메뉴 건너뛰기




Volumn 98, Issue 7, 2001, Pages 2239-2247

Interleukin-5 inhibits translocation of Bax to the mitochondria, cytochrome c release, and activation of caspases in human eosinophils

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; CASPASE INHIBITOR; CYTOCHROME C; INTERLEUKIN 5; PHOSPHATIDYLSERINE; PROTEIN BAX;

EID: 0035496905     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.V98.7.2239     Document Type: Article
Times cited : (87)

References (61)
  • 1
    • 0028841154 scopus 로고
    • Eosinophils: Biology and role in disease
    • Wardlaw AJ, Moqbel R, Kay AB. Eosinophils: biology and role in disease. Adv Immunol. 1995;60:151-266.
    • (1995) Adv Immunol , vol.60 , pp. 151-266
    • Wardlaw, A.J.1    Moqbel, R.2    Kay, A.B.3
  • 2
    • 0034049677 scopus 로고    scopus 로고
    • Mechanisms of eosinophil-associated inflammation
    • Gleich GJ. Mechanisms of eosinophil-associated inflammation. J Allergy Clin Immunol. 2000;105: 651-663.
    • (2000) J Allergy Clin Immunol , vol.105 , pp. 651-663
    • Gleich, G.J.1
  • 3
    • 0030035298 scopus 로고    scopus 로고
    • Eosinophil apoptosis and the resolution of airway inflammation in asthma
    • Woolley KL, Gibson PG, Carty K, et al. Eosinophil apoptosis and the resolution of airway inflammation in asthma. Am J Respir Crit Care Med. 1996; 154:237-243.
    • (1996) Am J Respir Crit Care Med , vol.154 , pp. 237-243
    • Woolley, K.L.1    Gibson, P.G.2    Carty, K.3
  • 4
    • 0030882371 scopus 로고    scopus 로고
    • Delayed eosinophil programmed cell death in vitro: A common feature of inhalant allergy and extrinsic and intrinsic atopic dermatitis
    • Wedi B, Raap U, Lewrick H, Kapp A. Delayed eosinophil programmed cell death in vitro: a common feature of inhalant allergy and extrinsic and intrinsic atopic dermatitis. J Allergy Clin Immunol. 1997;100:536-543.
    • (1997) J Allergy Clin Immunol , vol.100 , pp. 536-543
    • Wedi, B.1    Raap, U.2    Lewrick, H.3    Kapp, A.4
  • 6
    • 0026315499 scopus 로고
    • Eosinophil hematopoietins antagonize the programmed cell death of eosinophils: Cytokine and glucocorticoid effects on eosinophils maintained by endothelial cell-conditioned medium
    • Her E, Frazer J, Austen KF, Owen WF Jr. Eosinophil hematopoietins antagonize the programmed cell death of eosinophils: cytokine and glucocorticoid effects on eosinophils maintained by endothelial cell-conditioned medium. J Clin Invest. 1991;88:1982-1987.
    • (1991) J Clin Invest , vol.88 , pp. 1982-1987
    • Her, E.1    Frazer, J.2    Austen, K.F.3    Owen W.F., Jr.4
  • 7
    • 0025723962 scopus 로고
    • Analysis of the survival of mature human eosinophils: Interleukin-5 prevents apoptosis in mature human eosinophils
    • Yamaguchi Y, Suda T, Ohta S, et al. Analysis of the survival of mature human eosinophils: interleukin-5 prevents apoptosis in mature human eosinophils. Blood. 1991;78:2542-2547.
    • (1991) Blood , vol.78 , pp. 2542-2547
    • Yamaguchi, Y.1    Suda, T.2    Ohta, S.3
  • 9
    • 0031569468 scopus 로고    scopus 로고
    • Direct demonstration of delayed eosinophil apoptosis as a mechanism causing tissue eosinophilia
    • Simon HU, Yousefi S, Schranz C, et al. Direct demonstration of delayed eosinophil apoptosis as a mechanism causing tissue eosinophilia. J Immunol. 1997;158:3902-3908.
