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Volumn 200, Issue 1, 1999, Pages 1-18

The apoptosis cascade - Morphological and immunohistochemical methods for its visualization

Author keywords

bcl 2; Caspases; Differentiation; Phosphatidylserine flip; TUNEL

Indexed keywords

ANTIBODY; CASPASE; CELL RECEPTOR; CYTOKERATIN; CYTOSKELETON PROTEIN; DNA FRAGMENT; PHOSPHATIDYLSERINE; PROTEIN BCL 2; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; T LYMPHOCYTE ANTIGEN;

EID: 0033048814     PISSN: 03402061     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004290050254     Document Type: Review
Times cited : (281)

References (103)
  • 1
    • 0029118306 scopus 로고
    • Monoclonal antiphosphatidylserine antibody inhibits intercellular fusion of the choriocarcinoma line, JAR
    • Adler RR, Ng AK, Rote NS (1995) Monoclonal antiphosphatidylserine antibody inhibits intercellular fusion of the choriocarcinoma line, JAR. Biol Reprod 53:905-910
    • (1995) Biol Reprod , vol.53 , pp. 905-910
    • Adler, R.R.1    Ng, A.K.2    Rote, N.S.3
  • 2
    • 0031044652 scopus 로고    scopus 로고
    • Mammalian cell death proteases: A family of highly conserved aspartate specific cysteine proteases
    • Alnemri ES (1997) Mammalian cell death proteases: a family of highly conserved aspartate specific cysteine proteases. J Cell Biochem 64:33-42
    • (1997) J Cell Biochem , vol.64 , pp. 33-42
    • Alnemri, E.S.1
  • 3
    • 0029852111 scopus 로고    scopus 로고
    • Regulatory mechanisms in maintenance and modulation of transmembrane lipid asymmetry: Pathophysiological implications
    • Bevers EM, Comfurius P, Zwaal RFA (1996) Regulatory mechanisms in maintenance and modulation of transmembrane lipid asymmetry: pathophysiological implications. Lupus 5:480-487
    • (1996) Lupus , vol.5 , pp. 480-487
    • Bevers, E.M.1    Comfurius, P.2    Zwaal, R.F.A.3
  • 5
    • 0031922434 scopus 로고    scopus 로고
    • Relation between Bcl-2, cell proliferation, and the androgen receptor status in prostate tissue and precursors of prostate cancer
    • Bonkhoff H, Fixemer T, Remberger K (1998) Relation between Bcl-2, cell proliferation, and the androgen receptor status in prostate tissue and precursors of prostate cancer. Prostate 34:251-258
    • (1998) Prostate , vol.34 , pp. 251-258
    • Bonkhoff, H.1    Fixemer, T.2    Remberger, K.3
  • 6
    • 0030707519 scopus 로고    scopus 로고
    • Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin
    • Brancolini C, Lazarevic D, Rodriguez J, Schneider C (1997) Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin. J Cell Biol 139:759-771
    • (1997) J Cell Biol , vol.139 , pp. 759-771
    • Brancolini, C.1    Lazarevic, D.2    Rodriguez, J.3    Schneider, C.4
  • 7
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen LA, Miller DK, Anhalt GJ, Rosen A (1994) Specific cleavage of the 70-kDa protein of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J Biol Chem 269:30757-30760
    • (1994) J Biol Chem , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 8
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulin C, Salvesen GS, Oshima RG (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
  • 9
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P (1998) Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94:727-737
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 10
    • 0032563323 scopus 로고    scopus 로고
    • Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment
    • Chou JJ, Matsuo H, Duan H, Wagner G (1998) Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Cell 94:171-180
    • (1998) Cell , vol.94 , pp. 171-180
    • Chou, J.J.1    Matsuo, H.2    Duan, H.3    Wagner, G.4
  • 11
