) 200-211
    • (1998) Biochem. Biophys. Acta , vol.1448 , pp. 200-211
    • Kerkhoff, C.1    Klempt, M.2    Sorg, C.3
  • 5
    • 0242335600 scopus 로고    scopus 로고
    • S100A9/S100A8: myeloid representatives of the S100 protein family as prominent players in innate immunity
    • Nacken W., Roth J., Sorg C., and Kerkhoff C. S100A9/S100A8: myeloid representatives of the S100 protein family as prominent players in innate immunity. Microsc. Res. Tech. 60 (2003) 569-580
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 569-580
    • Nacken, W.1    Roth, J.2    Sorg, C.3    Kerkhoff, C.4
  • 6
    • 14644404879 scopus 로고    scopus 로고
    • The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2
    • Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., and Doussiere J. The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2. FASEB J. 19 (2005) 467-469
    • (2005) FASEB J. , vol.19 , pp. 467-469
    • Kerkhoff, C.1    Nacken, W.2    Benedyk, M.3    Dagher, M.C.4    Sopalla, C.5    Doussiere, J.6
  • 8
    • 0034795140 scopus 로고    scopus 로고
    • The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses
    • Schmidt A.M., Yan S.D., Yan S.F., and Stern D.M. The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. J. Clin. Invest. 108 (2001) 949-955
    • (2001) J. Clin. Invest. , vol.108 , pp. 949-955
    • Schmidt, A.M.1    Yan, S.D.2    Yan, S.F.3    Stern, D.M.4
  • 9
    • 33746920337 scopus 로고    scopus 로고
    • Advanced glycation end products: sparking the development of diabetic vascular injury
    • Goldin A., Beckman J.A., Schmidt A.M., and Creager M.A. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 114 (2006) 597-605
    • (2006) Circulation , vol.114 , pp. 597-605
    • Goldin, A.1    Beckman, J.A.2    Schmidt, A.M.3    Creager, M.A.4
  • 10
    • 0034704068 scopus 로고    scopus 로고
    • Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation
    • Huttunen H.J., Kuja-Panula J., Sorci G., Agneletti A.L., Donato R., and Rauvala H. Coregulation of neurite outgrowth and cell survival by amphoterin and S100 proteins through receptor for advanced glycation end products (RAGE) activation. J. Biol. Chem. 275 (2000) 40096-40105
    • (2000) J. Biol. Chem. , vol.275 , pp. 40096-40105
    • Huttunen, H.J.1    Kuja-Panula, J.2    Sorci, G.3    Agneletti, A.L.4    Donato, R.5    Rauvala, H.6
  • 11
    • 27644494779 scopus 로고    scopus 로고
    • Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity
    • Nakatani Y., Yamazaki M., Chazin W.J., and Yui S. Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc ion and its implication for apoptosis-inducing activity. Mediators Inflamm. 2005 (2005) 280-292
    • (2005) Mediators Inflamm. , vol.2005 , pp. 280-292
    • Nakatani, Y.1    Yamazaki, M.2    Chazin, W.J.3    Yui, S.4
  • 12
    • 0035999163 scopus 로고    scopus 로고
    • Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosis-inducing activity
    • Yui S., Nakatani Y., Hunter M.J., Chazin W.J., and Yamazaki M. Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosis-inducing activity. Mediators Inflamm. 11 (2002) 165-172
    • (2002) Mediators Inflamm. , vol.11 , pp. 165-172
    • Yui, S.1    Nakatani, Y.2    Hunter, M.J.3    Chazin, W.J.4    Yamazaki, M.5
  • 13
    • 0032701911 scopus 로고    scopus 로고
    • The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils
    • Kerkhoff C., Klempt M., Kaever V., and Sorg C. The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils. J. Biol. Chem. 274 (1999) 32672-32679
    • (1999) J. Biol. Chem. , vol.274 , pp. 32672-32679
    • Kerkhoff, C.1    Klempt, M.2    Kaever, V.3    Sorg, C.4
  • 14
    • 0032524649 scopus 로고    scopus 로고
    • High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14
    • Hunter M.J., and Chazin W.J. High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J. Biol. Chem. 273 (1998) 12427-12435
    • (1998) J. Biol. Chem. , vol.273 , pp. 12427-12435
