메뉴 건너뛰기




Volumn 39, Issue 1, 1999, Pages 49-59

Regulation of apoptosis: Involvement of Bcl-2-related proteins

Author keywords

Apoptosis; Bax; Bcl 2

Indexed keywords

ANIMALIA;

EID: 0032610587     PISSN: 09265287     EISSN: None     Source Type: Journal    
DOI: 10.1051/rnd:19990103     Document Type: Review
Times cited : (33)

References (50)
  • 2
    • 0031809920 scopus 로고    scopus 로고
    • Mechanisms controlling cellular suicide: Role of Bcl-2 and caspases
    • Allen R.T., Cluck M.W., Agrawal D.K., Mechanisms controlling cellular suicide: role of Bcl-2 and caspases, Cell Mol. Life Sci. 54 (1998) 427-445.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 427-445
    • Allen, R.T.1    Cluck, M.W.2    Agrawal, D.K.3
  • 4
    • 0029795396 scopus 로고    scopus 로고
    • Elevated levels of apoptosis regulator proteins p53 and Bel-2 are independent prognostic biomarkers in surgically treated clinically localized prostate cancer
    • Bauer J.J., Sesterhenn I.A., Mostofi F.K., Mcleod D.G., Srivastava S., Moul J.W., Elevated levels of apoptosis regulator proteins p53 and Bel-2 are independent prognostic biomarkers in surgically treated clinically localized prostate cancer, J. Urol. 156 (1996) 1511-1516.
    • (1996) J. Urol. , vol.156 , pp. 1511-1516
    • Bauer, J.J.1    Sesterhenn, I.A.2    Mostofi, F.K.3    Mcleod, D.G.4    Srivastava, S.5    Moul, J.W.6
  • 5
    • 0030048476 scopus 로고    scopus 로고
    • Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis
    • Chen C.Y., Faller D.V., Phosphorylation of Bcl-2 protein and association with p21Ras in Ras-induced apoptosis, J. Biol. Chem. 271 (1996) 2376-2379.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2376-2379
    • Chen, C.Y.1    Faller, D.V.2
  • 6
    • 0031034997 scopus 로고    scopus 로고
    • Interaction of CED-4 with CED-3 and CED-9: A molecular framework for cell death
    • Chinnaiyan A.M., O'Rourke K., Lane Br., Dixit V.M., Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death, Science 275 (1997) 1122-1126.
    • (1997) Science , vol.275 , pp. 1122-1126
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Lane, Br.3    Dixit, V.M.4
  • 7
    • 0031449933 scopus 로고    scopus 로고
    • Prediction of the tertiary structure and substrate binding site of caspase-8
    • Chou K.-C., Jones D., Heinrikson R.L., Prediction of the tertiary structure and substrate binding site of caspase-8, FEBS 419 (1997) 49-54.
    • (1997) FEBS , vol.419 , pp. 49-54
    • Chou, K.-C.1    Jones, D.2    Heinrikson, R.L.3
  • 9
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., Nagata S., A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD, Nature 391 (1998) 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 11
    • 0029658983 scopus 로고    scopus 로고
    • Bax and Bcl-xs are induced at the onset of apoptosis in involuting mammary epithelial cells
    • Heermeier K., Benedict M., Li M., Furth P., Nanez G., Hennighausen I., Bax and Bcl-xs are induced at the onset of apoptosis in involuting mammary epithelial cells, Mech. Dev. 56 (1996) 197-207.
    • (1996) Mech. Dev. , vol.56 , pp. 197-207
    • Heermeier, K.1    Benedict, M.2    Li, M.3    Furth, P.4    Nanez, G.5    Hennighausen, I.6
  • 12
    • 0025835716 scopus 로고
    • Bcl-2 protein is topographically restricted in tissues characterised by apoptotic cell death
    • Hockenbery D.M., Zulter M., Hickey W., Nahm M., Korsmeyer S.J., Bcl-2 protein is topographically restricted in tissues characterised by apoptotic cell death, Proc. Natl. Acad. Sci. USA 88 (1991) 6961-6965.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6961-6965
    • Hockenbery, D.M.1    Zulter, M.2    Hickey, W.3    Nahm, M.4    Korsmeyer, S.J.5
  • 14
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-xL during apoptosis
    • Hsu Y.-T., Wolter K.G., Youle R.J., Cytosol-to-membrane redistribution of Bax and Bcl-xL during apoptosis, Biochemistry 94 (1997) 3668-3672.
