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Volumn 108, Issue 4, 2009, Pages 1019-1031

Helix 3 is necessary and sufficient for prion protein's anti-Bax function

Author keywords

B cell lymphoma 2 associated protein X; Helix 3; MCF 7 cells; Neuron; Prion protein; Structure function

Indexed keywords

ALANINE; OCTAPEPTIDE; PRION PROTEIN; PROLINE; PROTEIN BAX;

EID: 58549104172     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05851.x     Document Type: Article
Times cited : (6)

References (55)
  • 1
    • 0043208949 scopus 로고    scopus 로고
    • Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/Doppel-induced neurodegeneration
    • Atarashi R., Nishida N., Shigematsu K., Goto S., Kondo T., Sakaguchi S. Katamine S. (2003) Deletion of N-terminal residues 23-88 from prion protein (PrP) abrogates the potential to rescue PrP-deficient mice from PrP-like protein/Doppel-induced neurodegeneration. J. Biol. Chem. 278, 28944 28949.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28944-28949
    • Atarashi, R.1    Nishida, N.2    Shigematsu, K.3    Goto, S.4    Kondo, T.5    Sakaguchi, S.6    Katamine, S.7
  • 2
    • 0027236794 scopus 로고
    • Structural basis of amino acid alpha helix propensity
    • Blaber M., Zhang X. J. Matthews B. W. (1993) Structural basis of amino acid alpha helix propensity. Science 260, 1637 1640.
    • (1993) Science , vol.260 , pp. 1637-1640
    • Blaber, M.1    Zhang, X.J.2    Matthews, B.W.3
  • 3
    • 0035914410 scopus 로고    scopus 로고
    • Prion protein protects human neurons against Bax-mediated apoptosis
    • Bounhar Y., Zhang Y., Goodyer C. G. LeBlanc A. (2001) Prion protein protects human neurons against Bax-mediated apoptosis. J. Biol. Chem. 276, 39145 39149.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39145-39149
    • Bounhar, Y.1    Zhang, Y.2    Goodyer, C.G.3    Leblanc, A.4
  • 4
    • 33751271909 scopus 로고    scopus 로고
    • Prion protein prevents Bax-mediated cell death in the absence of other Bcl-2 family members in Saccharomyces cerevisiae
    • Bounhar Y., Mann K. K., Roucou X. LeBlanc A. C. (2006) Prion protein prevents Bax-mediated cell death in the absence of other Bcl-2 family members in Saccharomyces cerevisiae. FEMS Yeast Res. 6, 1204 1212.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 1204-1212
    • Bounhar, Y.1    Mann, K.K.2    Roucou, X.3    Leblanc, A.C.4
  • 5
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown D. R., Schulz-Schaeffer W. J., Schmidt B. Kretzschmar H. A. (1997a) Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146, 104 112.
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 6
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown D. R., Qin K., Herms J. W. et al. (1997b) The cellular prion protein binds copper in vivo. Nature 390, 684 687.
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1    Qin, K.2    Herms, J.W.3
  • 7
    • 0033571055 scopus 로고    scopus 로고
    • Normal prion protein has an activity like that of superoxide dismutase
    • Brown D. R., Wong B. S., Hafiz F., Clive C., Haswell S. J. Jones I. M. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344 (Pt. 1 1 5.
    • (1999) Biochem. J. , vol.344 , Issue.1 , pp. 1-5
    • Brown, D.R.1    Wong, B.S.2    Hafiz, F.3    Clive, C.4    Haswell, S.J.5    Jones, I.M.6
  • 9
    • 33747183020 scopus 로고    scopus 로고
    • Axotomy-induced motoneuron death is delayed in mice overexpressing PrPc
    • Coulpier M., Messiaen S., Boucreaux D. Eloit M. (2006) Axotomy-induced motoneuron death is delayed in mice overexpressing PrPc. Neuroscience 141, 1827 1834.
    • (2006) Neuroscience , vol.141 , pp. 1827-1834
    • Coulpier, M.1    Messiaen, S.2    Boucreaux, D.3    Eloit, M.4
  • 11
    • 9144239220 scopus 로고    scopus 로고
    • Prion protein prevents human breast carcinoma cell line from tumor necrosis factor alpha-induced cell death
    • Diarra-Mehrpour M., Arrabal S., Jalil A. et al. (2004) Prion protein prevents human breast carcinoma cell line from tumor necrosis factor alpha-induced cell death. Cancer Res. 64, 719 727.
    • (2004) Cancer Res. , vol.64 , pp. 719-727
