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Emerging Therapeutic Targets Volume 5, 2001 - Issue 2
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Review

Heat shock proteins: new keys to the development of cytoprotective therapies

Michael Tytell Department of Neurobiology and Anatomy, Wake Forest University School of Medicine, Winston-Salem, NC 27157, USA
&
Philip L Hooper University of Colorado Health Sciences, Department of Endocrinology, Denver, Colorado, USA
Pages 267-287 | Published online: 25 Feb 2005

Bibliography

  • RITOSSA FM: A new puffing system induced by temperature shock and DNP in Drosophila. Experientia (1962) 18:571–573.
  • •The publication credited with the first report of heat shock proteins.
  • WELCH WJ, GARRELS GP, THOMAS GP et al.: Biochemical charaterization of the mammalian stress proteins and identification of two stress proteins as glucose and Ca+2 ionophore regulated proteins. j Biol. Chem. (1983) 258:7102–7111.
  • KELLEY PM, SCHLESINGER MJ: The effect of amino acid analogues and heat shock on gene expression in chicken embryo fibroblasts. Cell (1978) 15:1277–1286.
  • •The first report of heat shock proteins in mammalian cells.
  • KELLEY PM, ALIPERTI G, SCHLESINGER MJ: In vitro synthesis of heat-shock proteins by mRNAs from chicken embryo fibroblasts. J. Biol. Chem. (1980) 255:3230–3233.
  • KELLEY PM, SCHLESINGER MJ: Antibodies to two majorchicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol. Cell Biol. (1982) 2:267–274.
  • •One of the first illustrations of the phylogenetic conservation of Hsp70.
  • ADAMS C, RINNE RW: Stress protein formation: gene expression and environmental interaction with evolutionary significance. Int. Rev. CytoL (1982) 79:305–315.
  • CRAIG EA, GROSS CA: Is Hsp7 0 the cellular thermometer? Trends Biochem. (1991) 16:135–140.
  • ••An intriguing hypothesis on the functional significance ofthe Hsp70 response.
  • FEDER ME, HOFMANN GE: Heat-shock proteins, molecular chaperones and the stress response: evolutionary and ecological physiology. Ann. Rev. Physiol. (1999) 61:243–282.
  • ••Good, recent review of the stress response in diverseorganisms and its functional significance.
  • NICOLET CM, CRAIG EA: Functional analysis of a conserved amino-terminal region of Hsp70 by site-directed mutagenesis. Yeast (1991) 7:699–716.
  • •Analysis of structure/function relationships of Hsp70 in yeast.
  • HIGHTOWER LE, LI T: Structure and function of the mammalian Hsp70 family. In: Heat Shock Proteins in the Nervous System. Mayer J & Brown I (Eds.), Academic Press, London. (1994):1–30.
  • LI T, HIGHTOWER LE: Effects of dexamethasone, heat shock and serum responses on the inhibition of Hsc70 synthesis by antisense RNA in NIH 313 cells. J Physiol. (1995) 164:344–355.
  • KIANG JG, TSOKOS GC: Heat shock protein 70 kDa: molecular biology, biochemistry and physiology. Pharmacol. Ther. (1998) 80:183–201.
  • ••Excellent review of the Hsp70 regulation and function.
  • LATCHMAN DS: Stress Proteins. Springer Berlin (1998) :1–422.
  • ••Excellent current review of the major Hsps, their functionsand their roles in several diseases.
  • AGASHE VR, HARTL FU: Roles of molecular chaperones in cytoplasmic protein folding. Semin. Cell Dev. (2000) 11:15–25.
  • •Current review of function.
  • FELDMAN DE, FRYDMAN J: Protein folding in viva the importance of molecular chaperones. CUIT. Opin. Struc. Biol. (2000) 10:26–33.
  • •Current review of function.
  • BROWN CR, MARTIN RL, HANSEN WJ et al.: The constitu- tive and stress inducible forms of Hsp70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J. Cell Biol. (1993) 120:1101–1112.
  • ••One of the few reports to directly compare Hsc70 and Hsp70with regard to function.
  • DEAN DO, KENT CR, TYTELL M: Constitutive and inducible heat shock protein 70 immunoreactivity in the normal rat eye. Invest. Ophthalmol. Vis. Sci. (1999) 40:2952–2962.
  • •Shows that unstressed retina contains a unique distribution of Hsp70.
  • WELCH WJ: Mammalian stress response: cell physiology, structure/function of stress proteins and implications for medicine and disease. Physiol. Rev. (1992) 72:1063–1081.