    • (1997) J Immunol , vol.158 , pp. 3902-3908
    • Simon, H.U.1    Yousefi, S.2    Schranz, C.3
  • 10
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 1997;275:1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 11
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med. 1997;3: 614-620.
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 12
    • 0033110882 scopus 로고    scopus 로고
    • Expression of Bcl-2 and its homologues in human eosinophils: Modulation by interleukin-5
    • Dewson G, Walsh GM, Wardlaw AJ. Expression of Bcl-2 and its homologues in human eosinophils: modulation by interleukin-5. Am J Respir Cell Mol Biol. 1999;20:720-728.
    • (1999) Am J Respir Cell Mol Biol , vol.20 , pp. 720-728
    • Dewson, G.1    Walsh, G.M.2    Wardlaw, A.J.3
  • 13
    • 0032014925 scopus 로고    scopus 로고
    • Human eosinophils express Bcl-2 family proteins: Modulation of Mcl-1 expression by IFN-γ
    • Druilhe A, Arock M, Le Goff L, Pretolani M. Human eosinophils express Bcl-2 family proteins: modulation of Mcl-1 expression by IFN-γ. Am J Respir Cell Mol Biol. 1998;18:315-322.
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 315-322
    • Druilhe, A.1    Arock, M.2    Le Goff, L.3    Pretolani, M.4
  • 15
    • 0034053746 scopus 로고    scopus 로고
    • Bcl-2 expression in sputum eosinophils in patients with acute asthma
    • Jang AS, Choi IS, Lee S, et al. Bcl-2 expression in sputum eosinophils in patients with acute asthma. Thorax. 2000;55:370-374.
    • (2000) Thorax , vol.55 , pp. 370-374
    • Jang, A.S.1    Choi, I.S.2    Lee, S.3
  • 16
    • 0031014771 scopus 로고    scopus 로고
    • IL-5 but not interferon-γ (IFN-γ) inhibits eosinophil apoptosis by up-regulation of bcl-2 expression
    • Ochiai K, Kagami M, Matsumura R, Tomioka H. IL-5 but not interferon-γ (IFN-γ) inhibits eosinophil apoptosis by up-regulation of bcl-2 expression. Clin Exp Immunol. 1997;107:198-204.
    • (1997) Clin Exp Immunol , vol.107 , pp. 198-204
    • Ochiai, K.1    Kagami, M.2    Matsumura, R.3    Tomioka, H.4
  • 17
    • 0034107113 scopus 로고    scopus 로고
    • Effect of IL-5, glucocorticoid, and Fas ligation on Bcl-2 homologue expression and caspase activation in circulating human eosinophils
    • Zangrilli J, Robertson N, Shetty A, et al. Effect of IL-5, glucocorticoid, and Fas ligation on Bcl-2 homologue expression and caspase activation in circulating human eosinophils. Clin Exp Immunol. 2000;120:12-21.
    • (2000) Clin Exp Immunol , vol.120 , pp. 12-21
    • Zangrilli, J.1    Robertson, N.2    Shetty, A.3
  • 18
    • 0032129211 scopus 로고    scopus 로고
    • L in delayed eosinophil apoptosis mediated by granulocyte-macrophage colony-stimulating factor and interleukin-5
    • L in delayed eosinophil apoptosis mediated by granulocyte-macrophage colony-stimulating factor and interleukin-5. Blood. 1998;92:778-783.
    • (1998) Blood , vol.92 , pp. 778-783
    • Dibbert, B.1    Daigle, I.2    Braun, D.3
  • 19
    • 0030780106 scopus 로고    scopus 로고
    • Movement of Bax from the cytosol to mitochondria during apoptosis
    • Wolter KG, Hsu YT, Smith CL, et al. Movement of Bax from the cytosol to mitochondria during apoptosis. J Cell Biol. 1997;139:1281-1292.
