621
Views
41
CrossRef citations to date
0
Altmetric
Original Article

Regulation of heat shock gene transcription in neuronal cells

&
Pages 433-444 | Received 10 Oct 2004, Accepted 25 Apr 2005, Published online: 09 Jul 2009

References

  • Lindquist S, Craig EA. The heat shock proteins. Annual Reviews in Genetics 1988;22:631–637.
  • Georgopolis C, Welch WJ. Role of the major heat shock proteins as molecular chaperones. Annual Reviews in Cell Biology 1993;9:601–634.
  • Beere H1\4. 'The stress of dying': The role of heat shock proteins in the regulation of apoptosis. Journal of Cell Science 2004;117: 2641–2651.
  • Hsu AL, Murphy CT, Kenyon C. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science 2003;300: 1142–1145.
  • Verbeke P, Fonager J, Clark BF, Rattan SI. Heat shock response and ageing: Mechanisms and applications. Cellular Biology International 2001;25:845–857.
  • Bonelli MA, Alfieri RR, Poli M, Petronini PG, Borghetti AF. Heat-induced proteasomic degradation of HSF1 in serum-starved human fibroblasts aging in vitro. Experimental Cell Research 2001;267: 165–172.
  • Gutsmann-Conrad A, Heydari AR, You S, Richardson A. The expression of heat shock protein 70 decreases with cellular senescence in vitro and in cells derived from young and old human subjects. Experimental Cell Research 1998;241: 404–413.
  • Lee YK, Manalo D, Liu AY. Heat shock response, heat shock transcription factor and cell aging. Biological Signals 1996;5:180–191.
  • Liu AY, Lee YK, Manalo D, Huang LE. Attenuated heat shock transcriptional response in aging: Molecular mechanism and implication in the biology of aging. Exs 1996;77:393–408.
  • Ciocca DR, Clark GM, Tandon AK, Fuqua SA, Welch WJ, McGuire WL. Heat shock protein hsp70 in patients with axillary lymph node-negative breast cancer: Prognostic implications. Journal of the National Cancer Institute 1993;85:570–574.
  • Ciocca DR, Vargas-Roig LM. Hsp27 as a prognostic and predictive factor in cancer. Progress in Molecular Subcellular Biology 2002;28:205–218.
  • Cornford PA, Dodson AR, Parsons KF, Desmond AD, Woolfenden A, Fordham M, et al. Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Research 2000;60:7099–7105.
  • Sarto C, Binz PA, Mocarelli P. Heat shock proteins in human cancer. Electrophoresis 2000;21:1218–1226.
  • Nylandsted J, Rohde M, Brand K, Bastholm L, Elling F, Jaattela M. Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bc1-2. Proceedings of the National Academy of Sciences (USA) 2000;97:7871–7876.
  • Gabai VL,, Meriin AB, Yaglom JA, Volloch VZ, Sherman MY. Role of Hsp70 in regulation of stress-kinase JNK: Implications in apoptosis and aging. FEBS Letters 1998;438:1–4.
  • Nollen EA, Morimoto RI. Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins. Journal of Cellular Science 2002;115:2809–2816.
  • Kalwy SA, Akbar MT, Coffin RS, de Belleroche J, Latchman DS. Heat shock protein 27 delivered via a herpes simplex virus vector can protect neurons of the hippocampus against kainic-acid-induced cell loss. Brain Research & Molecular Brain Research 2003;111: 91–103.
  • Hashimoto K, Tomitaka S, Narita N, Minabe Y, Iyo M, Fukui S. Induction of heat shock protein (HSP)-70 in posterior cingulate and retrosplenial cortex of rat brain by dizocilpine and phencyclidine: Lack of protective effects of sigma receptor ligands. Addiction Biology 1996;1:61–70.
  • Krueger AM, Armstrong JN, Plumier J, Robertson HA, Currie RW. Cell specific expression of Hsp70 in neurons and glia of the rat hippocampus after hyperthermia and kainic acid-induced seizure activity. Brain Research & Molecular Brain Research 1999;71: 265–278.