  • MALLOUK Y, VAYSSIER-TAUSSAT M, BONVENTRE JV etal.: Heat shock protein 70 and ATP as partners in cell homeostasis (Review). Int. J. Mol. Med. (1999) 4:463–474.
  • MAYER MP, SCHRODER H, RUDIGER S et al.: Multistepmechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. (2000) 7:586–593.
  • MORISHIMA Y, MURPHY PJ, LI DP et al.: Stepwiseassembly of a glucocorticoid receptor.Hsp90 hetero-complex resolves two sequential ATP-dependent events involving first Hsp70 and then Hsp90 in opening of the steroid binding pocket. J. Biol. Chem. (2000) 275:18054–18060.
  • UNGEWICKELL E: The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles. EMBO J (1985) 4:3385–3391.
  • ••Key, initial observation linking Hsp70 to a basic cellularfunction
  • OSTERMANN J, VOOS W, KANG PJ et al.: Precursorproteins in transit through mitochondrial contact sites interact with Hsp70 in the matrix. FEBS Lett. (1990) 277:281–284.
  • UNGERMANN C, NEUPERT W, CYR DM: The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science (1994) 266:1250–1253.
  • ••Description of the key role of Hsp70 in protein translocationinto mictochondria.
  • AGARRABERES FA, TERLECKY SR, DICE JF: An intralyso- somal Hsp70 is required for a selective pathway of lysosomal protein degradation. J. Cell Biol. (1997) 137:825–834.
  • ••Extends the protein translocation function of Hsp70 toanother organelle, the lysosome.
  • MORIMOTO R, SANTORO MG: Stress-inducibleresponse and heat shock proteins: New pharma-cologic targets for cytoprotection. Nature Biotech. (1998) 16:833–838.
  • MORIMOTO RI: Cells in stress: transcriptional activa-tion of heat shock genes. Science (1993) 259:1409–1410.
  • •Mechanism of regulation of Hsp70 gene expression.
  • ABRAVAYA K, MYERS MP, MURPHY SP et al.: The human heat shock protein Hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. (1992) 6:1153–1164.
  • •Another important study of Hsp70 gene expression.
  • STEPHANOU A, ISENBERG DA, NAKAJIMA K et al.: Signaltransducer and activator of transcription-1 and heat shock factor-1 interact and activate the transcription of Hsp-70 and Hsp-90b gene promoters./ Biol. Chem. (1999) 274:1723–1728.
  • SORGER PK, PELHAM HR: Cloning and expression of agene encoding Hsc73, the major Hsp70-like protein in unstressed rat cells. EMBO J (1987) 6:993–998.
  • RIABOWOL KT, MIZZEN LA, WELCH WJ: Heat shock is lethal to fibroblasts microinjected with antibodies against Hsp70. Science (1988) 242:433–436.
  • ••First observation that showed directly that Hsp70 is essentialfor heat stress tolerance.
  • CAMPANINI C, PETRONINI PG, ALFIERI R et al.: Decreasedexpression of heat shock protein mRNAand protein in WI-38 human fibroblasts aging in vitro. Ann. NY Acad. Sci. (1992) 663:442–443.
  • HOLBROOK NJ, UDELSMAN R: Heat shock protein geneexpression in response to physiologic stress and aging. In: The Biology of Heat Shock Proteins and Molecular Chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. (1990577–593
  • LEE YK, MANALO D, LIU AY: Heat shock response, heatshock transcription factor and cell aging. Biol. Signals (1996) 5:180–191.
  • VOLLOCH V, MOSSER DD, MASSIE B et al.: Reduced thermotolerance in aged cells results from a loss of an hsp72-mediated control o fJNK signaling pathway. Cell Stress Chaperones (1998) 3:265–271.
  • •Links age-related decrement in stress tolerance to the impact of Hsp70 deficit on signal transduction.
  • JÄÄTTELA M, WISSING D, KOKHOLM K et al.: Hsp70 exerts its antiapoptotic function downstream of caspase-3-like proteases. EMBO J. (1998) 17:6124–6134.
  • LASUNSKAIA EB, FRIDLIANSKAIA II, GUZHOVA IV et al.:Accumulation of major stress protein 70kDa protects meyloid and lymphoid cells from death by apoptosis. Apoptosis (1997) 2:156–163.
  • MOSSER DD, CARON AW, BOURGET L et al.: Role of the human heat shock protein Hsp70 in protection against stress-induced apoptosis. Molec. Cell. Biol. (1997) 17:5317–5327.
  • ••This and other papers by this group reveal key informationabout the intersection of the Hsp70 response and apoptosis.
  • VAYSSIER M, POLLA BS: Heat shock proteins chaper- oning life and death. Cell Stress Chaperones (1998) 3:221–227.
