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Volumn 68, Issue 14, 2008, Pages 5648-5657

SerpinB2 protection of retinoblastoma protein from calpain enhances tumor cell survival

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CALPASTATIN; LYSINE; PLASMINOGEN ACTIVATOR INHIBITOR 2; PROTEASOME; RETINOBLASTOMA PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 48649098028     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-07-5850     Document Type: Article
Times cited : (53)

References (48)
  • 1
    • 33748067733 scopus 로고    scopus 로고
    • Retinoblastoma family genes
    • Du W, Pogoriler J. Retinoblastoma family genes. Oncogene 2006;25:5190-200.
    • (2006) Oncogene , vol.25 , pp. 5190-5200
    • Du, W.1    Pogoriler, J.2
  • 2
    • 0037313618 scopus 로고    scopus 로고
    • Coordinated regulation of life and death by RB
    • Chau BN, Wang JY. Coordinated regulation of life and death by RB. Nat Rev Cancer 2003;3:130-8.
    • (2003) Nat Rev Cancer , vol.3 , pp. 130-138
    • Chau, B.N.1    Wang, J.Y.2
  • 5
    • 2342507124 scopus 로고    scopus 로고
    • Differential regulation of apoptotic genes by Rb in human versus mouse cells
    • Young AP, Longmore GD. Differential regulation of apoptotic genes by Rb in human versus mouse cells. Oncogene 2004;23:2587-99.
    • (2004) Oncogene , vol.23 , pp. 2587-2599
    • Young, A.P.1    Longmore, G.D.2
  • 6
    • 19644364034 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic communication in apoptotic response to genotoxic and inflammatory stress
    • Wang JY. Nucleo-cytoplasmic communication in apoptotic response to genotoxic and inflammatory stress. Cell Res 2005;15:43-8.
    • (2005) Cell Res , vol.15 , pp. 43-48
    • Wang, J.Y.1
  • 8
    • 0035252592 scopus 로고    scopus 로고
    • E2Fs regulate the expression of genes involved in differentiation, development, proliferation, and apoptosis
    • Muller H, Bracken AP, Vernell R, et al. E2Fs regulate the expression of genes involved in differentiation, development, proliferation, and apoptosis. Genes Dev 2001;15:267-85.
    • (2001) Genes Dev , vol.15 , pp. 267-285
    • Muller, H.1    Bracken, A.P.2    Vernell, R.3
  • 9
    • 85006277004 scopus 로고    scopus 로고
    • Direct coupling of the cell cycle and cell death machinery by E2F
    • Nahle Z, Polakoff J, Davuluri RV, et al. Direct coupling of the cell cycle and cell death machinery by E2F. Nat Cell Biol 2002;4:859-64.
    • (2002) Nat Cell Biol , vol.4 , pp. 859-864
    • Nahle, Z.1    Polakoff, J.2    Davuluri, R.V.3
  • 10
    • 0042691816 scopus 로고    scopus 로고
    • Inhibition of retinoblastoma protein degradation by interaction with the serpin plasminogen activator inhibitor 2 via a novel consensus motif
    • Darnell GA, Antalis TM, Johnstone RW, et al. Inhibition of retinoblastoma protein degradation by interaction with the serpin plasminogen activator inhibitor 2 via a novel consensus motif. Mol Cell Biol 2003;23:6520-32.
    • (2003) Mol Cell Biol , vol.23 , pp. 6520-6532
    • Darnell, G.A.1    Antalis, T.M.2    Johnstone, R.W.3
  • 11
    • 0028787122 scopus 로고
    • Biological and clinical aspects of plasminogen activator inhibitor type 2
    • Kruithof EK, Baker MS, Bunn CL. Biological and clinical aspects of plasminogen activator inhibitor type 2. Blood 1995;86:4007-24.