  • Vidair CA, Doxsey SJ, Dewey WC. Thermotolerant cells possess an enhanced capacity to repair heat-induced alterations to centrosome structure and function. Journal of Cellular Physiology 1995;163:194–203.
  • Batulan Z, Shinder GA, Minotti S, He BP, Doroudchi MM, Nalbantoglu J, et al. High threshold for induction of the stress response in motor neurons is associated with failure to activate HSF1. Journal of Neuroscience 2003;23:5789–5798.
  • Guzhova I, Kislyakova K, Moskaliova 0, Fridlanskaya I, Tytell M, Cheetham M, et al. In vitro studies show that Hsp70 can be released by glia and that exogenous Hsp70 can enhance neuronal stress tolerance. Brain Research 2001;914: 66–73.
  • Bechtold DA, Rush SJ, Brown IR. Localization of the heat-shock protein Hsp70 to the synapse following hyperthermic stress in the brain. Journal of Neurochemistry 2000;74: 641–646.
  • Ty-tell M, Greenberg SG, Lasek RJ. Heat shock-like protein is transferred from glia to axon. Brain Research 1986;363:161–164.
  • Asea A, Calderwood S. Regulation of signal transduction by intracellular and extracellular hsp70. Oxford: Oxford University Press; 2005.
  • Calderwood SK. Chaperones and slow death-a recipe for tumor immunotherapy. Trends in Biotechnology 2005;23:57–59.
  • Helfand SL. Neurobiology. Chaperones take flight. Science 2002;295:809–810.
  • Cowan KJ, Diamond MI, Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Human Molecular Genetics 2003;12:1377–1391.
  • Berke SJ, Paulson HL. Protein aggregation and the ubiquitin proteasome pathway: Gaining the UPPer hand on neurodegeneration. Current Opinions in Genetic Development 2003;13:253–261.
  • Harrison PJ, Procter AW, Exworthy T, Roberts GW, Najlerahim A, Barton AJ, et al. Heat shock protein (hsx70) mRNA expression in human brain: Effects of neurodegenerative disease and agonal state. Neuropathology & Applied Neurobiology 1993;19:10–21.
  • Muchowski PJ, Schaffar G, Sittler A, Wanker EE, Hayer-Hartl MK, Hard FU. Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proceedings of the National Academy of Sciences (USA) 2000;97: 7841–7846.
  • Zatloukal K, Stumptner C, Fuchsbichler A, Heid H, Schnoelzer M, Kenner L, et al. p62 is a common component of cytoplasmic inclusions in protein aggregation diseases. American Journal of Pathology 2002;160:255–263.
  • Garigan D, Hsu AL, Fraser AG, Kamath RS, Ahringer J, Kenyon C. Genetic analysis of tissue aging in Caenorhabditis elegans: A role for heat-shock factor and bacterial proliferation. Genetics 2002;161:1101–1112.
  • Kurapati R, Passananti HB, Rose MR, Tower J. Increased hsp22 RNA levels in Drosophila lines genetically selected for increased longevity. Journal of Gerontology A, Biological Science & Medical Science 2000;55:B552–B559.
  • Tatar M, Khazaeli AA, Curtsinger J NV. Chaperoning extended life. Nature 1997;390:30.
  • Morrow G, Battistini S, Zhang P, Tanguay RM. Decreased lifespan in absence of expression of the mitochon-drial small heat shock protein Hsp22 in Drosophila. Journal of Biological Chemistry 2004;279:43382–43385.
  • Morrow G, Samson M, Michaud S, Tanguay RM. Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress. Faseb Journal 2004;18:598–599.
  • Wyttenbach A, Sauvageot 0, Carmichael J, Diaz-Latoud C, Arrigo AP, Rubinsztein DC. Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Human Molecular Genetics 2002;11: 1137–1151.
  • Benndorf R, Welsh MJ. Shocking degeneration. Natural Genetics 2004;36:547–548.
  • Voellmy R. Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein expression in higher eukaryotes. Critical Reviews in Eukaryotic Gene Expression 1994;4:357–401.
  • Wu C. Heat shock transcription factors: Structure and regulation. Annual Reviews in Cellular Development Biology 1995;11:441–469.