    • Diarra-Mehrpour, M.1    Arrabal, S.2    Jalil, A.3
  • 13
    • 19944427251 scopus 로고    scopus 로고
    • Genetic mapping of activity determinants within cellular prion proteins: N-terminal modules in PrPC offset pro-apoptotic activity of the Doppel helix B/B′ region
    • Drisaldi B., Coomaraswamy J., Mastrangelo P. et al. (2004) Genetic mapping of activity determinants within cellular prion proteins: N-terminal modules in PrPC offset pro-apoptotic activity of the Doppel helix B/B′ region. J. Biol. Chem. 279, 55443 55454.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55443-55454
    • Drisaldi, B.1    Coomaraswamy, J.2    Mastrangelo, P.3
  • 15
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard L. Helenius A. (2001) ER quality control: towards an understanding at the molecular level. Curr. Opin. Cell Biol. 13, 431 437.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 16
    • 20044381672 scopus 로고    scopus 로고
    • Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: The disease associated D202N mutation destabilizes the helical conformation
    • Gallo M., Paludi D., Cicero D. O. et al. (2005) Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation. Int. J. Immunopathol. Pharmacol. 18, 95 112.
    • (2005) Int. J. Immunopathol. Pharmacol. , vol.18 , pp. 95-112
    • Gallo, M.1    Paludi, D.2    Cicero, D.O.3
  • 17
    • 34248351522 scopus 로고    scopus 로고
    • Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants
    • Jodoin J., Laroche-Pierre S., Goodyer C. G. LeBlanc A. C. (2007) Defective retrotranslocation causes loss of anti-Bax function in human familial prion protein mutants. J. Neurosci. 27, 5081 5091.
    • (2007) J. Neurosci. , vol.27 , pp. 5081-5091
    • Jodoin, J.1    Laroche-Pierre, S.2    Goodyer, C.G.3    Leblanc, A.C.4
  • 18
    • 0033860451 scopus 로고    scopus 로고
    • Effect of proteasome inhibitors on the release into the cytosol of free polymannose oligosaccharides from glycoproteins
    • Karaivanova V. K. Spiro R. G. (2000) Effect of proteasome inhibitors on the release into the cytosol of free polymannose oligosaccharides from glycoproteins. Glycobiology 10, 727 735.
    • (2000) Glycobiology , vol.10 , pp. 727-735
    • Karaivanova, V.K.1    Spiro, R.G.2
  • 20
    • 15744398507 scopus 로고    scopus 로고
    • Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor
    • Kiachopoulos S., Bracher A., Winklhofer K. F. Tatzelt J. (2005) Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. J. Biol. Chem. 280, 9320 9329.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9320-9329
    • Kiachopoulos, S.1    Bracher, A.2    Winklhofer, K.F.3    Tatzelt, J.4
  • 21
    • 38849125000 scopus 로고    scopus 로고
    • In silico comparative analysis of DNA and amino acid sequences for prion protein gene
    • Kim Y., Lee J. Lee C. (2008) In silico comparative analysis of DNA and amino acid sequences for prion protein gene. Transbound. Emerg. Dis. 55, 105 114.
    • (2008) Transbound. Emerg. Dis. , vol.55 , pp. 105-114
    • Kim, Y.1    Lee, J.2    Lee, C.3
  • 22
    • 0033566067 scopus 로고    scopus 로고
    • Prions prevent neuronal cell-line death
    • Kuwahara C., Takeuchi A. M., Nishimura T. et al. (1999) Prions prevent neuronal cell-line death. Nature 400, 225 226.
    • (1999) Nature , vol.400 , pp. 225-226
    • Kuwahara, C.1    Takeuchi, A.M.2    Nishimura, T.3
  • 23
    • 0242674782 scopus 로고    scopus 로고
    • Unravelling the controversy of prion diseases
    • in. Wang, E. Snyder, S., eds), pp. Academic Press, New York.
    • LeBlanc A. (1998) Unravelling the controversy of prion diseases, in Handbook of the Aging Brain (Wang E. Snyder S., eds), pp. 202 214. Academic Press, New York.
    • (1998) Handbook of the Aging Brain , pp. 202-214
    • Leblanc, A.1
  • 25
    • 20444454586 scopus 로고    scopus 로고
    • Mammalian prion protein suppresses Bax-induced cell death in yeast
    • Li A. Harris D. A. (2005) Mammalian prion protein suppresses Bax-induced cell death in yeast. J. Biol. Chem. 280, 17430 17434.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17430-17434
    • Li, A.1    Harris, D.A.2
  • 26
    • 33646105873 scopus 로고    scopus 로고
