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Volumn 105, Issue 36, 2008, Pages 13626-13631

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease

Author keywords

HSF1; Neurodegeneration; Protein misfolding; Prp; Transmissible spongiform encephalopathy

Indexed keywords

HEAT SHOCK FACTOR 1; HEAT SHOCK PROTEIN; PRION PROTEIN; PROTEINASE K; UNCLASSIFIED DRUG;

EID: 51649130437     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0806319105     Document Type: Article
Times cited : (63)

References (55)
  • 2
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS (2006) Prions and their partners in crime. Nature 443:803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 4
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G, et al. (2003) Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302:871-874.
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1
  • 6
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 7
    • 2342620357 scopus 로고
    • Localization of RNA from heat-induced polysomes at puff sites in Drosophila melanogaster
    • McKenzie SL, Henikoff S, Meselson M (1975) Localization of RNA from heat-induced polysomes at puff sites in Drosophila melanogaster. Proc Natl Acad Sci USA 72:1117-1121.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1117-1121
    • McKenzie, S.L.1    Henikoff, S.2    Meselson, M.3
  • 9
    • 0033655148 scopus 로고    scopus 로고
    • Analysis of the mammalian heat-shock response. Inducible gene expression and heat-shock factor activity
    • Mathew A, Shi Y, Jolly C, Morimoto RI (2000) Analysis of the mammalian heat-shock response. Inducible gene expression and heat-shock factor activity. Methods Mol Biol 99:217-255.
    • (2000) Methods Mol Biol , vol.99 , pp. 217-255
    • Mathew, A.1    Shi, Y.2    Jolly, C.3    Morimoto, R.I.4
  • 10
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide SD, Morimoto RI (2005) Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 280:33097-330100.
    • (2005) J Biol Chem , vol.280 , pp. 33097-330100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 11
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R (1998) Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94:471-480.
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 12
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev 12:654-666.
    • (1998) Genes Dev , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 13
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • Sarge KD, Murphy SP, Morimoto RI (1993) Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol Cell Biol 13:1392-1407.
    • (1993) Mol Cell Biol , vol.13 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 14
    • 0027159173 scopus 로고
    • Activation of Drosophila heat shock factor: Conformational change associated with a monomer-to-trimer transition
    • Westwood JT, Wu C (1993) Activation of Drosophila heat shock factor: conformational change associated with a monomer-to-trimer transition. Mol Cell Biol 13:3481-3486.
    • (1993) Mol Cell Biol , vol.13 , pp. 3481-3486
    • Westwood, J.T.1    Wu, C.2
  • 15
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM (2004) The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15:1254-1261.
    • (2004) Mol Biol Cell , vol.15 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 16
    • 34547420555 scopus 로고    scopus 로고
    • Demyelination, astrogliosis, and accumulation of ubiquitinated proteins, hallmarks of CNS disease in hsf1-deficient mice
    • Homma S, et al. (2007) Demyelination, astrogliosis, and accumulation of ubiquitinated proteins, hallmarks of CNS disease in hsf1-deficient mice. J Neurosci 27:7974-7986.
    • (2007) J Neurosci , vol.27 , pp. 7974-7986
    • Homma, S.1
  • 17
    • 0036840377 scopus 로고    scopus 로고
    • Heat shock transcription factor 2 is not essential for embryonic development, fertility, or adult cognitive and psychomotor function in mice
    • McMillan DR, et al. (2002) Heat shock transcription factor 2 is not essential for embryonic development, fertility, or adult cognitive and psychomotor function in mice. Mol Cell Biol 22:8005-8014.