  • Kampinga HH, Brunsting JF, Stege GJ, Burgman PW, Konings AW. Thermal protein denaturation and protein aggregation in cells made thermotolerant by various chemicals: Role of heat shock proteins. Experimental Cell Research 1995;219:536–546.
  • Kampinga HH. Hyperthermia, thermotolerance and topoisomerase II inhibitors. British Journal of Cancer 1995;72:333–338.
  • Ananthan J, Goldberg AL, Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science 1986;232:522–524.
  • McMillan DR, Xiao X, Shao L, Graves K, Benjamin IJ. Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis. Journal of Biological Chemistry 1998;273: 7523–7528.
  • Heydari AR, You S, Takahashi R, Gutsmann-Conrad A, Sarge KD, Richardson A. Age-related changes in activation of heat shock transcription factor 1 in rat hepatocytes. Experimental Cell Research 2000;256: 83–93.
  • He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, et al. Elevated expression of heat shock factor 2a stimulates HSF1-induced transcription during stress. Journal of Biological Chemistry 2003;278:35465–35475.
  • Nakai A, Tanabe M, Kawazoe Y, Inazawa J, Morimoto RI, Nagata K. HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator. Molecular & Cellular Biology 1997;17:469–481.
  • Brown IR, Rush SJ. Cellular localization of the heat shock transcription factors HSF1 and HSF2 in the rat brain during postnatal development and following hyperthermia. Brain Research 1999;821:333–340.
  • Marcuccilli CJ, Mathur SK, Morimoto RI, Miller RJ. Regulatory differences in the stress response of hippocampal neurons and glial cells after heat shock. Journal of Neuroscience 1996;16:478–485.
  • Kaarniranta K, Oksala N, Karjalainen HM, Suuronen T, Sistonen L, Helminen HJ, et al. Neuronal cells show regulatory differences in the hsp70 gene response. Brain Research & Molecular Brain Research 2002;101:136–140.
  • Zuo J, Rungger D, Voellmy R. Activation of the DNA-binding form of human heat shock factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Molecular Cell Biology 1995;15: 4319–4330.
  • Nunes SL, Calderwood SK. Heat shock factor 1 and the heat shock cognate 70 protein associate in high molecular weight complexes in the cytoplasm of NIH-3T3 cells. Biochemistry & Biophysics Research Communications 1995;213:1–6.
  • Knauf U, Newton EM, Kyriakis J, Kingston RE. Repression of heat shock factor 1 activity at control temperature by phosphorylation. Genes Development 1996;10:2782–2793.
  • Price BD, Calderwood SK. Calcium is essential for multistep activation of the heat shock factor in permeabilized cells. Molecular Cell Biology 1991;11:3365–3368.
  • Hensold JO, Hunt CR, Calderwood SK, Houseman DE, Kingston RE. DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells. Molecular Cell Biology 1990;10:1600–1608.
  • Westwood T, Wu C. Activation of drosophila heat shock factor: Conformational changes associated with monomer-to-trimer transition. Molecular Cell Biology 1993;13:3481–3486.
  • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998;94: 471–480.
  • Rabindran SK, Haroun RI, Clos J, Wisniewski J, Wu C. Regulation of heat shock factor timer formation: Role of a conserved leucine zipper. Science 1993;259:230–234.
  • Baler R, Dahl G, Voellmy R. Activation of human heat shock transcription is accompanied by oligomerization, modification and rapid translocation of heat shock transcription facor HSF-1. Molecular Cell Biology 1993;13: 2486–2496.
  • Sarge KD, Murphy SP, Morimoto RI. 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. Molecular Cell Biology 1993;13: 1392–1407.
  • Guo Y, Guettouche T, Fenna M, Boellmann F, Pratt WB, Toft DO, et al. Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. Journal of Biological Chemistry 2001;276:45791–45799.
  • Wang X, Grammatikakis N, Siganou A, Stevenson MA, Calderwood SK. Interactions between extracellular signal regulated protein kinase 1 (ERK1), 14-3-3 epsilon and heat shock factor 1 during stress. Journal of Biological Chemistry 2004;279: 49460–49469.
  • Wang X, Grammatikakis N, Siganou A, Calderwood SK. Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Molecular Cell Biology 2003;23:6013–6026.