    • Overexpression of PrPC and its antiapoptosis function in gastric cancer
    • Liang J., Pan Y. L., Ning X. X. et al. (2006) Overexpression of PrPC and its antiapoptosis function in gastric cancer. Tumour Biol. 27, 84 91.
    • (2006) Tumour Biol. , vol.27 , pp. 84-91
    • Liang, J.1    Pan, Y.L.2    Ning, X.X.3
  • 27
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • Liemann S. Glockshuber R. (1999) Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein. Biochem. 38, 3258 3267.
    • (1999) Biochem. , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2
  • 28
    • 50849114500 scopus 로고    scopus 로고
    • Cytosolic prion protein is the predominant anti-Bax prion protein form: Exclusion of transmembrane and secreted prion protein forms in the anti-Bax function
    • Lin D. T., Jodoin J., Baril M., Goodyer C. G. LeBlanc A. C. (2008) Cytosolic prion protein is the predominant anti-Bax prion protein form: exclusion of transmembrane and secreted prion protein forms in the anti-Bax function. Biochim. Biophys. Acta Mol. Cell Res. 1783, 2001 2012.
    • (2008) Biochim. Biophys. Acta Mol. Cell Res. , vol.1783 , pp. 2001-2012
    • Lin, D.T.1    Jodoin, J.2    Baril, M.3    Goodyer, C.G.4    Leblanc, A.C.5
  • 29
    • 0035910069 scopus 로고    scopus 로고
    • Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation
    • Ma J. Lindquist S. (2001) Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl Acad. Sci. USA 98, 14955 14960.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14955-14960
    • Ma, J.1    Lindquist, S.2
  • 30
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley M. P., Bolton D. C. Prusiner S. B. (1983) A protease-resistant protein is a structural component of the scrapie prion. Cell 35, 57 62.
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 31
    • 36349016768 scopus 로고    scopus 로고
    • Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death
    • Meslin F., Hamai A., Gao P., Jalil A., Cahuzac N., Chouaib S. Mehrpour M. (2007a) Silencing of prion protein sensitizes breast adriamycin-resistant carcinoma cells to TRAIL-mediated cell death. Cancer Res. 67, 10910 10919.
    • (2007) Cancer Res. , vol.67 , pp. 10910-10919
    • Meslin, F.1    Hamai, A.2    Gao, P.3    Jalil, A.4    Cahuzac, N.5    Chouaib, S.6    Mehrpour, M.7
  • 32
    • 36148932985 scopus 로고    scopus 로고
    • Efficacy of adjuvant chemotherapy according to prion protein expression in patients with estrogen receptor-negative breast cancer
    • Meslin F., Conforti R., Mazouni C. et al. (2007b) Efficacy of adjuvant chemotherapy according to prion protein expression in patients with estrogen receptor-negative breast cancer. Ann. Oncol. 18, 1793 1798.
    • (2007) Ann. Oncol. , vol.18 , pp. 1793-1798
    • Meslin, F.1    Conforti, R.2    Mazouni, C.3
  • 36
    • 0030811015 scopus 로고    scopus 로고
    • Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix
    • Muramoto T., DeArmond S. J., Scott M., Telling G. C., Cohen F. E. Prusiner S. B. (1997) Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an alpha-helix. Nat. Med. 3, 750 755.
    • (1997) Nat. Med. , vol.3 , pp. 750-755
    • Muramoto, T.1    Dearmond, S.J.2    Scott, M.3    Telling, G.C.4    Cohen, F.E.5    Prusiner, S.B.6
  • 37
    • 35248890542 scopus 로고    scopus 로고
    • Bcl-2 overexpression delays caspase-3 activation and rescues cerebellar degeneration in prion-deficient mice that overexpress amino-terminally truncated prion
    • Nicolas O., Gavin R., Braun N., Urena J. M., Fontana X., Soriano E., Aguzzi A. Antonio del Rio J. (2007) Bcl-2 overexpression delays caspase-3 activation and rescues cerebellar degeneration in prion-deficient mice that overexpress amino-terminally truncated prion. FASEB J. 21, 3107 3117.
    • (2007) FASEB J. , vol.21 , pp. 3107-3117
    • Nicolas, O.1    Gavin, R.2    Braun, N.3    Urena, J.M.4    Fontana, X.5    Soriano, E.6    Aguzzi, A.7    Antonio Del Rio, J.8
  • 39
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi W., Vilette D., Guiraud P., Arlotto M., Riondel J., Laude H., Lehmann S. Favier A. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J. Biol. Chem. 278, 9064 9072.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6    Lehmann, S.7    Favier, A.8