    • (1997) J Cell Biol , vol.139 , pp. 1281-1292
    • Wolter, K.G.1    Hsu, Y.T.2    Smith, C.L.3
  • 20
    • 0032574761 scopus 로고    scopus 로고
    • Bax directly induces release of cytochrome c from isolated mitochondria
    • Jurgensmeier JM, Xie Z, Deveraux Q, et al. Bax directly induces release of cytochrome c from isolated mitochondria. Proc Natl Acad Sci U S A. 1998;95:4997-5002.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4997-5002
    • Jurgensmeier, J.M.1    Xie, Z.2    Deveraux, Q.3
  • 21
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rossé T, Olivier R, Monney L, et al. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature. 1998;391:496-499.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rossé, T.1    Olivier, R.2    Monney, L.3
  • 22
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 1999;18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 23
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. Biochem J. 1997;326:1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 24
    • 0033582526 scopus 로고    scopus 로고
    • Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis
    • Sun XM, MacFarlane M, Zhuang J, et al. Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J Biol Chem. 1999;274:5053-5060.
    • (1999) J Biol Chem , vol.274 , pp. 5053-5060
    • Sun, X.M.1    MacFarlane, M.2    Zhuang, J.3
  • 25
    • 0034630330 scopus 로고    scopus 로고
    • Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis
    • Bratton SB, MacFarlane M, Cain K, Cohen GM. Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis. Exp Cell Res. 2000;256:27-33.
    • (2000) Exp Cell Res , vol.256 , pp. 27-33
    • Bratton, S.B.1    MacFarlane, M.2    Cain, K.3    Cohen, G.M.4
  • 26
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of Bid by caspase-8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of Bid by caspase-8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 1998;94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 27
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen-Sand A, Nichols A, et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol. 1999;144:891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen-Sand, A.2    Nichols, A.3
  • 28
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 1996;86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 29
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature. 1999;397:441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 30
    • 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, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell. 2000;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
  • 31
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M, et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell. 2000;102:43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 32
    • 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, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997;91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 33
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex
    • Cain K, Brown DG, Langlais C, Cohen GM. Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex. J Biol Chem. 1999; 274:22686-22692.
    • (1999) J Biol Chem , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3    Cohen, G.M.4
  • 34
    • 0030890790 scopus 로고    scopus 로고
    • Processing/activation of at least four interleukin-1β converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells
    • MacFarlane M, Cain K, Sun XM, Alnemri ES, Cohen GM. Processing/activation of at least four interleukin-1β converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells. J Cell Biol. 1997; 137:469-479.
    • (1997) J Cell Biol , vol.137 , pp. 469-479
    • MacFarlane, M.1    Cain, K.2    Sun, X.M.3    Alnemri, E.S.4    Cohen, G.M.5
  • 35
    • 0028302030 scopus 로고
    • Eosinophil adhesion to nasal polyp endothelium is P-selectin-dependent
    • Symon FA, Walsh GM, Watson SR, Wardlaw AJ. Eosinophil adhesion to nasal polyp endothelium is P-selectin-dependent. J Exp Med. 1994;180: 371-376.
    • (1994) J Exp Med , vol.180 , pp. 371-376
    • Symon, F.A.1    Walsh, G.M.2    Watson, S.R.3    Wardlaw, A.J.4
  • 36
    • 0032144245 scopus 로고    scopus 로고
    • A comparative study of different methods for the assessment of apoptosis and necrosis in human eosinophils
    • Walsh GM, Dewson G, Wardlaw AJ, Levi-Schaffer F, Moqbel R. A comparative study of different methods for the assessment of apoptosis and necrosis in human eosinophils. J Immunol Methods. 1998;217:153-163.
    • (1998) J Immunol Methods , vol.217 , pp. 153-163
    • Walsh, G.M.1    Dewson, G.2    Wardlaw, A.J.3    Levi-Schaffer, F.4    Moqbel, R.5
  • 37
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin SJ, Reutelingsperger CP, McGahon AJ, et al. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J Exp Med. 1995;182:1545-1556.
    • (1995) J Exp Med , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3
  • 38
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • Scaduto RC Jr, Grotyohann LW. Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys J. 1999;76: 469-477.
    • (1999) Biophys J , vol.76 , pp. 469-477
    • Scaduto R.C., Jr.1    Grotyohann, L.W.2
  • 39
    • 0015883441 scopus 로고
    • Basophils in bronchial asthma with reference to reagin-type allergy
    • Kimura I, Moritani Y, Tanizaki Y. Basophils in bronchial asthma with reference to reagin-type allergy. Clin Allergy. 1973;3:195-202.