  • •Good review of potential interactions of Hsp70 with several signal transduction pathways.
  • MOSSER DD, CARON AW, BOURGET L et al.: The chaperone function of Hsp70 is required for protec-tion against stress-induced apoptosis. Mol. Cell Biol. (2000) 20:7146–7159.
  • •Important details on mechanism of Hsp70-mediated protec-tion and apoptosis.
  • WARRICK JM, CHAN HYE, GRAY-BOARD GL et al.: Suppression of polyglutamine-mediated neurodegen-eration in Drosophila by the molecular chaperone Hsp70. Nature Genetics (1999) 23:425–428.
  • ••First report that Hsp70 can suppress mutant protein toxicityin vivo.
  • BERNSTEIN SL, LIU AM, HANSEN BC et al.: Heat shock cognate-70 gene expression declines during normal aging of the primate retina. Invest. Ophthalmol Vis. Sci. (2000) 41:2857–2862.
  • STRICKLAND E, QU BH, MILLEN L et al.: The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator. I Biol. Chem. (1997) 272:25421–25424.
  • BUNN HF: Pathogenesis and treatment of sickle cell disease. N Engl. J. Med. (1997) 337:762–769.
  • PETIT MD, WASSENAAR A, VAN D, V et al.: Depressed responsiveness of peripheral blood mononuclear cells to heat- shock proteins in periodontitis patients. J. Dent. Res. (1999) 78:1393–1400.
  • LUDWIG D, STAHL M, IBRAHIM ET et al.: Enhanced intestinal expression of heat shock protein 70 in patients with inflammatory bowel diseases. Dig. Dis. sci. (1999) 44:1440–1447.
  • ROKUTAN K: Role of heat shock proteins in gastric mucosal protection. J. Gastroenterol. Hepatol. (2000) Suppl. 15:D12–D19.
  • MACHT LM, ELSON CJ, KIRWAN JR et al.: Relationship between disease severity and responses by blood mononuclear cells from patients with rheumatoid arthritis to human heat- shock protein 60. Immunology (2000) 99:208–214.
  • JOHNSON AD, BERBERIAN PA, TYTELL M et al.: Differen-tial distribution of 70-kD heat shock protein in athero-sclerosis - its potential role in arterial SMC survival. Arterioscler. Thromb. Vasc. Biol. (1995) 15:27–36.
  • •One of several reports by this group linking Hsps to Atherosclerosis.
  • KIANG JG, GIST ID, TSOKOS GC: Biochemical require-ments for the expression of heat shock protein 72 kda in human breast cancer MCF-7 cells. Mol. Cell Biochem. (1999) 199:179–188.
  • WRIGHT BH, CORTON JM, EL NAHAS AM et al: Elevatedlevels of circulating heat shock protein 70 (Hsp70) in peripheral and renal vascular disease. Heart Vessels (2000) 15:18–22.
  • TROST SU, OMENS JH, KARLON WJ et al.: Protectionagainst myocardial dysfunction after a brief ischemic period in transgenic mice expressing inducible heat shock protein 70.1 Clin. Invest (1998) 101:855–862.
  • AMICI C, GIORGI C, ROSSI A et al.: Selective inhibition of virus protein synthesis by prostaglandin Al: a transla-tional block associated with Hsp70 synthesis. j Vim/ (1994) 68:6890–6899.
  • ROSSI A, ELIA G, SANTORO MG: 2-Cyclopenten-1 -one, a new inducer of heat shock protein 70 with antiviral activity. j Biol. Chem. (1996) 271:32192–32196.
  • •Demonstrates that an agent that increases Hsps also has antiviral activity.
  • GANDOUR-EDWARDS R, MCCLAREN M, ISSEROFF RR: Irnmunolocalization of low-molecular-weight stress protein Hsp27 in normal skin and common cutaneous lesions. Am. J. Dermatopathol (1994) 16:504–509.
  • VILLAR J, EDELSON JD, POST M et al.: Induction of heatstress proteins is associated with decreased mortality in an animal model of acute lung injury. Am. Rev. Respir. Dis. (1993) 147:177–181.
  • MATTSON MP: Neur °protective signaling and the aging brain: take away my food and let me run. Brain Res. (2000) 886:47–53.
  • ••Intriguing review of the hypothesis that Hsp70 may beinvolved in the increased lifespan seen with caloric restric-tion in animals
  • TATZELT J, VOELLMY R, WELCH WJ: Abnormalities instress proteins in prion diseases. Cell Mot. Neurobiol. (1998) 18:721-729. Possible link between prion diseases and Hsps.