  • 41
    • 0142135128 scopus 로고    scopus 로고
    • Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons
    • Roucou X., Guo Q., Zhang Y., Goodyer C. G. LeBlanc A. C. (2003) Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons. J. Biol. Chem. 278, 40877 40881.
    • (2003) J. Biol. Chem. , vol.278 , pp. 40877-40881
    • Roucou, X.1    Guo, Q.2    Zhang, Y.3    Goodyer, C.G.4    Leblanc, A.C.5
  • 42
    • 0346729697 scopus 로고    scopus 로고
    • Neuroprotective functions of prion protein
    • Roucou X., Gains M. LeBlanc A. C. (2004) Neuroprotective functions of prion protein. J. Neurosci. Res. 75, 153 161.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 153-161
    • Roucou, X.1    Gains, M.2    Leblanc, A.C.3
  • 43
    • 21744447704 scopus 로고    scopus 로고
    • Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells
    • Roucou X., Giannopoulos P. N., Zhang Y., Jodoin J., Goodyer C. G. LeBlanc A. (2005) Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells. Cell Death Differ. 12, 783 795.
    • (2005) Cell Death Differ. , vol.12 , pp. 783-795
    • Roucou, X.1    Giannopoulos, P.N.2    Zhang, Y.3    Jodoin, J.4    Goodyer, C.G.5    Leblanc, A.6
  • 45
    • 0015762456 scopus 로고
    • A human cell line from a pleural effusion derived from a breast carcinoma
    • Soule H. D., Vazguez J., Long A., Albert S. Brennan M. (1973) A human cell line from a pleural effusion derived from a breast carcinoma. J. Natl Cancer Inst. 51, 1409 1416.
    • (1973) J. Natl Cancer Inst. , vol.51 , pp. 1409-1416
    • Soule, H.D.1    Vazguez, J.2    Long, A.3    Albert, S.4    Brennan, M.5
  • 46
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki W., Petersen R. B., Gambetti P. Surewicz W. K. (1998) Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem. 273, 31048 31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 47
    • 0037073678 scopus 로고    scopus 로고
    • Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form
    • Vanik D. L. Surewicz W. K. (2002) Disease-associated F198S mutation increases the propensity of the recombinant prion protein for conformational conversion to scrapie-like form. J. Biol. Chem. 277, 49065 49070.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49065-49070
    • Vanik, D.L.1    Surewicz, W.K.2
  • 48
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles J. H., Cohen F. E., Prusiner S. B., Goodin D. B., Wright P. E. Dyson H. J. (1999) Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl Acad. Sci. USA 96, 2042 2047.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, H.J.6
  • 49
    • 33745953139 scopus 로고    scopus 로고
    • BCL-2 in the crosshairs: Tipping the balance of life and death
    • Walensky L. D. (2006) BCL-2 in the crosshairs: tipping the balance of life and death. Cell Death Differ. 13, 1339 1350.
    • (2006) Cell Death Differ. , vol.13 , pp. 1339-1350
    • Walensky, L.D.1
  • 51
    • 0035476688 scopus 로고    scopus 로고
    • Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein
    • Yedidia Y., Horonchik L., Tzaban S., Yanai A. Taraboulos A. (2001) Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein. EMBO J. 20, 5383 5391.
    • (2001) EMBO J. , vol.20 , pp. 5383-5391
    • Yedidia, Y.1    Horonchik, L.2    Tzaban, S.3    Yanai, A.4    Taraboulos, A.5
  • 52
    • 0028206341 scopus 로고
    • BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax
    • Yin X.-M., Oltvai Z. N. Korsmeyer S. J. (1994) BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature 369, 321 323.
    • (1994) Nature , vol.369 , pp. 321-323
    • Yin, X.-M.1    Oltvai, Z.N.2    Korsmeyer, S.J.3
  • 54
    • 18444397736 scopus 로고    scopus 로고
    • Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection
    • Zanata S. M., Lopes M. H., Mercadante A. F. et al. (2002) Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J. 21, 3307 3316.
    • (2002) EMBO J. , vol.21 , pp. 3307-3316
    • Zanata, S.M.1    Lopes, M.H.2    Mercadante, A.F.3


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