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM (1997) Caspases: the executioners of apoptosis. Biochem J 326:1-16
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 12
    • 0025012042 scopus 로고
    • Cell death via apoptosis and its relationship to growth, development and dif-ferentiation of both tumour and normal cells
    • Cotter TG, Lennon SV, Glynn JG, Martin SJ (1990) Cell death via apoptosis and its relationship to growth, development and dif-ferentiation of both tumour and normal cells. Anticancer Res 10:1153-1159
    • (1990) Anticancer Res , vol.10 , pp. 1153-1159
    • Cotter, T.G.1    Lennon, S.V.2    Glynn, J.G.3    Martin, S.J.4
  • 13
    • 0029959632 scopus 로고    scopus 로고
    • Specific cleavage of alpha-fodrin during fas-and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1 beta-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease
    • Cryns VL, Bergeron L, Zhu H, Li H, Yuan J (1996) Specific cleavage of alpha-fodrin during Fas-and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1 beta-converting enzyme/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease. J Biol Chem 271:31277-31282
    • (1996) J Biol Chem , vol.271 , pp. 31277-31282
    • Cryns, V.L.1    Bergeron, L.2    Zhu, H.3    Li, H.4    Yuan, J.5
  • 14
    • 0029792058 scopus 로고    scopus 로고
    • Apoptosis of epithelial cells in vivo involves tissue transglutaminase upregulation
    • Cummings M (1996) Apoptosis of epithelial cells in vivo involves tissue transglutaminase upregulation. J Pathol 179:288-293
    • (1996) J Pathol , vol.179 , pp. 288-293
    • Cummings, M.1
  • 15
    • 0032579414 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas-and ceramide-mediated apoptosis in Jurkat T lymphocytes
    • Cuvillier O, Rosenthal DS, Smulson ME, Spiegel S (1998) Sphingosine 1-phosphate inhibits activation of caspases that cleave poly(ADP-ribose) polymerase and lamins during Fas-and ceramide-mediated apoptosis in Jurkat T lymphocytes. J Biol Chem 273:2910-2916
    • (1998) J Biol Chem , vol.273 , pp. 2910-2916
    • Cuvillier, O.1    Rosenthal, D.S.2    Smulson, M.E.3    Spiegel, S.4
  • 16
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC (1997) X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388:300-304
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 19
    • 0030669101 scopus 로고    scopus 로고
    • Defining apoptosis: Players and systems
    • Erickson GF (1997) Defining apoptosis: players and systems. J Soc Gynecol Invest 4:219-228
    • (1997) J Soc Gynecol Invest , vol.4 , pp. 219-228
    • Erickson, G.F.1
  • 20
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein CED-3 and mammalian interleukin-1-beta-converting enzyme
    • Fernandez-Alnemri T, Litwack G, Alnemri ES (1994) CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein CED-3 and mammalian interleukin-1-beta-converting enzyme. J Biol Chem 269:30761-30764
    • (1994) J Biol Chem , vol.269 , pp. 30761-30764
    • Fernandez-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 21
    • 0027325778 scopus 로고
    • Biochemical events in naturally occuring forms of cell death
    • Fesus L (1993) Biochemical events in naturally occuring forms of cell death. FEBS Lett 328:1-5
    • (1993) FEBS Lett , vol.328 , pp. 1-5
    • Fesus, L.1
  • 22
    • 0029862039 scopus 로고    scopus 로고
    • Transglutaminase induction by various cell death and apoptosis pathways
    • Fesus L, Madi A, Balajthy Z, Nemes Z, Szondy Z (1996) Transglutaminase induction by various cell death and apoptosis pathways. Experientia 52:942-949
    • (1996) Experientia , vol.52 , pp. 942-949
    • Fesus, L.1    Madi, A.2    Balajthy, Z.3    Nemes, Z.4    Szondy, Z.5
  • 23
    • 0023267422 scopus 로고