    • Hunter, M.J.1    Chazin, W.J.2
  • 16
    • 33846396238 scopus 로고    scopus 로고
    • Cytotoxic effects of intra- and extracellular zinc chelation on human breast cancer cells
    • Hashemi M., Ghavami S., Eshraghi M., Booy E.P., and Los M. Cytotoxic effects of intra- and extracellular zinc chelation on human breast cancer cells. Eur. J. Pharm. 557 (2007) 9-19
    • (2007) Eur. J. Pharm. , vol.557 , pp. 9-19
    • Hashemi, M.1    Ghavami, S.2    Eshraghi, M.3    Booy, E.P.4    Los, M.5
  • 17
    • 27644584179 scopus 로고    scopus 로고
    • Cancer-specific toxicity of apoptin is independent of death receptors but involves the loss of mitochondrial membrane potential and the release of mitochondrial cell-death mediators by a Nur77-dependent pathway
    • Maddika S., Booy E.P., Johar D., Gibson S.B., Ghavami S., and Los M. Cancer-specific toxicity of apoptin is independent of death receptors but involves the loss of mitochondrial membrane potential and the release of mitochondrial cell-death mediators by a Nur77-dependent pathway. J. Cell Sci. 118 (2005) 4485-4493
    • (2005) J. Cell Sci. , vol.118 , pp. 4485-4493
    • Maddika, S.1    Booy, E.P.2    Johar, D.3    Gibson, S.B.4    Ghavami, S.5    Los, M.6
  • 18
    • 0031777737 scopus 로고    scopus 로고
    • Intracellular localization of migration inhibitory factor-related protein (MRP) and detection of cell surface MRP binding sites on human leukemia cell lines
    • Koike T., Kondo K., Makita T., Kajiyama K., Yoshida T., and Morikawa M. Intracellular localization of migration inhibitory factor-related protein (MRP) and detection of cell surface MRP binding sites on human leukemia cell lines. J. Biochem. (Tokyo) 123 (1998) 1079-1087
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1079-1087
    • Koike, T.1    Kondo, K.2    Makita, T.3    Kajiyama, K.4    Yoshida, T.5    Morikawa, M.6
  • 19
    • 1342347862 scopus 로고    scopus 로고
    • Vitamin D enhances caspase-dependent and independent TNF-induced breast cancer cell death: the role of reactive oxygen species
    • Weitsman G.E., Ravid A., Liberman U.A., and Koren R. Vitamin D enhances caspase-dependent and independent TNF-induced breast cancer cell death: the role of reactive oxygen species. Ann. N.Y. Acad. Sci. 1010 (2003) 437-440
    • (2003) Ann. N.Y. Acad. Sci. , vol.1010 , pp. 437-440
    • Weitsman, G.E.1    Ravid, A.2    Liberman, U.A.3    Koren, R.4
  • 20
    • 36248987708 scopus 로고    scopus 로고
    • Akt is transferred to the nucleus of cells treated with apoptin, and it participates in apoptin-induced cell death
    • Maddika S., Bay G.H., Kroczak T.J., Ande S.R., Maddika S., Wiechec E., Gibson S.B., and Los M. Akt is transferred to the nucleus of cells treated with apoptin, and it participates in apoptin-induced cell death. Cell Prolif. 40 (2007) 835-848
    • (2007) Cell Prolif. , vol.40 , pp. 835-848
    • Maddika, S.1    Bay, G.H.2    Kroczak, T.J.3    Ande, S.R.4    Maddika, S.5    Wiechec, E.6    Gibson, S.B.7    Los, M.8
  • 21
    • 0036778523 scopus 로고    scopus 로고
    • The role of caspases in cryoinjury: caspase inhibition strongly improves the recovery of cryopreserved hematopoietic and other cells
    • Stroh C., Cassens U., Samraj A.K., Sibrowski W., Schulze-Osthoff K., and Los M. The role of caspases in cryoinjury: caspase inhibition strongly improves the recovery of cryopreserved hematopoietic and other cells. Faseb J. 16 (2002) 1651-1653
    • (2002) Faseb J. , vol.16 , pp. 1651-1653
    • Stroh, C.1    Cassens, U.2    Samraj, A.K.3    Sibrowski, W.4    Schulze-Osthoff, K.5    Los, M.6
  • 22
    • 0031943314 scopus 로고    scopus 로고
    • Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocyte-derived calprotectin: involvement of protein synthesis and generation of reactive oxygen species in target cells