    • (1995) Blood , vol.86 , pp. 4007-4024
    • Kruithof, E.K.1    Baker, M.S.2    Bunn, C.L.3
  • 12
    • 0025746246 scopus 로고
    • Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2
    • Kumar S, Baglioni C. Protection from tumor necrosis factor-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2. J Biol Chem 1991;266:20960-4.
    • (1991) J Biol Chem , vol.266 , pp. 20960-20964
    • Kumar, S.1    Baglioni, C.2
  • 13
    • 33646411478 scopus 로고    scopus 로고
    • Induction of the plasminogen activator inhibitor-2 in cells expressing the ZNF198/FGFR1 fusion kinase that is involved in atypical myeloproliferative disease
    • Kasyapa CS, Kunapuli P, Hawthorn L, Cowell JK. Induction of the plasminogen activator inhibitor-2 in cells expressing the ZNF198/FGFR1 fusion kinase that is involved in atypical myeloproliferative disease. Blood 2006;107:3693-9.
    • (2006) Blood , vol.107 , pp. 3693-3699
    • Kasyapa, C.S.1    Kunapuli, P.2    Hawthorn, L.3    Cowell, J.K.4
  • 14
    • 1642380279 scopus 로고    scopus 로고
    • Helicobacter pylori induces plasminogen activator inhibitor 2 in gastric epithelial cells through nuclear factor-κB and RhoA. Implications for invasion and apoptosis
    • Varro A, Noble PJ, Pritchard DM, et al. Helicobacter pylori induces plasminogen activator inhibitor 2 in gastric epithelial cells through nuclear factor-κB and RhoA. Implications for invasion and apoptosis. Cancer Res 2004;64:1695-702.
    • (2004) Cancer Res , vol.64 , pp. 1695-1702
    • Varro, A.1    Noble, P.J.2    Pritchard, D.M.3
  • 15
    • 0035110958 scopus 로고    scopus 로고
    • Overexpression of plasminogen activator inhibitor type 2 in basal keratinocytes enhances papilloma formation in transgenic mice
    • Zhou HM, Bolon I, Nichols A, Wohlwend A, Vassalli JD. Overexpression of plasminogen activator inhibitor type 2 in basal keratinocytes enhances papilloma formation in transgenic mice. Cancer Res 2001;61:970-6.
    • (2001) Cancer Res , vol.61 , pp. 970-976
    • Zhou, H.M.1    Bolon, I.2    Nichols, A.3    Wohlwend, A.4    Vassalli, J.D.5
  • 16
    • 0032101523 scopus 로고    scopus 로고
    • The serine proteinase inhibitor (serpin) plasminogen activation inhibitor type 2 protects against viral cytopathic effects by constitutive interferon α/β priming
    • Antalis TM, La Linn M, Donnan K, et al. The serine proteinase inhibitor (serpin) plasminogen activation inhibitor type 2 protects against viral cytopathic effects by constitutive interferon α/β priming. J Exp Med 1998;187:1799-811.
    • (1998) J Exp Med , vol.187 , pp. 1799-1811
    • Antalis, T.M.1    La Linn, M.2    Donnan, K.3
  • 17
    • 33748464019 scopus 로고    scopus 로고
    • NF-nB translocation prevents host cell death after low-dose challenge by Legionella pneumophila
    • Losick VP, Isberg RR. NF-nB translocation prevents host cell death after low-dose challenge by Legionella pneumophila. J Exp Med 2006;203:2177-89.
    • (2006) J Exp Med , vol.203 , pp. 2177-2189
    • Losick, V.P.1    Isberg, R.R.2
  • 18
    • 0028874970 scopus 로고
    • Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis. Evidence for an alternate biological function
    • Dickinson JL, Bates EJ, Ferrante A, Antalis TM. Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis. Evidence for an alternate biological function. J Biol Chem 1995;270:27894-904.