  • He B, Meng YH, Mivechi NH. Glycogen synthase kinase 3b and extracellular signal-regulated protein kinase inactivate heat shock transcription factor 1 by facilitating the disappearance of transcriptionally active granules after heat shock. Molecular Cell Biology 1998;18: 6624–6632.
  • Brunet A, Kanai F, Stehn J, Xu J, Sarbassova D, Frangioni JV, et al. 14-3-3 transits to the nucleus and participates in dynamic nucleocytoplasmic transport. Journal of Cell Biology 2002;156:817–828.
  • Hunt C, Calderwood SK. Characterization and sequence of a mouse H5P70 gene and its expression in mouse cell lines. Gene 1990;87:199–204.
  • Wu C. Activating protein factor binds in vitro to upstream control sequences in heat shock gene chromatin. Nature 1984;311:81–84.
  • Us JT, Wu C. Protein traffic on the heat shock promoter: Parking, stalling, and trucking along. Cell 1993;74:1–4.
  • Rasmussen EB, Us JT. In vivo transcriptional pausing and cap formation on three Drosophila heat shock genes. Proceedings of the National Academy of Sciences (USA) 1993;90:7923–7927.
  • Brown SA, Kingston RE. Disruption of downstream chromatin by a transcriptional activator. Genes Development 1997;11:3116–3121.
  • Fivaz J, Bassi MC, Pinaud S, Mirkovitch J. RNA polymerase II promoter-proximal pausing upregulates c-fos gene expression. Gene 2000;255:185–194.
  • Schneider EE, Albert T, Wolf DA, Eick D. Regulation of c-Myc and immunoglobulin kappa gene transcription by promoter proximal pausing of RNA polymerase II. Current Topics in Microbiology & Immunology 1999;246:225–231.
  • Dahmus ME. The role of multisite phosphorylation in the regulation of RNA polymerase II activity. Progress in Nucleic Acids Research and Molecular Biology 1994;48:143–179.
  • Kobor MS, Greenblatt J. Regulation of transcriptional elongation by phosphorylation. Biochimica et Biophysica Acta 2002;1577:261–275.
  • Schwartz BE, Werner JK, Lis JT. Indirect immunofluorescent labeling of Drosophila polytene chromosomes: Visualizing protein interactions with chromatin in vivo. Methods in Enzymology 2004;376:393–404.
  • Lis JT, Mason P, Peng J, Price DH, Werner J. p-TEFb kinase recruitement and function at heat shock loci. Genes Development 2000;14:792–803.
  • Anders MN, Lemon BD, Tijian R. Transcriptional coactivator complexes. Annual Reviews in Biochemistry 2001;70:475–501.
  • Park JM, Werner J, Kim JM, Lis JT, Kim YJ. Mediator, not holoenzyme, is directly recruited to the heat shock promoter by HSF upon heat shock. Molecular Cell 2001;8:9–19.
  • Guidi BW, Bjornsdottir G, Hopkins DC, Lacomis L, Erdjument-Bromage H, Tempst P, et al. Mutual targeting of mediator and the TFIIH kinase Kin28. Journal of Biological Chemistry 2004;279: 29114–29120.
  • Nowak SJ, Corces VG. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Development 2000;14:3003–3013.
  • Smith ST, Petruk S, Sedkov Y, Cho E, Tillib S, Canaani E, et al. Modulation of heat shock gene expression by the TAC1 chromatin-modifying complex. Natural Cell Biology 2004;6:162–167.
  • Sullivan EK, Weirich CS, Guyon JR, Sif S, Kingston RE. Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF. Molecular Cell Biology 2001;21: 5826–5837.
  • Corey LL, Weirich CS, Benjamin IJ, Kingston RE. Localized recruitment of a chromatin-remodeling activity by an activator in vivo drives transcriptional elongation. Genes Development 2003;17:1392–1401.
  • Thomson S, Hollis A, Hazzalin CA, Mahadevan LC. Distinct stimulus-specific histone modifications at hsp70 chromatin targeted by the transcription factor heat shock factor-1. Molecular Cell 2004;15:585–594.