    • Mikami M., Yamazaki M., and Yui S. Kinetical analysis of tumor cell death-inducing mechanism by polymorphonuclear leukocyte-derived calprotectin: involvement of protein synthesis and generation of reactive oxygen species in target cells. Microbiol. Immunol. 42 (1998) 211-221
    • (1998) Microbiol. Immunol. , vol.42 , pp. 211-221
    • Mikami, M.1    Yamazaki, M.2    Yui, S.3
  • 23
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D., Nunez G., Milliman C., Schreiber R.D., and Korsmeyer S.J. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348 (1990) 334-336
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 27
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., and Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412 (2001) 95-99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 28
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 (2004) 205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 29
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: regulators of the cellular life-or-death switch
    • Cory S., and Adams J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2 (2002) 647-656
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 30
  • 31
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden M.G., and Thompson C.B. Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?. Nat. Cell Biol. 1 (1999) E209-E216
    • (1999) Nat. Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 33
    • 0842302344 scopus 로고    scopus 로고
    • Mitochondrial morphology is dynamic and varied
    • Rube D.A., and van der Bliek A.M. Mitochondrial morphology is dynamic and varied. Mol. Cell. Biochem. 256-257 (2004) 331-339
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 331-339
    • Rube, D.A.1    van der Bliek, A.M.2
  • 35
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y., Krueger E.W., Oswald B.J., and McNiven M.A. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell Biol. 23 (2003) 5409-5420
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 36
    • 27144477744 scopus 로고    scopus 로고
    • Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1
    • Yu T., Fox R.J., Burwell L.S., and Yoon Y. Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1. J. Cell Sci. 118 (2005) 4141-4151
    • (2005) J. Cell Sci. , vol.118 , pp. 4141-4151
    • Yu, T.1    Fox, R.J.2    Burwell, L.S.3    Yoon, Y.4
  • 38
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang H.G., Wang J., Yang X., Hsu H.C., and Mountz J.D. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 23 (2004) 2009-2015
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 39
    • 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. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Molecular cell 8 (2001) 613-621
    • (2001) Molecular cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 40
    • 0032902356 scopus 로고    scopus 로고
    • The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: the S100A9 and S100A8 positive cells underlie and invade tumor mass
    • Stulik J., Osterreicher J., Koupilova K., Knizek J., Macela A., Bures J., Jandik P., Langr F., Dedic K., and Jungblut P.R. The analysis of S100A9 and S100A8 expression in matched sets of macroscopically normal colon mucosa and colorectal carcinoma: the S100A9 and S100A8 positive cells underlie and invade tumor mass. Electrophoresis 20 (1999) 1047-1054
    • (1999) Electrophoresis , vol.20 , pp. 1047-1054
    • Stulik, J.1    Osterreicher, J.2    Koupilova, K.3    Knizek, J.4    Macela, A.5    Bures, J.6    Jandik, P.7    Langr, F.8    Dedic, K.9    Jungblut, P.R.10
  • 41
    • 0030898101 scopus 로고    scopus 로고
    • Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway
    • Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., and Sorg C. Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J. Biol. Chem. 272 (1997) 9496-9502
    • (1997) J. Biol. Chem. , vol.272 , pp. 9496-9502
    • Rammes, A.1    Roth, J.2    Goebeler, M.3    Klempt, M.4    Hartmann, M.5    Sorg, C.6
  • 42