    • (1973) Clin Allergy , vol.3 , pp. 195-202
    • Kimura, I.1    Moritani, Y.2    Tanizaki, Y.3
  • 40
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ. Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem. 1997;272:13829-13834.
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 41
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandes-Alnemri T, Armstrong RC, Krebs J, et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc Natl Acad Sci U S A. 1996;93:7464-7469.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7464-7469
    • Fernandes-Alnemri, T.1    Armstrong, R.C.2    Krebs, J.3
  • 42
    • 0029861379 scopus 로고    scopus 로고
    • The Ced-3/interleukin 1β converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2α are substrates for the apoptotic mediator CPP32
    • Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, et al. The Ced-3/interleukin 1β converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2α are substrates for the apoptotic mediator CPP32. J Biol Chem. 1996;271:27099-27106.
    • (1996) J Biol Chem , vol.271 , pp. 27099-27106
    • Srinivasula, S.M.1    Fernandes-Alnemri, T.2    Zangrilli, J.3
  • 43
    • 0030826338 scopus 로고    scopus 로고
    • FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b
    • Scaffidi C, Medema JP, Krammer PH, Peter ME. FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b. J Biol Chem. 1997;272:26953-26958.
    • (1997) J Biol Chem , vol.272 , pp. 26953-26958
    • Scaffidi, C.1    Medema, J.P.2    Krammer, P.H.3    Peter, M.E.4
  • 45
    • 0033601746 scopus 로고    scopus 로고
    • Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner
    • Slee EA, Harte MT, Kluck RM, et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. J Cell Biol. 1999;144:281-292.
    • (1999) J Cell Biol , vol.144 , pp. 281-292
    • Slee, E.A.1    Harte, M.T.2    Kluck, R.M.3
  • 46
    • 0028903933 scopus 로고
    • Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo
    • Zamzami N, Marchetti P, Castedo M, et al. Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo. J Exp Med. 1995;181:1661-1672.
    • (1995) J Exp Med , vol.181 , pp. 1661-1672
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3
  • 47
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998;281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 50
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson B, Montessuit S, Lauper S, Eskes R, Martinou JC. Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem J. 2000;345:271-278.
    • (2000) Biochem J , vol.345 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 51
    • 0034119019 scopus 로고    scopus 로고
    • Bcl-2 and Bax proteins are present in interphase nuclei of mammalian cells
    • Hoetelmans R, van Slooten HJ, Keijzer R, et al. Bcl-2 and Bax proteins are present in interphase nuclei of mammalian cells. Cell Death Differ. 2000;7:384-392.
    • (2000) Cell Death Differ , vol.7 , pp. 384-392
    • Hoetelmans, R.1    Van Slooten, H.J.2    Keijzer, R.3
  • 52
    • 0033808687 scopus 로고    scopus 로고
    • Translocation of Bax to mitochondria during apoptosis measured by laser scanning cytometry
    • Bedner E, Li X, Kunicki J, Darzynkiewicz Z. Translocation of Bax to mitochondria during apoptosis measured by laser scanning cytometry. Cytometry. 2000;41:83-88.
    • (2000) Cytometry , vol.41 , pp. 83-88
    • Bedner, E.1    Li, X.2    Kunicki, J.3    Darzynkiewicz, Z.4
  • 53
    • 0032505674 scopus 로고    scopus 로고
    • Nuclear translocation and increased expression of Bax and disturbance in cell cycle progression without prominent apoptosis induced by hyperthermia
    • Nishita M, Inoue S, Tsuda M, Tateda C, Miyashita T. Nuclear translocation and increased expression of Bax and disturbance in cell cycle progression without prominent apoptosis induced by hyperthermia. Exp Cell Res. 1998;244:357-366.
    • (1998) Exp Cell Res , vol.244 , pp. 357-366
    • Nishita, M.1    Inoue, S.2    Tsuda, M.3    Tateda, C.4    Miyashita, T.5
  • 54
    • 0034721780 scopus 로고    scopus 로고
    • Temperature-dependent arrest of neutrophil apoptosis: Failure of Bax insertion into mitochondria at 15°C prevents the release of cytochrome c
    • Pryde JG, Walker A, Rossi AG, Hannah S, Haslett C. Temperature-dependent arrest of neutrophil apoptosis: failure of Bax insertion into mitochondria at 15°C prevents the release of cytochrome c. J Biol Chem. 2000;275:33574-33584.