    • (1995) J Biol Chem , vol.270 , pp. 27894-27904
    • Dickinson, J.L.1    Bates, E.J.2    Ferrante, A.3    Antalis, T.M.4
  • 19
    • 0029127095 scopus 로고
    • Plasminogen activator inhibitor type 2 prevents programmed cell death of human macrophages infected with Mycobacterium avium, serovar 4
    • Gan H, Newman GW, Remold HG. Plasminogen activator inhibitor type 2 prevents programmed cell death of human macrophages infected with Mycobacterium avium, serovar 4. J Immunol 1995;155:1304-15.
    • (1995) J Immunol , vol.155 , pp. 1304-1315
    • Gan, H.1    Newman, G.W.2    Remold, H.G.3
  • 20
    • 0025103776 scopus 로고
    • Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by tumor necrosis factor
    • Pytel BA, Peppel K, Baglioni C. Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by tumor necrosis factor. J Cell Physiol 1990;144:416-22.
    • (1990) J Cell Physiol , vol.144 , pp. 416-422
    • Pytel, B.A.1    Peppel, K.2    Baglioni, C.3
  • 21
    • 0037330709 scopus 로고    scopus 로고
    • Mechanisms by which DNA tumor virus oncoproteins target the Rb family of pocket proteins
    • Helt AM, Galloway DA. Mechanisms by which DNA tumor virus oncoproteins target the Rb family of pocket proteins. Carcinogenesis 2003;24:159-69.
    • (2003) Carcinogenesis , vol.24 , pp. 159-169
    • Helt, A.M.1    Galloway, D.A.2
  • 22
    • 33644770294 scopus 로고    scopus 로고
    • Targeting retinoblastoma protein for degradation by proteasomes
    • Ying H, Xiao ZX. Targeting retinoblastoma protein for degradation by proteasomes. Cell Cycle 2006;5:506-8.
    • (2006) Cell Cycle , vol.5 , pp. 506-508
    • Ying, H.1    Xiao, Z.X.2
  • 23
    • 0032031417 scopus 로고    scopus 로고
    • The caspase-RB connection in cell death
    • Tan X, Wang JY. The caspase-RB connection in cell death. Trends Cell Biol 1998;8:116-20.
    • (1998) Trends Cell Biol , vol.8 , pp. 116-120
    • Tan, X.1    Wang, J.Y.2
  • 24
    • 0030899360 scopus 로고    scopus 로고
    • Degradation of retinoblastoma protein in tumor necrosis factorand CD95-induced cell death
    • Tan X, Martin SJ, Green DR, Wang JY. Degradation of retinoblastoma protein in tumor necrosis factorand CD95-induced cell death. J Biol Chem 1997;272:9613-16.
    • (1997) J Biol Chem , vol.272 , pp. 9613-9616
    • Tan, X.1    Martin, S.J.2    Green, D.R.3    Wang, J.Y.4
  • 27
    • 0034936674 scopus 로고    scopus 로고
    • Calpain function in the modulation of signal transduction molecules
    • Sato K, Kawashima S. Calpain function in the modulation of signal transduction molecules. Biol Chem 2001;382:743-51.
    • (2001) Biol Chem , vol.382 , pp. 743-751
    • Sato, K.1    Kawashima, S.2
  • 28
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4. calpain is essential for embryonic development but not for cell growth and division
    • Arthur JS, Elce JS, Hegadorn C, Williams K, Greer PA. Disruption of the murine calpain small subunit gene, Capn4. calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 2000;20:4474-81.
    • (2000) Mol Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 29
    • 0029048989 scopus 로고
    • Casein zymography. a method to study A-calpain, μ-calpain, and their inhibitory agents
    • Raser KJ, Posner A, Wang KK. Casein zymography. a method to study A-calpain, μ-calpain, and their inhibitory agents. Arch Biochem Biophys 1995;319:211-16.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.3
  • 31
    • 0032402111 scopus 로고    scopus 로고
    • Proteasome inhibitors induce apoptosis in glucocorticoid-resistant chronic lymphocytic leukemic lymphocytes
    • Chandra J, Niemer I, Gilbreath J, et al. Proteasome inhibitors induce apoptosis in glucocorticoid-resistant chronic lymphocytic leukemic lymphocytes. Blood 1998;92:4220-9.