    • 22944472086 scopus 로고    scopus 로고
    • Induction of apoptotic cell death in tumor cells by S100A8/A9 released from inflammatory cells upon cellular activation
    • Kerkhoff C., and Ghavami S. Induction of apoptotic cell death in tumor cells by S100A8/A9 released from inflammatory cells upon cellular activation. Current Medical Chemistry (AIAA) 4 (2005) 383-391
    • (2005) Current Medical Chemistry (AIAA) , vol.4 , pp. 383-391
    • Kerkhoff, C.1    Ghavami, S.2
  • 43
    • 0036479102 scopus 로고    scopus 로고
    • The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells
    • Robinson M.J., Tessier P., Poulsom R., and Hogg N. The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells. J. Biol. Chem. 277 (2002) 3658-3665
    • (2002) J. Biol. Chem. , vol.277 , pp. 3658-3665
    • Robinson, M.J.1    Tessier, P.2    Poulsom, R.3    Hogg, N.4
  • 44
    • 0035313549 scopus 로고    scopus 로고
    • Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells
    • Srikrishna G., Panneerselvam K., Westphal V., Abraham V., Varki A., and Freeze H.H. Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol. 166 (2001) 4678-4688
    • (2001) J. Immunol. , vol.166 , pp. 4678-4688
    • Srikrishna, G.1    Panneerselvam, K.2    Westphal, V.3    Abraham, V.4    Varki, A.5    Freeze, H.H.6
  • 45
    • 0035830423 scopus 로고    scopus 로고
    • Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells
    • Kerkhoff C., Sorg C., Tandon N.N., and Nacken W. Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry 40 (2001) 241-248
    • (2001) Biochemistry , vol.40 , pp. 241-248
    • Kerkhoff, C.1    Sorg, C.2    Tandon, N.N.3    Nacken, W.4
  • 47
    • 1842421190 scopus 로고    scopus 로고
    • S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner
    • Sorci G., Riuzzi F., Agneletti A.L., Marchetti C., and Donato R. S100B causes apoptosis in a myoblast cell line in a RAGE-independent manner. J. Cell Physiol. 199 (2004) 274-283
    • (2004) J. Cell Physiol. , vol.199 , pp. 274-283
    • Sorci, G.1    Riuzzi, F.2    Agneletti, A.L.3    Marchetti, C.4    Donato, R.5
  • 48
    • 0142229704 scopus 로고    scopus 로고
    • Intracellular and extracellular roles of S100 proteins
    • Donato R. Intracellular and extracellular roles of S100 proteins. Microsc. Res. Tech. 60 (2003) 540-551
    • (2003) Microsc. Res. Tech. , vol.60 , pp. 540-551
    • Donato, R.1
  • 49
    • 0033153086 scopus 로고    scopus 로고
    • The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice
    • Los M., Wesselborg S., and Schulze-Osthoff K. The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity 10 (1999) 629-639
    • (1999) Immunity , vol.10 , pp. 629-639
    • Los, M.1    Wesselborg, S.2    Schulze-Osthoff, K.3
  • 51
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 52
    • 0037044737 scopus 로고    scopus 로고
    • Effect of Bcl-2 overexpression on mitochondrial structure and function
    • Kowaltowski A.J., Cosso R.G., Campos C.B., and Fiskum G. Effect of Bcl-2 overexpression on mitochondrial structure and function. J. Biol. Chem. 277 (2002) 42802-42807
    • (2002) J. Biol. Chem. , vol.277 , pp. 42802-42807
    • Kowaltowski, A.J.1    Cosso, R.G.2    Campos, C.B.3    Fiskum, G.4
  • 53
    • 0033593230 scopus 로고    scopus 로고
    • Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL
    • Finucane D.M., Bossy-Wetzel E., Waterhouse N.J., Cotter T.G., and Green D.R. Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL. J. Biol. Chem. 274 (1999) 2225-2233
    • (1999) J. Biol. Chem. , vol.274 , pp. 2225-2233
    • Finucane, D.M.1    Bossy-Wetzel, E.2    Waterhouse, N.J.3    Cotter, T.G.4    Green, D.R.5
  • 54
    • 10044219516 scopus 로고    scopus 로고
    • Activation of p38 MAPK is required for Bax translocation to mitochondria, cytochrome c release and apoptosis induced by UVB irradiation in human keratinocytes