    • (2000) J Biol Chem , vol.275 , pp. 33574-33584
    • Pryde, J.G.1    Walker, A.2    Rossi, A.G.3    Hannah, S.4    Haslett, C.5
  • 55
    • 0032566649 scopus 로고    scopus 로고
    • Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis
    • Marzo I, Brenner C, Zamzami N, et al. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science. 1998;281:2027-2031.
    • (1998) Science , vol.281 , pp. 2027-2031
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3
  • 56
    • 0034199444 scopus 로고    scopus 로고
    • Glucocorticoid-induced apoptotic pathways in eosinophils: Comparison with glucocorticoid-sensitive leukemia cells
    • Arai Y, Nakamura Y, Inoue F, et al. Glucocorticoid-induced apoptotic pathways in eosinophils: comparison with glucocorticoid-sensitive leukemia cells. Int J Hematol. 2000;71:340-349.
    • (2000) Int J Hematol , vol.71 , pp. 340-349
    • Arai, Y.1    Nakamura, Y.2    Inoue, F.3
  • 57
    • 0033771527 scopus 로고    scopus 로고
    • Role of caspases in dexamethasone-induced apoptosis and activation of c-Jun NH2-terminal kinase and p38 mitogen-activated protein kinase in human eosinophils
    • Zhang JP, Wong CK, Lam CW. Role of caspases in dexamethasone-induced apoptosis and activation of c-Jun NH2-terminal kinase and p38 mitogen-activated protein kinase in human eosinophils. Clin Exp Immunol. 2000;122:20-27.
    • (2000) Clin Exp Immunol , vol.122 , pp. 20-27
    • Zhang, J.P.1    Wong, C.K.2    Lam, C.W.3
  • 58
    • 0033605722 scopus 로고    scopus 로고
    • Caspase-9 can be activated without proteolytic processing
    • Stennicke HR, Deveraux QL, Humke EW, et al. Caspase-9 can be activated without proteolytic processing. J Biol Chem. 1999;274:8359-8362.
    • (1999) J Biol Chem , vol.274 , pp. 8359-8362
    • Stennicke, H.R.1    Deveraux, Q.L.2    Humke, E.W.3
  • 59
    • 0029913802 scopus 로고    scopus 로고
    • Requirement of Lyn and Syk tyrosine kinases for the prevention of apoptosis by cytokines in human eosinophils
    • Yousefi S, Hoessli DC, Blaser K, Mills GB, Simon HU. Requirement of Lyn and Syk tyrosine kinases for the prevention of apoptosis by cytokines in human eosinophils. J Exp Med. 1996;183:1407-1414.
    • (1996) J Exp Med , vol.183 , pp. 1407-1414
    • Yousefi, S.1    Hoessli, D.C.2    Blaser, K.3    Mills, G.B.4    Simon, H.U.5
  • 60
    • 0032479926 scopus 로고    scopus 로고
    • Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for edsinophil activation and degranulation
    • Pazdrak K, Olszewska-Pazdrak B, Stafford S, Garofalo RP, Alam R. Lyn, Jak2, and Raf-1 kinases are critical for the antiapoptotic effect of interleukin 5, whereas only Raf-1 kinase is essential for edsinophil activation and degranulation. J Exp Med. 1998;188:421-429.
    • (1998) J Exp Med , vol.188 , pp. 421-429
    • Pazdrak, K.1    Olszewska-Pazdrak, B.2    Stafford, S.3    Garofalo, R.P.4    Alam, R.5
  • 61
    • 0030742318 scopus 로고    scopus 로고
    • Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to the prolongation of eosinophil survival
    • Pazdrak K, Adachi T, Alam R. Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to the prolongation of eosinophil survival. J Exp Med. 1997;186:561-568.
    • (1997) J Exp Med , vol.186 , pp. 561-568
    • Pazdrak, K.1    Adachi, T.2    Alam, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.