  • Xia W, Voellmy R. Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active timers. Journal of Biological Chemistry 1997;272:4094–4102.
  • Choi HS, Li B, Lin Z, Huang E, Liu AYC. cAMP and cAMP-dependent protein kinase regulate the human heat shock protein 70 gene promoter activity. Journal of Biological Chemistry 1991;266: 11858–11865.
  • Holmberg CI, Leppa S, Eriksson JE, Sistonen L. The phorbol ester 12-0-Tetradecanoylphorbol 13-acetate enhances the heat-induced stress response. Journal of Biological Chemistry 1997;272:6792–6798.
  • Chu B, Zhong R, Soncin F, Stevenson MA, Calderwood SK. Transcriptional activity of heat shock factor 1 at 37°C is repressed through phosphorylation on two distinct serine residues by glycogen synthase kinase 3 and protein kinase C a and C Journal of Biological Chemistry 1998;273: 18640–18646.
  • Bijur GN, Jope RS. Opposing actions of phosphatidylinositol 3-kinase and glycogen synthase kinase-3beta in the regulation of HSF-1 activity. Journal of Neurochemistry 2000;75:2401–2408.
  • Chu B, Soncin F, Price BD, Stevenson MA, Calderwood SK. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. Journal of Biological Chemistry 1996;271: 30847–30857.
  • Kline MP, Morimoto RI. Repression of the heat shock factor 1 transcriptional activation domain is modulated by constitutive phosphorylation. Molecular Cell Biology 1997;17:2107–2115.
  • Holmberg CI, Hietakangas V, Mikhailov A, Rantanen JO, Kallio M, Meinander A, Hellman J, et al. Phosphorylation of serine 230 promotes inducible transcriptional activity of heat shock factor 1. EMBO Journal 2001;20:3800–3810.
  • Soncin F, Asea A, Zhang X, Stevenson MA, Calderwood SK. Role of calcium activated kinases and phosphatases in heat shock factor-1 activation [in process citation]. International Journal of Molecular Medicine 2000;6: 705–710.
  • Park J, Liu AY. Pervanadate induces the hyperphosphorylation but not the activation of heat shock factor 1. Journal of Cellular Physiology 2000;185:348–357.
  • Shamovsky I, Gershon D. Novel regulatory factors of HSF-1 activation: Facts and perspectives regarding their involvement in the age-associated attenuation of the heat shock response. Mechanics of Ageing Development 2004;125:767–775.
  • Walker GA, Thompson FJ, Brawley A, Scanlon T, Devaney E. Heat shock factor functions at the convergence of the stress response and developmental pathways in Caenorhabditis elegans. Faseb Journal 2003;17:1960–1962.
  • Bhat RV, Budd Haeberlein SL, Avila J. Glycogen synthase kinase 3: A drug target for CNS therapies. Journal of Neurochemistry 2004;89:1313–1317.
  • Van Everbroeck BR, Boons J, Cras P. 14-3-3 {gamma} -isoform detection distinguishes sporadic Creutzfeldt-Jakob disease from other dementias. Journal of Neurology, Neurosurgery & Psychiatry 2005;76: 100–102.
  • Dai Q, Zhang C, Wu Y, McDonough H, Whaley RA, Godfrey V, et al. CHIP activates HSF1 and confers protection against apoptosis and cellular stress. Embo Journal 2003;22:5446–5458.
  • Zhang C, Xu Z, He XR, Michael LH, Patterson C. CHIP, a co-chaperone/ubiquitin ligase that regulates protein quality control, is required for maximal cardioprotection after myocardial infarction in mice. American Journal of Physiology & Heart Circulation Physiology 2005;288:H2836–H2842.
  • Takahashi R, Imai Y. Pael receptor, endoplasmic reticulum stress, and Parkinson's disease. Journal of Neurology 2003;250(Suppl 3) :11125–11129.
  • Jana NR, Dikshit P, Goswami A, Kotliarova S, Murata S, Tanaka K, et al. Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes. Journal of Biological Chemistry 2005;280:11635–11640.
  • Stephanou A, Latchman DS. Transcriptional regulation of the heat shock protein genes by STAT family transcription factors. Gene Expression 1999;7:311–319.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.