    • Van Laethem A., Van Kelst S., Lippens S., Declercq W., Vandenabeele P., Janssens S., Vandenheede J.R., Garmyn M., and Agostinis P. Activation of p38 MAPK is required for Bax translocation to mitochondria, cytochrome c release and apoptosis induced by UVB irradiation in human keratinocytes. Faseb J. 18 (2004) 1946-1948
    • (2004) Faseb J. , vol.18 , pp. 1946-1948
    • Van Laethem, A.1    Van Kelst, S.2    Lippens, S.3    Declercq, W.4    Vandenabeele, P.5    Janssens, S.6    Vandenheede, J.R.7    Garmyn, M.8    Agostinis, P.9
  • 55
    • 0035369143 scopus 로고    scopus 로고
    • The mitochondrial apoptosome: a killer unleashed by the cytochrome seas
    • Adrain C., and Martin S.J. The mitochondrial apoptosome: a killer unleashed by the cytochrome seas. Trends Biochem. Sci. 26 (2001) 390-397
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 390-397
    • Adrain, C.1    Martin, S.J.2
  • 58
    • 33746827856 scopus 로고    scopus 로고
    • Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration
    • Munoz-Pinedo C., Guio-Carrion A., Goldstein J.C., Fitzgerald P., Newmeyer D.D., and Green D.R. Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 11573-11578
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11573-11578
    • Munoz-Pinedo, C.1    Guio-Carrion, A.2    Goldstein, J.C.3    Fitzgerald, P.4    Newmeyer, D.D.5    Green, D.R.6
  • 59
    • 12544251669 scopus 로고    scopus 로고
    • Mitochondrial release of pro-apoptotic proteins: electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes
    • Uren R.T., Dewson G., Bonzon C., Lithgow T., Newmeyer D.D., and Kluck R.M. Mitochondrial release of pro-apoptotic proteins: electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes. J. Biol. Chem. 280 (2005) 2266-2274
    • (2005) J. Biol. Chem. , vol.280 , pp. 2266-2274
    • Uren, R.T.1    Dewson, G.2    Bonzon, C.3    Lithgow, T.4    Newmeyer, D.D.5    Kluck, R.M.6
  • 60
    • 17844394478 scopus 로고    scopus 로고
    • Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    • Otera H., Ohsakaya S., Nagaura Z., Ishihara N., and Mihara K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. Embo J. 24 (2005) 1375-1386
    • (2005) Embo J. , vol.24 , pp. 1375-1386
    • Otera, H.1    Ohsakaya, S.2    Nagaura, Z.3    Ishihara, N.4    Mihara, K.5
  • 61
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • Arnoult D., Gaume B., Karbowski M., Sharpe J.C., Cecconi F., and Youle R.J. Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization. Embo J. 22 (2003) 4385-4399
    • (2003) Embo J. , vol.22 , pp. 4385-4399
    • Arnoult, D.1    Gaume, B.2    Karbowski, M.3    Sharpe, J.C.4    Cecconi, F.5    Youle, R.J.6
  • 62
    • 0017253440 scopus 로고
    • Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase
    • Ferguson-Miller S., Brautigan D.L., and Margoliash E. Correlation of the kinetics of electron transfer activity of various eukaryotic cytochromes c with binding to mitochondrial cytochrome c oxidase. J. Biol. Chem. 251 (1976) 1104-1115
    • (1976) J. Biol. Chem. , vol.251 , pp. 1104-1115
    • Ferguson-Miller, S.1    Brautigan, D.L.2    Margoliash, E.3
  • 63
    • 1042302135 scopus 로고    scopus 로고
    • The cardiolipins-cytochrome c interaction and the mitochondrial regulation of apoptosis
    • Iverson S.L., and Orrenius S. The cardiolipins-cytochrome c interaction and the mitochondrial regulation of apoptosis. Arch. Biochem. Biophys. 423 (2004) 37-46
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 37-46
    • Iverson, S.L.1    Orrenius, S.2
  • 64
    • 0015523121 scopus 로고
    • Cytochrome c reactivity in its complexes with mammalian cytochrome c oxidase and yeast peroxidase
    • Mochan E., and Nicholls P. Cytochrome c reactivity in its complexes with mammalian cytochrome c oxidase and yeast peroxidase. Biochim. Biophys. Acta 267 (1972) 309-319
    • (1972) Biochim. Biophys. Acta , vol.267 , pp. 309-319
    • Mochan, E.1    Nicholls, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.