    • Detection of DNA damage in individual cells by flow cytometric analysis using anti-ssDNA monoclonal antibody
    • Frankfurt OS (1987) Detection of DNA damage in individual cells by flow cytometric analysis using anti-ssDNA monoclonal antibody. Exp Cell Res 170:369-380
    • (1987) Exp Cell Res , vol.170 , pp. 369-380
    • Frankfurt, O.S.1
  • 24
    • 0029995766 scopus 로고    scopus 로고
    • A license to kill
    • Fraser A, Evan G (1996) A license to kill. Cell 85:781-784
    • (1996) Cell , vol.85 , pp. 781-784
    • Fraser, A.1    Evan, G.2
  • 25
    • 0025267048 scopus 로고
    • Reversible large-scale deformations in the membranes of electrically-treated cells: Electro-induced bleb formation
    • Gass GV, Chernomordik LV (1990) Reversible large-scale deformations in the membranes of electrically-treated cells: electro-induced bleb formation. Biochim Biophys Acta 1023:1-11
    • (1990) Biochim Biophys Acta , vol.1023 , pp. 1-11
    • Gass, G.V.1    Chernomordik, L.V.2
  • 26
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais FG, Thornberry NA, Ruffolo SC, Nicholson DW, Roy S (1998) Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J Biol Chem 273: 17102-17108
    • (1998) J Biol Chem , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 27
    • 0030605878 scopus 로고    scopus 로고
    • Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells
    • Greidinger EL, Miller DK, Yamin TT, Casciola-Rosen L, Rosen A (1996) Sequential activation of three distinct ICE-like activities in Fas-ligated Jurkat cells. FEBS Lett 390:299-303
    • (1996) FEBS Lett , vol.390 , pp. 299-303
    • Greidinger, E.L.1    Miller, D.K.2    Yamin, T.T.3    Casciola-Rosen, L.4    Rosen, A.5
  • 28
    • 0031776721 scopus 로고    scopus 로고
    • Sequential and rapid activation of select caspases during apoptosis of normal intestinal epithelial cells
    • Grossmann J, Mohr S, Lapentina EG, Fiocchi C, Levine AD (1998) Sequential and rapid activation of select caspases during apoptosis of normal intestinal epithelial cells. Am J Physiol 274:G1117-G1124
    • (1998) Am J Physiol , vol.274
    • Grossmann, J.1    Mohr, S.2    Lapentina, E.G.3    Fiocchi, C.4    Levine, A.D.5
  • 29
    • 0031446274 scopus 로고    scopus 로고
    • Apoptosis and the shape of death
    • Hengartner MO (1997) Apoptosis and the shape of death. Dev Genet 21:245-248
    • (1997) Dev Genet , vol.21 , pp. 245-248
    • Hengartner, M.O.1
  • 30
    • 0031867833 scopus 로고    scopus 로고
    • Cleavage of betacatenin and plakoglobin and shedding of VE-cadherin during endothelial apoptosis: Evidence for a role for caspases and metalloproteinases
    • Herren B, Levkau B, Raines EW, Ross R (1998) Cleavage of betacatenin and plakoglobin and shedding of VE-cadherin during endothelial apoptosis: evidence for a role for caspases and metalloproteinases. Mol Biol Cell 9:1589-1601
    • (1998) Mol Biol Cell , vol.9 , pp. 1589-1601
    • Herren, B.1    Levkau, B.2    Raines, E.W.3    Ross, R.4
  • 31
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenberry D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ (1990) Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348:334-336
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenberry, D.1    Nunez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 32
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Hsu YT, Youle RJ (1997) Nonionic detergents induce dimerization among members of the Bcl-2 family. J Biol Chem 272:13829-13834
    • (1997) J Biol Chem , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 33
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Hsu YT, Youle RJ (1998) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations. J Biol Chem 273:10777-10783