  • YAMAGUCHI K, GAUR VP, TYTELL M et al.: Ocular distri-bution of 70-kDa heat-shock protein in rats with normal and dystrophic retinas. Cell Tissue Res. (1991) 264:497–506.
  • WU T, YUAN Y, WU Y et al.: Presence of antibodies toheat stress proteins in workers exposed to benzene and in patients with benzene poisoning. Cell Stress Chaperones (1998) 3:161–167.
  • •An example of one consequence of the stress response in humans.
  • WU T, CHEN S, WANG C et al.: Presence of antibodies against Hsp71 and its possible significance in patients with acute heat-induced illness. Molecular chaperones and the heat shock response. Cold Spring Harbor Symposium on Molecular Chaperones and the Heat Shock Response (2000) 270.
  • GEHRING WJ, WEHNER R: Heat shock protein synthesis and thermotolerance in Cataglyphis, an ant from the Sahara desert. Proc. NMI Acad. Sci. USA (1995) 92:2994–2998.
  • ••First to suggest that Hsps may be involved in adaptation toextreme environments.
  • ZATSEPINA OG, ULMASOV KA, BERESTEN SF et al.: Thermotolerant desert lizards characteristically differ in terms of heat-shock system regulation. J Exp. Biol. (2000) 203 (Pt 6):1017–1025.
  • •Adaptation to extreme environment and the stress response.
  • CHANG J, KNOWLTON AA, WASSER JS: Expression of heat shock proteins in turtle and mammal hearts: relationship to anoxia tolerance. Am. J Physiol Regul. Integr. Comp Physiol (2000) 278:R209–R214.
  • BITAR MS, FAROOK T, JOHN B et al.: Heat-shock protein 72/73 and impaired wound healing in diabetic and hypercortisolemic states. Surgery (1999) 125:594–601.
  • STROKOV IA, MANUKHINA EB, BAKHTINA LY et al.: The function of endogenous protective systems in patients with insulin- dependent diabetes mellitus and polyneuropathy: effect of antioxidant therapy. Bull. Exp. Biol. Med. (2000) 130:986–990.
  • MCMURTRY AL, CHO K, YOUNG LJ et al.: Expression of Hsp70 in healing wounds of diabetic and nondiabetic mice. J. Surg. Res. (1999) 86:36–41.
  • BROWNLEE M: Negative consequences of glycation.Metabolism (2000) 49 (Suppl. 1)9–13.
  • JNATTELA M: Heat shock proteins as cellular lifeguards. Ann. Med. (1999) 31:261–271.
  • ••Good, recent review on the functional significance of Hspsin cell stress tolerance.
  • (NO AUTHORS LISTED) Major cardiovascular events in hypertensive patients randomized to doxazosin vs. chlorthalidone: the an tihyp ertensive and lipid-lowering treatment to prevent heart attack trial (ALLHAT). ALLHAT Collaborative Research Group. JAMA (2000) 283:1967–1975.
  • •Large study showing an unexpectedly poor outcome with a popular medication.
  • MENG X, BROWN JM, AO L et al. : Norepinephrine induces cardiac heat shock protein 70 and delayed cardioprotection in the rat through a-1 adrenocep-tors. Cardiovasc. Res. (1996) 32:374–383.
  • •Demonstrates modulation of Hsp70 by an a-adrenergic agonist.
  • COHN JN, ARCHIBALD DG, ZIESCHE S et al.: Effect of vasodilator therapy on mortality in chronic conges-tive heart failure. Results of a Veterans Administration Cooperative Study. N Engl. J. Med. (1986) 314:1547–1552.
  • KNOWLTON AA, KAPADIA S, TORRE-AMIONE G et al.: Differential expression of heat shock proteins in normal and failing human hearts. J. Mol. Cell Cardiol. (1998) 30:811–818.
  • •Important study relating heart failure to Hsps.
  • KONSTAM MA, SMITH JJ, PATTEN R et al.: Calcium channel blockers in heart failure: help or hindrance?' Card Fail. (1996) 2:S251–S257.
  • •An edititorial suggesting that calcium channel blockers are not as beneficial as anticipated.
  • LOW-FRIEDRICH I, SCHOEPPE W: Effects of calcium channel blockers on stress protein synthesis in cardiac myocytes. J. Cardiovasc. Pharmacol. (1991) 17:800–806.
  • KNOWLTON AA, SUN L: Heat-shock factor-1, steroidhormones and regulation of heat-shock protein expression in the heart. Am." Physiol Heart Circ. Physiol. (2001) 280:H455–H464.
  • •Good paper on the basic science of Hsps and steroid hormones.