    • (1998) Blood , vol.92 , pp. 4220-4229
    • Chandra, J.1    Niemer, I.2    Gilbreath, J.3
  • 32
    • 2442718801 scopus 로고    scopus 로고
    • On the sequential determinants of calpain cleavage
    • Tompa P, Buzder-Lantos P, Tantos A, et al. On the sequential determinants of calpain cleavage. J Biol Chem 2004;279:20775-85.
    • (2004) J Biol Chem , vol.279 , pp. 20775-20785
    • Tompa, P.1    Buzder-Lantos, P.2    Tantos, A.3
  • 33
    • 0033832629 scopus 로고    scopus 로고
    • Noncaspase proteases in apoptosis
    • Johnson DE. Noncaspase proteases in apoptosis. Leukemia 2000;14:1695-703.
    • (2000) Leukemia , vol.14 , pp. 1695-1703
    • Johnson, D.E.1
  • 34
    • 1242272925 scopus 로고    scopus 로고
    • Differences in stability of repressor complexes at promoters underlie distinct roles for Rb family members
    • Young AP, Longmore GD. Differences in stability of repressor complexes at promoters underlie distinct roles for Rb family members. Oncogene 2004;23:814-23.
    • (2004) Oncogene , vol.23 , pp. 814-823
    • Young, A.P.1    Longmore, G.D.2
  • 35
    • 33645285881 scopus 로고    scopus 로고
    • Is the loss of pRb essential for the mouse skin carcinogenesis?
    • Ruiz S, Santos M, Paramio JM. Is the loss of pRb essential for the mouse skin carcinogenesis? Cell Cycle 2006;5:625-9.
    • (2006) Cell Cycle , vol.5 , pp. 625-629
    • Ruiz, S.1    Santos, M.2    Paramio, J.M.3
  • 36
    • 0027496668 scopus 로고
    • FVB/N mice. an inbred strain sensitive to the chemical induction of squamous cell carcinomas in the skin
    • Hennings H, Glick AB, Lowry DT, Krsmanovic LS, Sly LM, Yuspa SH. FVB/N mice. an inbred strain sensitive to the chemical induction of squamous cell carcinomas in the skin. Carcinogenesis 1993;14:2353-8.
    • (1993) Carcinogenesis , vol.14 , pp. 2353-2358
    • Hennings, H.1    Glick, A.B.2    Lowry, D.T.3    Krsmanovic, L.S.4    Sly, L.M.5    Yuspa, S.H.6
  • 37
    • 1842553539 scopus 로고    scopus 로고
    • An anti-tumor necrosis factor-α antibody inhibits the development of experimental skin tumors
    • Scott KA, Moore RJ, Arnott CH, et al. An anti-tumor necrosis factor-α antibody inhibits the development of experimental skin tumors. Mol Cancer Ther 2003;2:445-51.
    • (2003) Mol Cancer Ther , vol.2 , pp. 445-451
    • Scott, K.A.1    Moore, R.J.2    Arnott, C.H.3
  • 38
    • 33745826605 scopus 로고    scopus 로고
    • Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli
    • Tan Y, Wu C, De Veyra T, Greer PA. Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli. J Biol Chem 2006;281:17689-98.
    • (2006) J Biol Chem , vol.281 , pp. 17689-17698
    • Tan, Y.1    Wu, C.2    De Veyra, T.3    Greer, P.A.4
  • 39
    • 0031862730 scopus 로고    scopus 로고
    • Growth suppression by an E2F-binding-defective retinoblastoma protein (RB). contribution from the RB C pocket
    • Whitaker LL, Su H, Baskaran R, Knudsen ES, Wang JY. Growth suppression by an E2F-binding-defective retinoblastoma protein (RB). contribution from the RB C pocket. Mol Cell Biol 1998;18:4032-42.