    • (1998) J Biol Chem , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 34
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of bax and bcl-xL during apoptosis
    • Hsu YT, Wolter KG, Youle RJ (1997) Cytosol-to-membrane redistribution of bax and bcl-xL during apoptosis. Proc Natl Acad Sci USA 94:3668-3672
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 35
    • 0032515874 scopus 로고    scopus 로고
    • Bel-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation
    • Hu Y, Benedict MA, Wu D, Inohara N, Nunez G (1998) Bel-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. Proc Natl Acad Sci USA 95:4386-4391
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nunez, G.5
  • 36
    • 0000954147 scopus 로고    scopus 로고
    • Apoptosis-inducing members of the tumor necrosis factor supergene family: Potential functions in placentas
    • in press
    • Hunt JS, Rasmussen CA, Phillips TA, Bowen JA, Bluethmann H (1999) Apoptosis-inducing members of the tumor necrosis factor supergene family: potential functions in placentas. Trophoblast Res (in press)
    • (1999) Trophoblast Res
    • Hunt, J.S.1    Rasmussen, C.A.2    Phillips, T.A.3    Bowen, J.A.4    Bluethmann, H.5
  • 37
    • 0031754353 scopus 로고    scopus 로고
    • Villous cytotrophoblast regulation of the syncytial apoptotic cascade in the human placenta
    • Huppertz B, Frank HG, Kingdom JCP, Reister F, Kaufmann P (1998) Villous cytotrophoblast regulation of the syncytial apoptotic cascade in the human placenta. Histochem Cell Biol 110:495-508
    • (1998) Histochem Cell Biol , vol.110 , pp. 495-508
    • Huppertz, B.1    Frank, H.G.2    Kingdom, J.C.P.3    Reister, F.4    Kaufmann, P.5
  • 38
    • 0032502776 scopus 로고    scopus 로고
    • Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-xL
    • Inohara N, Ekhterae D, Garcia I, Carrio R, Merino J, Merry A, Chen S, Nunez G (1998) Mtd, a novel Bcl-2 family member activates apoptosis in the absence of heterodimerization with Bcl-2 and Bcl-xL. J Biol Chem 273:8705-5710
    • (1998) J Biol Chem , vol.273 , pp. 8705-15710
    • Inohara, N.1    Ekhterae, D.2    Garcia, I.3    Carrio, R.4    Merino, J.5    Merry, A.6    Chen, S.7    Nunez, G.8
  • 39
    • 0031894491 scopus 로고    scopus 로고
    • A role for caspases in lens fiber differentiation
    • Ishizaki Y, Jacobson MD, Raff MC (1998) A role for caspases in lens fiber differentiation. J Cell Biol 140:153-158
    • (1998) J Cell Biol , vol.140 , pp. 153-158
    • Ishizaki, Y.1    Jacobson, M.D.2    Raff, M.C.3
  • 40
    • 0031873504 scopus 로고    scopus 로고
    • Cell surface and nuclear changes during TNF-alpha-induced apoptosis in WEHI 164 murine fibrosarcoma cells. A correlative light, scanning, and transmission electron microscopical study
    • Katsen AD, Vollmar B, Mestres-Ventura P, Menger MD (1998) Cell surface and nuclear changes during TNF-alpha-induced apoptosis in WEHI 164 murine fibrosarcoma cells. A correlative light, scanning, and transmission electron microscopical study. Virchows Arch 433:75-83
    • (1998) Virchows Arch , vol.433 , pp. 75-83
    • Katsen, A.D.1    Vollmar, B.2    Mestres-Ventura, P.3    Menger, M.D.4
  • 43
    • 0029876247 scopus 로고    scopus 로고
    • Cleavage of actin by interleukin 1β-converting enzyme to reverse DNase I inhibition
    • Kayalar C, Ord T, Testa MP, Zhong LT, Bredesen DE (1996) Cleavage of actin by interleukin 1β-converting enzyme to reverse DNase I inhibition. Proc Natl Acad Sci USA 93:2234-2238
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2234-2238
    • Kayalar, C.1    Ord, T.2    Testa, M.P.3    Zhong, L.T.4    Bredesen, D.E.5
  • 44
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239-257
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 46