    • (2002) Mol Cell Biol , vol.22 , pp. 8005-8014
    • McMillan, D.R.1
  • 18
    • 0038320258 scopus 로고    scopus 로고
    • Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis
    • Wang G, Zhang J, Moskophidis D, Mivechi NF (2003) Targeted disruption of the heat shock transcription factor (hsf)-2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis. Genesis 36:48-61.
    • (2003) Genesis , vol.36 , pp. 48-61
    • Wang, G.1    Zhang, J.2    Moskophidis, D.3    Mivechi, N.F.4
  • 19
    • 1542327630 scopus 로고    scopus 로고
    • Essential requirement for both hsf1 and hsf2 transcriptional activity in spermatogenesis and male fertility
    • Wang G, et al. (2004) Essential requirement for both hsf1 and hsf2 transcriptional activity in spermatogenesis and male fertility. Genesis 38:66-80.
    • (2004) Genesis , vol.38 , pp. 66-80
    • Wang, G.1
  • 20
    • 9144260619 scopus 로고    scopus 로고
    • HSF4 is required for normal cell growth and differentiation during mouse lens development
    • Fujimoto M, et al. (2004) HSF4 is required for normal cell growth and differentiation during mouse lens development. EMBO J 23:4297-4306.
    • (2004) EMBO J , vol.23 , pp. 4297-4306
    • Fujimoto, M.1
  • 21
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • Xiao X, et al. (1999) HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 18:5943-5952.
    • (1999) EMBO J , vol.18 , pp. 5943-5952
    • Xiao, X.1
  • 22
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai C, Whitesell L, Rogers AB, Lindquist S (2007) Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell 130:1005-1018.
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 23
    • 0032485258 scopus 로고    scopus 로고
    • Chaperoning brain diseases
    • Welch WJ, Gambetti P (1998) Chaperoning brain diseases. Nature 392:23-24.
    • (1998) Nature , vol.392 , pp. 23-24
    • Welch, W.J.1    Gambetti, P.2
  • 24
    • 28044469532 scopus 로고    scopus 로고
    • Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease
    • Katsuno M, et al. (2005) Pharmacological induction of heat-shock proteins alleviates polyglutamine-mediated motor neuron disease. Proc Natl Acad Sci USA 102:16801-16806.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16801-16806
    • Katsuno, M.1
  • 25
    • 27144503120 scopus 로고    scopus 로고
    • 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
    • Waza M, et al. (2005) 17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration. Nat Med 11:1088-1095.
    • (2005) Nat Med , vol.11 , pp. 1088-1095
    • Waza, M.1
  • 26
    • 1942486792 scopus 로고    scopus 로고
    • Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice
    • Kieran D, et al. (2004) Treatment with arimoclomol, a coinducer of heat shock proteins, delays disease progression in ALS mice. Nat Med 10:402-405.
    • (2004) Nat Med , vol.10 , pp. 402-405
    • Kieran, D.1
  • 27
    • 0035173598 scopus 로고    scopus 로고
    • Prominent stress response of Purkinje cells in Creutzfeldt-Jakob disease
    • Kovacs GG, et al. (2001) Prominent stress response of Purkinje cells in Creutzfeldt-Jakob disease. Neurobiol Dis 8:881-889.
    • (2001) Neurobiol Dis , vol.8 , pp. 881-889
    • Kovacs, G.G.1
  • 28
    • 0028288494 scopus 로고
    • Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain
    • Kenward N, Hope J, Landon M, Mayer RJ (1994) Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie-infected mouse brain. J Neurochem 62:1870-1877.
    • (1994) J Neurochem , vol.62 , pp. 1870-1877
    • Kenward, N.1    Hope, J.2    Landon, M.3    Mayer, R.J.4
  • 29
    • 0034689184 scopus 로고    scopus 로고
    • Heat shock modulates prion protein expression in human NT-2 cells
    • Shyu WC, Kao MC, Chou WY, Hsu YD, Soong BW (2000) Heat shock modulates prion protein expression in human NT-2 cells. Neuroreport 11:771-774.
    • (2000) Neuroreport , vol.11 , pp. 771-774
    • Shyu, W.C.1    Kao, M.C.2    Chou, W.Y.3    Hsu, Y.D.4    Soong, B.W.5
  • 30