    • (1997) Biochemistry , vol.94 , pp. 3668-3672
    • Hsu, Y.-T.1    Wolter, K.G.2    Youle, R.J.3
  • 16
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., Currie A.R., Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics, Br. J. Cancer 26 (1972) 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 17
    • 0031897258 scopus 로고    scopus 로고
    • Proteolytic activities that mediate apoptosis
    • Kidd V.J., Proteolytic activities that mediate apoptosis, Annu. Rev. Physiol. 60 (1998) 533-573.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 533-573
    • Kidd, V.J.1
  • 18
    • 9844226204 scopus 로고    scopus 로고
    • Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: Differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis
    • Kitanaka C., Namiki T., Noguchi K., Mochizuki T., Kagaya S., Chi S., Hayashi A., Asai A., Tsujimoto Y., Kuchino Y., Caspase-dependent apoptosis of COS-7 cells induced by Bax overexpression: differential effects of Bcl-2 and Bcl-xL on Bax-induced caspase activation and apoptosis, Oncogene 15 (1997) 1763-1772.
    • (1997) Oncogene , vol.15 , pp. 1763-1772
    • Kitanaka, C.1    Namiki, T.2    Noguchi, K.3    Mochizuki, T.4    Kagaya, S.5    Chi, S.6    Hayashi, A.7    Asai, A.8    Tsujimoto, Y.9    Kuchino, Y.10
  • 19
    • 0028036895 scopus 로고
    • Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2
    • Krajewski S., Krajewska M., Shabaik A., Miyashita T., Wang H.G., Reed J.C., Immunohistochemical determination of in vivo distribution of Bax, a dominant inhibitor of Bcl-2, Am. J. Pathol. 145 (1994) 1323-1336.
    • (1994) Am. J. Pathol. , vol.145 , pp. 1323-1336
    • Krajewski, S.1    Krajewska, M.2    Shabaik, A.3    Miyashita, T.4    Wang, H.G.5    Reed, J.C.6
  • 20
    • 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. 3 (1997) 614-619.
    • (1997) Nat. Med. , vol.3 , pp. 614-619
    • Kroemer, G.1
  • 21
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta-converting enzyme
    • Kuida K., Lippke J.A., Ku G., Harding M.W., Livingston D.J., Su M.S., Flavell R.A., Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta-converting enzyme, Science 267 (1995) 2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.6    Flavell, R.A.7
  • 22
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein
    • Kurschner C., Morgan J.I., Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein, Mol. Brain Res. 37 (1996) 249-258.
    • (1996) Mol. Brain Res. , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.I.2
  • 25
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X., Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c, Cell 86 (1996) 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
  • 26
    • 0029938521 scopus 로고    scopus 로고
    • The role of calcium in the regulation of apoptosis
    • McConkey D.J., Orrenius S., The role of calcium in the regulation of apoptosis. J. Leuk. Biol. 59 (1996) 775-783.
    • (1996) J. Leuk. Biol. , vol.59 , pp. 775-783
    • McConkey, D.J.1    Orrenius, S.2
  • 28
    • 0031036123 scopus 로고    scopus 로고
    • Apoptosis is accompanied by changes in Bcl-2 and Bax expression, induced by loss of attachment, and inhibited by specific extracellular matrix proteins in mammary epithelial cells
    • Merlo G.R., Cella N., Hynes N.F., Apoptosis is accompanied by changes in Bcl-2 and Bax expression, induced by loss of attachment, and inhibited by specific extracellular matrix proteins in mammary epithelial cells, Cell Growth Diff. 8 (1997) 251-260.
    • (1997) Cell Growth Diff. , vol.8 , pp. 251-260
    • Merlo, G.R.1    Cella, N.2    Hynes, N.F.3
  • 32
    • 0032513236 scopus 로고    scopus 로고
    • The binding properties and biological activities of Bcl-2 and Bax in cells exposed to apoptotic stimuli