    • 0031897258 scopus 로고    scopus 로고
    • Proteolytic activities that mediate apoptosis
    • Kidd VJ (1998) Proteolytic activities that mediate apoptosis. Annu Rev Physiol 60:533-573
    • (1998) Annu Rev Physiol , vol.60 , pp. 533-573
    • Kidd, V.J.1
  • 47
    • 0031655421 scopus 로고    scopus 로고
    • Processing/activation of caspases, -3 and -7 and -8 but not caspase-2, in the induction of apoptosis in B-chronic lymphocytic leukemia cells
    • King D, Pringle JH, Hutchinson M, Cohen GM (1998) Processing/activation of caspases, -3 and -7 and -8 but not caspase-2, in the induction of apoptosis in B-chronic lymphocytic leukemia cells. Leukemia 12:1553-1560
    • (1998) Leukemia , vol.12 , pp. 1553-1560
    • King, D.1    Pringle, J.H.2    Hutchinson, M.3    Cohen, G.M.4
  • 48
    • 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 (1997) The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 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
  • 50
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G (1997) The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nature Med 3:614-620
    • (1997) Nature Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 52
    • 0029891890 scopus 로고    scopus 로고
    • Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis
    • Laster SM, Mackenzie JM Jr (1996) Bleb formation and F-actin distribution during mitosis and tumor necrosis factor-induced apoptosis. Microsc Res Tech 34:272-280
    • (1996) Microsc Res Tech , vol.34 , pp. 272-280
    • Laster, S.M.1    Mackenzie J.M., Jr.2
  • 55
    • 0031946009 scopus 로고    scopus 로고
    • Deciphering the apoptotic pathway: All roads lead to death
    • Lincz LF (1998) Deciphering the apoptotic pathway: all roads lead to death. Immunol Cell Biol 76:1-19
    • (1998) Immunol Cell Biol , vol.76 , pp. 1-19
    • Lincz, L.F.1
  • 56
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X, Zou H, Slaughter C, Wang X (1997) DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175-184
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 57
    • 0027214913 scopus 로고
    • Modulation of phosphatidylserine epitope expression by BeWo cells during forskolin treatment
    • Lyden TW, Ng AK, Rote NS (1993) Modulation of phosphatidylserine epitope expression by BeWo cells during forskolin treatment. Placenta 14:177-186
    • (1993) Placenta , vol.14 , pp. 177-186
    • Lyden, T.W.1    Ng, A.K.2    Rote, N.S.3
  • 59
    • 0032080868 scopus 로고    scopus 로고
    • Activation of caspase-3 and apoptosis in cerebellar granule cells
    • Marks N, Berg MJ, Guidotti A, Saito M (1998) Activation of caspase-3 and apoptosis in cerebellar granule cells. J Neurosci Res 52:334-341
    • (1998) J Neurosci Res , vol.52 , pp. 334-341
    • Marks, N.1    Berg, M.J.2    Guidotti, A.3    Saito, M.4
  • 61
    • 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 Abi
    • Martin SJ, Reutelingsperger CP, McGahon AJ, Rader JA, Schie RC van, LaFace DM, Green DR (1995b) Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abi. J Exp Med 182:1545-1556
    • (1995) J Exp Med , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    Van Schie, R.C.5    LaFace, D.M.6    Green, D.R.7
  • 62
    • 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 NJ, Whyte MK, Gilbert CS, Evan GI (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
  • 64
    • 0031080248 scopus 로고    scopus 로고
    • The role of the caspase family of cysteine proteases in apoptosis
    • Miller DK (1997) The role of the caspase family of cysteine proteases in apoptosis. Semin Immunol 9:35-49
    • (1997) Semin Immunol , vol.9 , pp. 35-49
    • Miller, D.K.1
  • 65
    • 0032498625 scopus 로고    scopus 로고
    • Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation
    • Mills JC, Stone NC, Erhardt J, Pittman RN (1998) Apoptotic membrane blebbing is regulated by myosin light chain phosphorylation. J Cell Biol 140:627-636
    • (1998) J Cell Biol , vol.140 , pp. 627-636
    • Mills, J.C.1    Stone, N.C.2    Erhardt, J.3    Pittman, R.N.4
  • 66
    • 0031283328 scopus 로고    scopus 로고
    • Execution mechanisms of programmed cell death by caspase (ICE/CED-3) family proteases
    • Miura M, Hisahara S, Araki T, Okano H (1997) Execution mechanisms of programmed cell death by caspase (ICE/CED-3) family proteases. Heart Vessels [Suppl] 12:66-70
    • (1997) Heart Vessels [Suppl] , vol.12 , pp. 66-70
    • Miura, M.1    Hisahara, S.2    Araki, T.3    Okano, H.4
  • 67
    • 0031827908 scopus 로고    scopus 로고
    • The apoptotic and nonapoptotic nature of the terminal differentiation of erythroid cells
    • Morioka K, Tone S, Mukaida M, Takano-Ohmuro H (1998) The apoptotic and nonapoptotic nature of the terminal differentiation of erythroid cells. Exp Cell Res 240:206-217
    • (1998) Exp Cell Res , vol.240 , pp. 206-217
    • Morioka, K.1    Tone, S.2    Mukaida, M.3    Takano-Ohmuro, H.4
  • 68
    • 0029661437 scopus 로고    scopus 로고
    • Degradation of topoisomerase lia during adenovirus E1A-induced apoptosis is mediated by the activation of the ubiquitin proteolysis system
    • Nakajima T, Morita K, Ohi N, Arai T, Nozaki N, Kikuchi A, Osaka F, Yamao F, Oda K (1996) Degradation of topoisomerase lia during adenovirus E1A-induced apoptosis is mediated by the activation of the ubiquitin proteolysis system. J Biol Chem 271:24842-24849
    • (1996) J Biol Chem , vol.271 , pp. 24842-24849
    • Nakajima, T.1    Morita, K.2    Ohi, N.3    Arai, T.4    Nozaki, N.5    Kikuchi, A.6    Osaka, F.7    Yamao, F.8    Oda, K.9
  • 69
    • 0029608812 scopus 로고
    • Macrophage apoptosis in the absence of active interleukin-1 beta-converting enzyme
    • Nett-Fiordalisi M, Tomaselli K, Russell JH, Chaplin DD (1995) Macrophage apoptosis in the absence of active interleukin-1 beta-converting enzyme. J Leukoc Biol 58:717-724
    • (1995) J Leukoc Biol , vol.58 , pp. 717-724
    • Nett-Fiordalisi, M.1    Tomaselli, K.2    Russell, J.H.3    Chaplin, D.D.4
  • 70
    • 0030745636 scopus 로고    scopus 로고
    • Aminophospholipid translocase activity in JEG-3; a choriocarcinoma model of cytotrophoblast differentiation
    • Obringer AR, Dean KW, Channel SR, Rote NS (1997) Aminophospholipid translocase activity in JEG-3; a choriocarcinoma model of cytotrophoblast differentiation. Placenta 18:421-426
    • (1997) Placenta , vol.18 , pp. 421-426
    • Obringer, A.R.1    Dean, K.W.2    Channel, S.R.3    Rote, N.S.4
  • 71
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ (1993) Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 74:609-619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 72
    • 0031577548 scopus 로고    scopus 로고
    • Requirement of cell-cell contact in the induction of Jurkat T cell apoptosis: The membrane-anchored but not soluble form of FasL can trigger anti-CD3-induced apoptosis in Jurkat T cells
    • Oyaizu N, Kayagaki N, Yagita H, Pahwa S, Ikawa Y (1997) Requirement of cell-cell contact in the induction of Jurkat T cell apoptosis: the membrane-anchored but not soluble form of FasL can trigger anti-CD3-induced apoptosis in Jurkat T cells. Biochem Biophys Res Commun 238:670-675
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 670-675
    • Oyaizu, N.1    Kayagaki, N.2    Yagita, H.3    Pahwa, S.4    Ikawa, Y.5
  • 74
    • 0032031457 scopus 로고    scopus 로고
    • Functional roles of Fas and Bcl-2-regulated apoptosis of T lymphocytes