  • SUN L, CHANG J, KIRCHHOFF SR et al.: Activation of HSF and selective increase in heat-shock proteins by acute dexamethasone treatment. Am. J. Physiol Heart Circ. Physiol. (2000) 278 : H1091–H1097.
  • CURRIE RW, KARMAZYN M, KLOC M et al.: Heat shock response is associated with enhanced post-ischemic ventricular recovery. Circ. Res. (1988) 63:543–549.
  • DONNELLY TJ, SIEVERS RE, VISSERN FLJ et al.: Heat shock protein induction in rat hearts: A role for improved myocardial salvage after ischemia and reperfusion. Circulation (1992) 85 :769–778.
  • MESTRIL R, DILLMANN WH: Heat shock and adaptive response to ischemia. Trends Cardiovasc. Med. (1991) 1:240–244.
  • CHOPP M, CHEN H, HO K-L et al.: Transienthyperthermia protects against subsequent forebrain ischemic cell damage in the rat. Neurol (1989) 39:1396–1398.
  • •One of the first studies to show that the stress response can inhibit ischemic injury in vivo.
  • GREEN EJ, DIETRICH WD, VAN DIJK F et al: Protective effects of brain hypothermia on behavior and histopa-thology following global cerebral ischemia in rats. Brain Res. (1992) 580:197–204.
  • KATO H, ARAKI T, KOGURE K: Preserved neurotrans-mitter receptor binding following ischemia in precon-ditioned gerbil brain. Brain Res. Bull. (1992) 29:395–400.
  • MASSA SM, SWANSON RA, SHARP FR: The stress gene response in brain. Cerebrovasc. Brain Metab. Rev. (1996) 8:95–158.
  • ••Comprehensive review of the stress response in the brain.
  • MATSUYAMA K, CHIBA Y, IHAYA A et al.: Effect of spinal cord preconditioning on paraplegia during cross-clamping of the thoracic aorta. Ann. Thorac. Surg. (1997) 63:1315–1320.
  • PERDRIZET GA, SHAPIRO DS, REWINSKI MJ: Surgical stress and the heat shock response: in vivo models of stress conditioning. Ann. N. Y. Acad. Sci. (1999) 874:320–325.
  • ••This group has provided important observations on thepotential of the stress response to improve surgical outcomes.
  • BARBE MF, TYTELL M, GOWER DJ et al.: Hyperthermia protects against light damage in the rat retina. Science (1988) 241:1817–1820.
  • ••The first report linking Hsps to protection of neural tissue invivo.
  • DEMIDOV ON, TYRENKO W, SVISTOV AS et al.: Heat shock proteins in cardiosurgery patients. Eur. J. Cardiothorac. Surg. (1999) 16:444–449.
  • KOENIG WJ, LOHNER RA, PERDRIZET GA et al.: Improving acute skin-flap survival through stress conditioning using heat shock and recovery. Plast. Reconstr. Surg. (1992) 90:659–664.
  • •Important observation.
  • TRAUTINGER F, KNOBLER RM, HONIGSMANN H et al.: Increased expression of the 72-kDa heat shock protein and reduced sunburn cell formation in human skin after local hyperthermia. / Invest Dermatol. (1996) 107:442–443.
  • •Example of the role of Hsps in protection of the skin in humans.
  • GOWDA A, YANG CJ, ASIMAKIS GK et al.: Cardioprotec-tion by local heating: improved myocardial salvage after ischemia and reperfusion. Ann. Thorac. Surg. (1998) 65:1241–1247.
  • PERDRIZET GA, REWINSKI MJ, SCHVVEIZER RT et al.: Heat shock and recovery protects pancreatic islets from warm ischemic injury. Transplant. Proc. (1994) 26:3477–3478.
  • •Important observation on the potential significance of Hsps in organ transplantation.
  • PERDRIZET GA, KANEKO H, BUCKLEY TM et al.: Heat shock and recovery protects renal allografts from warm ischemic injury and enhances Hsp72 produc-tion. Transplant. Proc. (1993) 25:1670-1673. One of the first examples of the potential application of the stress response in organ transplantation.
  • HIRATSUKA M, YANO M, MORA BN et al.: Heat shock pretreatment protects pulmonary isografts from subsequent ischemia-rep erfusioninjury./ Heart Lung Transplant. (1998) 17:1238–1246.
  • FLOHE S, SPEIDEL N, FLACH R et al: Expression of Hsp 70 as a potential prognostic marker for acute rejection in human liver transplantation. Transpl. Int. (1998) 11:89–94.