    • Otter I., Conus S., Ravn U., Rager M., Olivier R., Monney L., Fabbro D., Borner Ch., The binding properties and biological activities of Bcl-2 and Bax in cells exposed to apoptotic stimuli, J. Biol. Chem. 273 (1998) 6110-6120.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6110-6120
    • Otter, I.1    Conus, S.2    Ravn, U.3    Rager, M.4    Olivier, R.5    Monney, L.6    Fabbro, D.7    Borner, Ch.8
  • 33
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan G., Humke E.W., Dixit V.M., Activation of caspases triggered by cytochrome c in vitro, FEBS Lett. 426 (1998) 151-154.
    • (1998) FEBS Lett. , vol.426 , pp. 151-154
    • Pan, G.1    Humke, E.W.2    Dixit, V.M.3
  • 34
    • 1842333237 scopus 로고    scopus 로고
    • Intraleukin-3-induced phosphorylation of BAD through the protein kinase Akt
    • del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G., Intraleukin-3-induced phosphorylation of BAD through the protein kinase Akt, Science 278 (1997) 687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Gonzalez-Garcia, M.2    Page, C.3    Herrera, R.4    Nunez, G.5
  • 35
    • 0346217883 scopus 로고    scopus 로고
    • Antiapoptotic action of prolactin is associated with up-regulation of Bcl-2 and down-regulation of Bax in HC11 mouse mammary epithelial cells
    • Ploszaj T., Motyl T., Orechowski A., Zimowska W., Wareski P., Skierski J., Zwierzchowski L., Antiapoptotic action of prolactin is associated with up-regulation of Bcl-2 and down-regulation of Bax in HC11 mouse mammary epithelial cells, Apoptosis 3 (1998) 1-10.
    • (1998) Apoptosis , vol.3 , pp. 1-10
    • Ploszaj, T.1    Motyl, T.2    Orechowski, A.3    Zimowska, W.4    Wareski, P.5    Skierski, J.6    Zwierzchowski, L.7
  • 36
    • 0030255449 scopus 로고    scopus 로고
    • Mechanisms of Bcl-2 family protein function and dysfunction in health and disease
    • Reed C.J., Mechanisms of Bcl-2 family protein function and dysfunction in health and disease, Behring Inst. Mitt. 97 (1996) 72-100.
    • (1996) Behring Inst. Mitt. , vol.97 , pp. 72-100
    • Reed, C.J.1
  • 39
    • 0022546957 scopus 로고
    • Analysis of the structure, transcripts, and protein products of Bcl-2, the gene involved in human follicular lymphoma
    • Tsujimoto Y., Croce C.M., Analysis of the structure, transcripts, and protein products of Bcl-2, the gene involved in human follicular lymphoma, Proc. Natl. Acad. Sci. 83 (1986) 5214-5218.
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 40
    • 0021821903 scopus 로고
    • Involvement of the Bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y., Cossmann J., Jaffe E., Croce C., Involvement of the Bcl-2 gene in human follicular lymphoma, Science 228 (1985) 1440-1443.
    • (1985) Science , vol.228 , pp. 1440-1443
    • Tsujimoto, Y.1    Cossmann, J.2    Jaffe, E.3    Croce, C.4
  • 41
    • 0030740251 scopus 로고    scopus 로고
    • CED-4 - The third horseman of apoptosis
    • Vaux D.L., CED-4 - the third horseman of apoptosis, Cell 90 (1997) 389-390.
    • (1997) Cell , vol.90 , pp. 389-390
    • Vaux, D.L.1
  • 47
    • 0030848374 scopus 로고    scopus 로고
    • Mitochondrial implication in accidental and programmed cell death: Apoptosis and necrosis
    • Zamzami N., Hirsch T., Dallaporta B., Petit P.X., Kroemer G., Mitochondrial implication in accidental and programmed cell death: apoptosis and necrosis, J. Bioenerg. Biomembr. 29 (1997) 185-193.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 185-193
    • Zamzami, N.1    Hirsch, T.2    Dallaporta, B.3    Petit, P.X.4    Kroemer, G.5
  • 48
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-XL
    • Zha J., Harada H., Yang E., Jockel J., Korsmeyer S.L., Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-XL, Cell 87 (1996) 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.L.5
  • 50
    • 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 W.J., Liu X., Lutschg A., Wang X., Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3, Cell 90 (1997) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.