    • (1998) Mol Cell Biol , vol.18 , pp. 4032-4042
    • Whitaker, L.L.1    Su, H.2    Baskaran, R.3    Knudsen, E.S.4    Wang, J.Y.5
  • 40
    • 0141927097 scopus 로고    scopus 로고
    • pRB contains an E2F1-specific binding domain that allows E2F1-induced apoptosis to be regulated separately from other E2F activities
    • Dick FA, Dyson N. pRB contains an E2F1-specific binding domain that allows E2F1-induced apoptosis to be regulated separately from other E2F activities. Mol Cell 2003;12:639-49.
    • (2003) Mol Cell , vol.12 , pp. 639-649
    • Dick, F.A.1    Dyson, N.2
  • 41
    • 0027393310 scopus 로고
    • The ovalbumin family of serpin proteins
    • Remold-O'Donnell E. The ovalbumin family of serpin proteins. FEBS Lett 1993;315:105-8.
    • (1993) FEBS Lett , vol.315 , pp. 105-108
    • Remold-O'Donnell, E.1
  • 42
    • 0032250184 scopus 로고    scopus 로고
    • Serpins and regulation of cell death
    • Bird PI. Serpins and regulation of cell death. Results Probl Cell Differ 1998;24:63-89.
    • (1998) Results Probl Cell Differ , vol.24 , pp. 63-89
    • Bird, P.I.1
  • 44
    • 0036661117 scopus 로고    scopus 로고
    • Aberrant expression of serpin squamous cell carcinoma antigen 2 in human tumor tissues and cell lines. evidence of protection from tumor necrosis factor-mediated apoptosis
    • Takeda A, Kajiya A, Iwasawa A, Nakamura Y, Hibino T. Aberrant expression of serpin squamous cell carcinoma antigen 2 in human tumor tissues and cell lines. evidence of protection from tumor necrosis factor-mediated apoptosis. Biol Chem 2002;383:1231-6.
    • (2002) Biol Chem , vol.383 , pp. 1231-1236
    • Takeda, A.1    Kajiya, A.2    Iwasawa, A.3    Nakamura, Y.4    Hibino, T.5
  • 45
    • 0034714281 scopus 로고    scopus 로고
    • Protease inhibitor 10 inhibits tumor necrosis factor α-induced cell death. Evidence for the formation of intracellular high Mr protease inhibitor 10-containing complexes
    • Schleef RR, Chuang TL. Protease inhibitor 10 inhibits tumor necrosis factor α-induced cell death. Evidence for the formation of intracellular high Mr protease inhibitor 10-containing complexes. J Biol Chem 2000;275:26385-9.
    • (2000) J Biol Chem , vol.275 , pp. 26385-26389
    • Schleef, R.R.1    Chuang, T.L.2
  • 46
    • 0038408712 scopus 로고    scopus 로고
    • Hurpin is a selective inhibitor of lysosomal cathepsin Land protects keratinocytes from ultraviolet-induced apoptosis
    • Welss T, Sun J, Irving JA, et al. Hurpin is a selective inhibitor of lysosomal cathepsin Land protects keratinocytes from ultraviolet-induced apoptosis. Biochemistry 2003;42:7381-9.
    • (2003) Biochemistry , vol.42 , pp. 7381-7389
    • Welss, T.1    Sun, J.2    Irving, J.A.3
  • 48
    • 3042813439 scopus 로고    scopus 로고
    • Unique and overlapping functions of pRb and p107 in the control of proliferation and differentiation in epidermis
    • Ruiz S, Santos M, Segrelles C, et al. Unique and overlapping functions of pRb and p107 in the control of proliferation and differentiation in epidermis. Development 2004;131:2737-48.
    • (2004) Development , vol.131 , pp. 2737-2748
    • Ruiz, S.1    Santos, M.2    Segrelles, C.3


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