    • 2942525558 scopus 로고    scopus 로고
    • Enlarged ventricles, astrogliosis and neurodegeneration in heat shock factor 1 null mouse brain
    • Santos SD, Saraiva MJ (2004) Enlarged ventricles, astrogliosis and neurodegeneration in heat shock factor 1 null mouse brain. Neuroscience 126:657-663.
    • (2004) Neuroscience , vol.126 , pp. 657-663
    • Santos, S.D.1    Saraiva, M.J.2
  • 31
    • 28844469898 scopus 로고    scopus 로고
    • Increase in activity during calorie restriction requires Sirt1
    • Chen D, Steele AD, Lindquist S, Guarente L (2005) Increase in activity during calorie restriction requires Sirt1. Science 310:1641.
    • (2005) Science , vol.310 , pp. 1641
    • Chen, D.1    Steele, A.D.2    Lindquist, S.3    Guarente, L.4
  • 32
    • 70449177837 scopus 로고
    • A note on a simple apparatus for detecting neurological deficit in rats and mice
    • Dunham NW, Miya TS (1957) A note on a simple apparatus for detecting neurological deficit in rats and mice. J Am Pharm Assoc Am Pharm Assoc 46:208-209.
    • (1957) J Am Pharm Assoc Am Pharm Assoc , vol.46 , pp. 208-209
    • Dunham, N.W.1    Miya, T.S.2
  • 33
    • 33846917641 scopus 로고    scopus 로고
    • The power of automated high-resolution behavior analysis revealed by its application to mouse models of Huntington's and prion diseases
    • Steele AD, Jackson WS, King OD, Lindquist S (2007) The power of automated high-resolution behavior analysis revealed by its application to mouse models of Huntington's and prion diseases. Proc Natl Acad Sci USA 104:1983-1988.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1983-1988
    • Steele, A.D.1    Jackson, W.S.2    King, O.D.3    Lindquist, S.4
  • 34
    • 36348958583 scopus 로고    scopus 로고
    • Diminishing apoptosis by deletion of Bax or overexpression of Bcl-2 does not protect against infectious prion toxicity in vivo
    • Steele AD, et al. (2007) Diminishing apoptosis by deletion of Bax or overexpression of Bcl-2 does not protect against infectious prion toxicity in vivo. J Neurosci 27:13022-13027.
    • (2007) J Neurosci , vol.27 , pp. 13022-13027
    • Steele, A.D.1
  • 35
    • 34248396416 scopus 로고    scopus 로고
    • Accumulation of prion protein in the brain that is not associated with transmissible disease
    • Piccardo P, Manson JC, King D, Ghetti B, Barron RM (2007) Accumulation of prion protein in the brain that is not associated with transmissible disease. Proc Natl Acad Sci USA 104:4712-4717.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4712-4717
    • Piccardo, P.1    Manson, J.C.2    King, D.3    Ghetti, B.4    Barron, R.M.5
  • 36
    • 0344030333 scopus 로고    scopus 로고
    • Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein
    • Lasmezas CI, et al. (1997) Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 275:402-405.
    • (1997) Science , vol.275 , pp. 402-405
    • Lasmezas, C.I.1
  • 37
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed LJ, Muench H (1938) A simple method of estimating fifty percent endpoints. The American Journal of Hygiene 27:493-497.
    • (1938) The American Journal of Hygiene , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 38
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer M, et al. (1996) Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 15:1255-1264.
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1
  • 39
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma J, Wollmann R, Lindquist S (2002) Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 40
    • 0037799236 scopus 로고    scopus 로고
    • Heat shock factor 1 contains two functional domains that mediate transcriptional repression of the c-fos and c-fms genes
    • Xie Y, Zhong R, Chen C, Calderwood SK (2003) Heat shock factor 1 contains two functional domains that mediate transcriptional repression of the c-fos and c-fms genes. J Biol Chem 278:4687-4698.
    • (2003) J Biol Chem , vol.278 , pp. 4687-4698
    • Xie, Y.1    Zhong, R.2    Chen, C.3    Calderwood, S.K.4
  • 41
    • 33646349241 scopus 로고    scopus 로고