  • JIANG Q, CROSS AS, SINGH IS et al.: Febrile coretemperature is essential for optimal host defense in bacterial peritonitis. Infect. Immun. (2000) 68:1265–1270.
  • VILLAR J, RIBEIRO SP, MULLEN JB et al: Induction of theheat shock response reduces mortality rate and organ damage in a sepsis-induced acute lung injury model. Grit. Care Med. (1994) 22:914–921.
  • DESHPANDE GG, HEIDEMANN SM, SARNAIK AP: Heat stress is associated with decreased lactic acidemia in rat sepsis. Grit. Care (Lond) (2000) 4:45–49.
  • HOTCHKISS R, NUNNALLY I, LINDQUIST S et al.:Hyperthermia protects mice against the lethal effects of endotoxin. Am. J. Physiol. (1993) 265:R1447–R1457.
  • •An early example of the potential role of the stress response in toxic shock.
  • KLUGER MJ: The adaptive value of fever. In: Fever: Basic Mechanisms and Mangement Mackowiak PA (Ed.), Raven Press, New York. (1990:105–124.
  • •Good review.
  • VAUGHN LK, VEALE WL, COOPER KE: Antipyresis: its effect on mortality rate of bacterially infected rabbits. Brain Res. Bull. (1980) 5:69–73.
  • HOOPER PL: Hot-tub therapy for type 2 diabetes mellitus. N Engl. J. Med. (1999) 341:924–925.
  • ••Important observation suggesting hyperthermia may be ofbenefit to diabetics.
  • SCARIM AL, HEITMEIER MR, CORBETT JA: Heat shock inhibits cytokine-induced nitric oxide synthase expression by rat and human islets. Endocrinol. (1998) 139:5050–5057.
  • BELLOMETTI S, GALZIGNA L: Serum levels of a prosta-glandin and a leukotriene after thermal mud pack therapy. J. Investig. Med. (1998) 46:140–145.
  • TEl C, TANAKA N: Thermal vasodilation as a treatment of congestive heart failure: a novel approach.J Cardiol. (1996) 27:29–30.
  • FEDER JH, ROSSI JM, SOLOMON J et al.: The consequences of expressing Hsp70 in Drosophila cells at normal temperatures. Genes Dev. (1992) 6:1402–1413.
  • JAATTELA M: Escaping cell death: survival proteins in cancer. Exp. Cell Res. (1999) 248:30–43.
  • •Good, recent review of Hsps and cancer cell survival.
  • UNEY JB, KEW JN, STALEY K et al: Tr ansfection-mediated expression of human Hsp70i protects rat dorsal root ganglian neurones and glia from severe heat stress. FEBS Lett. (1993) 334:313–316.
  • •Direct demonstration of the protective function of Hsp70 in neural tissue.
  • NOLLEN EA, BRUNSTING JF, ROELOFSEN H et al: In vivo chaperone activity of heat shock protein 70 and thermotolerance. Mot. Cell Biol. (1999) 19:2069–2079.
  • SIMON MM, REIKERSTORFER A, SCHVVARZ A et al: Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release. J. Clin. Invest (1995) 95:926–933.
  • SUZUKI K, SAWA Y, KANEDA Y et al: Overexpressed heat shock protein 70 attenuates hypoxic injury in coronary endothelial cells. j Mol. Cell Cardiol (1998) 30:1129–1136.
  • XU L, LEE JE, GIFFARD RG: Overexpression of bc1-2, bcl-XL or hsp70 in murine cortical astrocytes reduces injury of co-cultured neurons. Neurosci. Lett. (1999) 277:193–197.
  • •Suggest that glial Hsp70 may protect neurons
  • HUTTER JJ, MESTRIL R, TAM EKW et al: Overexpression of heat shock protein 72 in transgenic mice decreases infarct size in vivo. Circulation (1996) 94:1408–1411.
  • ••This and the next reference are the first two showing overex-pression of Hsp70 in transgenic mice can protect heart and brain from ischaemia.
  • PLUMIER J-CL, KRUEGER AM, CURRIE RW et al.: Transgenic mice expressing the human inducible Hsp70 have hippocampal neurons resistant to ischemic injury. Cell Stress Chaperones (1997) 2:162–167.
  • RAJDEV S, HARA K, KOKUBO Y et al.: Mice overex-pressing rat heat shock protein 70 are protected against cerebral infarction. Ann. Neurol. (2000) 47:782–791.
  • •Further documentation of enhanced ischemic tolerance in Hsp70 overexpressing mice.
  • MESTRIL R, GIORDANO FJ, CONDE AG et al.: Adenovirus-mediated gene transfer of a heat shock protein 70 (Hsp70) protects against simulated ischemia. j Mot. Cell Cardiol. (1996) 28:2351–2358.