    • Parijs L van, Biuckians A, Abbas AK (1998) Functional roles of Fas and Bcl-2-regulated apoptosis of T lymphocytes. J Immunol 160:2065-2071
    • (1998) J Immunol , vol.160 , pp. 2065-2071
    • Van Parijs, L.1    Biuckians, A.2    Abbas, A.K.3
  • 75
    • 14044258854 scopus 로고    scopus 로고
    • Lack of transglutaminase protein crosslinking leads to leakage of macromolecules from dying cells: Relationship to development of autoimmunity in MRL lpr/lpr mice
    • Piredda L, Amendolo A, Colizzi V, Davies P, Farrace MG, Fraziano M, Gentile V, Uray I, Piacentini M, Fesus L (1997) Lack of transglutaminase protein crosslinking leads to leakage of macromolecules from dying cells: relationship to development of autoimmunity in MRL lpr/lpr mice. Cell Death Differ 4:463-472
    • (1997) Cell Death Differ , vol.4 , pp. 463-472
    • Piredda, L.1    Amendolo, A.2    Colizzi, V.3    Davies, P.4    Farrace, M.G.5    Fraziano, M.6    Gentile, V.7    Uray, I.8    Piacentini, M.9    Fesus, L.10
  • 76
    • 0031178835 scopus 로고    scopus 로고
    • Bcl-2 expression in target cells leads to functional inhibition of caspase-3 protease family in human NK and lymphokine-activated killer cell granule-mediated apoptosis
    • Renvoize C, Roger R, Moulian N, Bertoglio J, Breard J (1997) Bcl-2 expression in target cells leads to functional inhibition of caspase-3 protease family in human NK and lymphokine-activated killer cell granule-mediated apoptosis. J Immunol 159:126-134
    • (1997) J Immunol , vol.159 , pp. 126-134
    • Renvoize, C.1    Roger, R.2    Moulian, N.3    Bertoglio, J.4    Breard, J.5
  • 78
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (1997) The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J 16:6914-6925
    • (1997) EMBO J , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 79
    • 0032541132 scopus 로고    scopus 로고
    • Detection of pro-caspase-3 in cytosol and mitochondria of various tissues
    • Samali A, Zhivotovsky B, Jones DP, Orrenius S (1998) Detection of pro-caspase-3 in cytosol and mitochondria of various tissues. FEBS Lett 431:167-169
    • (1998) FEBS Lett , vol.431 , pp. 167-169
    • Samali, A.1    Zhivotovsky, B.2    Jones, D.P.3    Orrenius, S.4
  • 80
    • 0031838286 scopus 로고    scopus 로고
    • Immunohistochemical study of Fas, Fas ligand and interleukin-1 beta converting enzyme expression in human prostatic cancer
    • Sasaki Y, Ahmed H, Takeuchi T, Moriyama N, Kawabe K (1998) Immunohistochemical study of Fas, Fas ligand and interleukin-1 beta converting enzyme expression in human prostatic cancer. Br J Urol 81:852-855
    • (1998) Br J Urol , vol.81 , pp. 852-855
    • Sasaki, Y.1    Ahmed, H.2    Takeuchi, T.3    Moriyama, N.4    Kawabe, K.5
  • 81
    • 0032473635 scopus 로고    scopus 로고
    • Phagocytic docking without shocking
    • Savill J (1998) Phagocytic docking without shocking. Nature 392:442-443
    • (1998) Nature , vol.392 , pp. 442-443
    • Savill, J.1
  • 84
    • 0032577703 scopus 로고    scopus 로고
    • Transient poly(ADP-ribosyl)ation of nuclear proteins and role of poly(ADP-ribose) polymerase in the early stages of apoptosis
    • Simbulan-Rosenthal CM, Rosenthal DS, Lyer S, Boulares AH, Smulson ME (1998) Transient poly(ADP-ribosyl)ation of nuclear proteins and role of poly(ADP-ribose) polymerase in the early stages of apoptosis. J Biol Chem 273:13703-13712
    • (1998) J Biol Chem , vol.273 , pp. 13703-13712
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Lyer, S.3    Boulares, A.H.4    Smulson, M.E.5
  • 86
    • 0032533317 scopus 로고    scopus 로고
    • Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3 (CPP32)-like activity
    • Stefanis L, Troy CM, Qi H, Shelanski ML, Greene LA (1998) Caspase-2 (Nedd-2) processing and death of trophic factor-deprived PC12 cells and sympathetic neurons occur independently of caspase-3 (CPP32)-like activity. J Neurosci 18:9204-9215