    • HSF1 down-regulates XAF1 through transcriptional regulation
    • Wang J, et al. (2006) HSF1 down-regulates XAF1 through transcriptional regulation. J Biol Chem 281:2451-2459.
    • (2006) J Biol Chem , vol.281 , pp. 2451-2459
    • Wang, J.1
  • 42
    • 85036804830 scopus 로고    scopus 로고
    • Prion pathogenesis is independent of Caspase-12
    • Steele AD, et al. (2007) Prion pathogenesis is independent of Caspase-12. Prion 1:1-5.
    • (2007) Prion , vol.1 , pp. 1-5
    • Steele, A.D.1
  • 43
    • 11844296730 scopus 로고    scopus 로고
    • Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease
    • Chiesa R, et al. (2005) Bax deletion prevents neuronal loss but not neurological symptoms in a transgenic model of inherited prion disease. Proc Natl Acad Sci USA 102:238-243.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 238-243
    • Chiesa, R.1
  • 44
    • 0346736509 scopus 로고    scopus 로고
    • Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae
    • Trotter EW, et al. (2002) Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J Biol Chem 277:44817-44825.
    • (2002) J Biol Chem , vol.277 , pp. 44817-44825
    • Trotter, E.W.1
  • 45
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • Hetz C, et al. (2008) Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc Natl Acad Sci USA 105:757-762.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 757-762
    • Hetz, C.1
  • 46
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • Morley JF, Morimoto RI (2003) Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol Biol Cell 15:657-664.
    • (2003) Mol Biol Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 48
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295:865-868.
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 49
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck PK, Bonini NM (2002) Pharmacological prevention of Parkinson disease in Drosophila. Nat Med 8:1185-1186.
    • (2002) Nat Med , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 50
    • 33846611068 scopus 로고    scopus 로고
    • The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes
    • Tagawa K, et al. (2007) The induction levels of heat shock protein 70 differentiate the vulnerabilities to mutant huntingtin among neuronal subtypes. J Neurosci 27:868-880.
    • (2007) J Neurosci , vol.27 , pp. 868-880
    • Tagawa, K.1
  • 51
    • 0028958208 scopus 로고
    • Scrapie prions selectively modify the stress response in neuroblastoma cells
    • Tatzelt J, et al. (1995) Scrapie prions selectively modify the stress response in neuroblastoma cells. Proc Natl Acad Sci USA 92:2944-2948.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2944-2948
    • Tatzelt, J.1
  • 53
    • 38949209515 scopus 로고    scopus 로고
    • Differential display of DNA-binding proteins reveals heat-shock factor 1 as a circadian transcription factor
    • Reinke H, et al. (2008) Differential display of DNA-binding proteins reveals heat-shock factor 1 as a circadian transcription factor. Genes Dev 22:331-345.
    • (2008) Genes Dev , vol.22 , pp. 331-345
    • Reinke, H.1
  • 54
    • 0032571397 scopus 로고    scopus 로고
    • Targeted deletion of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inductible apoptosis
    • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IJ (1998) Targeted deletion of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inductible apoptosis. J Biol Chem 273:7523-7528.
    • (1998) J Biol Chem , vol.273 , pp. 7523-7528
    • McMillan, D.R.1    Xiao, X.2    Shao, L.3    Graves, K.4    Benjamin, I.J.5
  • 55
    • 33644766915 scopus 로고    scopus 로고
    • Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis
    • Steele AD, Emsley JG, Ozdinler PH, Lindquist S, Macklis JD (2006) Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis. Proc Natl Acad Sci USA 103:3416-3421.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 3416-3421
    • Steele, A.D.1    Emsley, J.G.2    Ozdinler, P.H.3    Lindquist, S.4    Macklis, J.D.5


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