  • RADFORD NB, FINA M, BENJAMIN IJ et al.: Cardioprotec-tive effects of 70-kDa heat shock protein in transgenic mice. Proc. Natl. Acad. Sci. USA (1996) 93:2339–2342.
  • SUZUKI K, SAWA Y, KANEDA Y et al.: In vivo gene transfection with heat shock protein 70 enhances myocardial tolerance to ischemia-reperfusion injury in rat. J. Clin. Invest (1997) 99:1645–1650.
  • JAYAKUMAR J, SUZUKI K, KHAN M et al.: Gene therapy for myocardial protection : transfection of donor hearts with heat shock protein 70 gene protects cardiac function against ischemia-reperfusion injury. Circulation (2000) 102:111302–111306.
  • WELCH WJ, SUHAN JP: Cellular and biochemical events in mammalian cells during and after recovery from physiological stress. J. Cell Biol. (1986) 103:2035–2052.
  • ••The first detailed study of the cell biology of Hsp70 incultured cells.
  • MITANI K, FUJITA H, FUKUDA Y et al.: The role of inorganic metals and metalloporphyrins in the induction of haem oxygenase and heat-shock protein 70 in human hepatoma cells. Biochem. J. (1993) 290 ( Pt 3):819–825.
  • BEASLEY TC, TYTELL M, SWEATT AJ: Heat shock protein 70 in the retina of Xenopus laevis, in vivo and in vitro: effect of metabolic stress. Cell Tissue Res. (1997) 290:525–538.
  • BURGMAN PW, KAMPINGA HH, KONINGS AW: Possible role of localized protein denaturation in the mechanism of induction of thermotolerance by heat, sodium-arsenite and ethanol. Int. J. Hyperthermia (1993) 9:151–162.
  • WAGNER M, HERMANNS I, BITTINGER F et al.: Induction of stress proteins in human endothelial cells by heavy metal ions and heat shock. Am. J. Physiol (1999) 277:L1026–L1033.
  • LOWENSTEIN DH, CHAN PH, MILES MF: The stress protein response in cultured neurons: Characteriza-tion and evidence for a protective role in excitotox-icity. Neuron (1991) 7:1053–1060.
  • •One of the first reports indicating that Hsps may protect neurons from excitotoxicity.
  • UNOSHIMA M, NISHIZONO A, TAKITA-SONODA Y et al.: Effects of zinc acetate on splenocytes of endotoxemic mice: Enhanced immune response, reduced apoptosis and increased expression of heat shock protein 70.1 Lab Clin. Med. (2001) 137:28–37.
  • KADOYA C, DOMINO EF, YANG GY et al.: Preischemic but not postischemic zinc protoporphyrin treatment reduces infarct size and edema accumulation after temporary focal cerebral ischemia in rats. Stroke (1995) 26:1035–1038.
  • POWELL SR, HALL D, AIUTO L et al.: Zinc improves postischemic recovery of isolated rat hearts through inhibition of oxidative stress. Am. J. Physiol (1994) 266:H2497–H2507.
  • CORNWALL MW: Zinc iontophoresis to treat ischemic skin ulcers. Phys. Ther. (1981) 61:359–360.
  • PRASAD AS, FITZGERALD JT, BAO B et al.: Duration of symptoms and plasma cytokine levels in patients with the common cold treated with zinc acetate. A random-ized, double-blind, placebo-controlled trial. Ann. Intern. Med. (2000) 133:245–252.
  • MATSUBARA J, SHIDA T, ISHIOKA K et al.: Protective effect of zinc against lethality in irradiated mice. Environ. Res. (1986) 41:558–567.
  • YOSHIKAWA T, NAITO Y, TANIGAWA T et al.: Effect of zinc-carnosine chelate compound (Z-103), a novel antioxidant, on acute gastric mucosal injury induced by ischemia-reperfusion in rats. Free Radic. Res. Commun. (1991) 14:289–296.
  • NOVICK SC, WARRELL RP: Arsenicals in hematologic cancers. Semin. Oncol (2000) 27:495–501.
  • SACERDOTI D, ESCALANTE B, ABRAHAM NG et al: Treatment with tin prevents the development of hypertension in spontaneously hypertensive rats. Science (1989) 243:388–390.
  • LEVERE RD, ESCALANTE B, SCHWARTZMAN ML et al: Role of heme oxygenase in heme-mediated inhibition of rat brain Na+-K+- ATPase: protection by tin-protoporphyrin. Neurochem. Res. (1989) 14:861–864.