    • (1998) J Neurosci , vol.18 , pp. 9204-9215
    • Stefanis, L.1    Troy, C.M.2    Qi, H.3    Shelanski, M.L.4    Greene, L.A.5
  • 90
    • 0028928016 scopus 로고
    • The RNA-binding protein TIAR is translocated from the nucleus to the cytoplasm during Fas-mediated apoptotic cell death
    • Taupin JL, Qingsheng T, Kedersha N, Robertson M, Anderson P (1995) The RNA-binding protein TIAR is translocated from the nucleus to the cytoplasm during Fas-mediated apoptotic cell death. Proc Natl Acad Sci USA 92:1629-1633
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1629-1633
    • Taupin, J.L.1    Qingsheng, T.2    Kedersha, N.3    Robertson, M.4    Anderson, P.5
  • 91
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M, Quan LT, O'Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM (1995) Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81:801-809
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 92
    • 0025006126 scopus 로고
    • Binding of annexin V / placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets
    • Thiagarajan P, Tait JF (1990) Binding of annexin V / placental anticoagulant protein I to platelets. Evidence for phosphatidylserine exposure in the procoagulant response of activated platelets. J Biol Chem 265:17420-17423
    • (1990) J Biol Chem , vol.265 , pp. 17420-17423
    • Thiagarajan, P.1    Tait, J.F.2
  • 93
    • 0031616983 scopus 로고    scopus 로고
    • Special topic: Apoptosis
    • Thompson EB (1998) Special topic: apoptosis. Annu Rev Physiol 60:525-532
    • (1998) Annu Rev Physiol , vol.60 , pp. 525-532
    • Thompson, E.B.1
  • 94
    • 0030838164 scopus 로고    scopus 로고
    • The caspase family of cysteine proteases
    • Thornberry NA (1996) The caspase family of cysteine proteases. Br Med Bull 53:478-490
    • (1996) Br Med Bull , vol.53 , pp. 478-490
    • Thornberry, N.A.1
  • 97
    • 0028527479 scopus 로고
    • Back and forth: The regulation and function of transbilayer phospholipid movement in eukaryotic cells
    • Williamson P, Schlegel RA (1994) Back and forth: the regulation and function of transbilayer phospholipid movement in eukaryotic cells. Mol Membr Biol 11:199-216
    • (1994) Mol Membr Biol , vol.11 , pp. 199-216
    • Williamson, P.1    Schlegel, R.A.2
  • 98
    • 0028965578 scopus 로고
    • The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2
    • Yang T, Kozopas KM, Craig RW (1995) The intracellular distribution and pattern of expression of Mcl-1 overlap with, but are not identical to, those of Bcl-2. J Cell Biol 128:1173-1184
    • (1995) J Cell Biol , vol.128 , pp. 1173-1184
    • Yang, T.1    Kozopas, K.M.2    Craig, R.W.3
  • 99
    • 0029160465 scopus 로고
    • Apoptotic cells in the human endometrium and placental villi: Pitfalls in applying the TUNEL method
    • Yasuda M, Umemura S, Osamura YR, Kenjo T, Tsutsumi Y (1995) Apoptotic cells in the human endometrium and placental villi: pitfalls in applying the TUNEL method. Arch Histol Cytol 58:185-190
    • (1995) Arch Histol Cytol , vol.58 , pp. 185-190
    • Yasuda, M.1    Umemura, S.2    Osamura, Y.R.3    Kenjo, T.4    Tsutsumi, Y.5
  • 100
    • 0030987071 scopus 로고    scopus 로고
    • Transducing signals of life and death
    • Yuan J (1997) Transducing signals of life and death. Curr Opin Cell Biol 9:247-251
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 247-251
    • Yuan, J.1
  • 102
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X (1997) Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90:405-413
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


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