  • HAHN GM, SHIU EC, AUGER EA: Mammalian stress proteins Hsp70 and Hsp28 coinduced by nicotine and either ethanol or heat. Mol. Cell Biol. (1991) 11:6034–6040.
  • DE LORIMIER AA: Alcohol, wine and health. Am. J. Surg. (2000) 180:357–361.
  • •Editorial about the benefits of alcohol consumption.
  • RUBIN DT, HANAUER SB: Smoking and inflammatory bowel disease. Eur. J. Gastroenterol. Hepatol. (2000) 12:855–862.
  • BITTOUN R: Recurrent aphthous ulcers and nicotine. Med. J. Aust. (1991) 154:471–472.
  • PARULKAR AA, PENDERGRASS ML, GRANDA-AYALA R et Nonhypoglycemic effects of thiazolidinediones. Ann. Intern. Med. (2001) 1 3 4:61–71.
  • ••Good review of effects of this class of drugs.
  • MURATA T, HE S, HANGAI M et al.: Peroxisome proliferator-activated receptor-gamma ligands inhibit choroidal neovascularization. Invest. Ophthalmol. Vis. Sci. (2000) 41:2309–2317.
  • SARRAF P, MUELLER E, JONES D et al.: Differentiation and reversal of malignant changes in colon cancer through PPARgamma. Nature Med. (1998) 4:1046–1052.
  • GUAN YF, ZHANG YH, BREYER RM et al: Expression of peroxisome proliferator-activated receptor gamma (PPARgamma) in human transitional bladder cancer and its role in inducing cell death. Neoplasia. (1999) 1:330–339.
  • DEMETRI GD, FLETCHER CD, MUELLER E et al.: Induction of solid tumor differentiation by the peroxisome proliferator- activated receptor-gamma ligand trogli-tazone in patients with liposarcoma. Proc. Natl. Acad. Sci. USA (1999) 96:3951–3956.
  • ELLIS CN, VARANI J, FISHER GJ et al.: Troglitazone improves psoriasis and normalizes models of proliferative skin disease: ligands for peroxisome proliferator-activated receptor- gamma inhibit keratinocyte proliferation. Arch. Dermatol (2000) 136:609–616.
  • SU CG, WEN X, BAILEY ST et al.: A novel therapy for colitis utilizing PPAR-gamma ligands to inhibit the epithelial inflammatory response. J Clin. Invest. (1999) 104:383–389.
  • RICOTE M, HUANG J, FAJAS L et al.: Expression of the peroxisome proliferator-activated receptor gamma (PPARgamma) in human atherosclerosis and regulation in macrophages by colony stimulating factors and oxidized low density lipoprotein. Proc. Natl. Acad. Sci. USA (1998) 95:7614–7619.
  • STRAUS DS, PASCUAL G, LI M et al.: 15-deoxy-delta 12,14-prostaglandin J2 inhibits multiple steps in the NF- kappa B signaling pathway. Proc. Natl. Acad. Sci. USA (2000) 97:4844–4849.
  • MAGGI LBJR, SADEGHI H, WEIGAND C et al.: Anti-inflammatory actions of 15-deoxy-D 12'14-prost-aglandin j2 and toglitazone. Evidence for heat shock-dependent and -independent inhibition of cytokine-induced inducible nitric oxide synthase expression. Diabetes (2000) 49:346–355.
  • ••Important observation indicating the involvement of Hsps inthe effects of these agents.
  • NAGAI T, YASUNAMI Y, NAGATA N et al.: Amelioration of hyperglycemia in streptozotocin-induced diabetic rats receiving a marginal mass of islet grafts by trogli-tazone, an oral antidiabetic agent. Pancreas (1996) 13:381–387.
  • HOUSBY JN, CAHILL CM, CHU B et al.: Non-steroidal anti-inflammatory drugs inhibit the expression of cytokines and induce Hsp70 in human monocytes. Cytokine (1999) 11:347–358.
  • FAWCETT TVV, XU Q, HOLBROOK NJ: Potentiation of heat stress-induced hsp70 expression in vivo by aspirin. Cell Stress Chaperones (1997) 2:104–109.
  • •Role of salicylates in amplifying the Hsp response.
  • HANSSON L, ZANCHETTI A, CARRUTHERS SG et al.: Effects of intensive blood-pressure lowering and low-dose aspirin in patients with hypertension: principal results of the Hypertension Optimal Treatment (HOT) randomised trial. HOT Study Group. Lancet (1998) 351:1755–1762.
  • ARBER N, DUBOIS RN: Nonsteroidal anti-inflammatory drugs and prevention of colorectal cancer. Curr. Gastroenterol Rep. (1999) 1:441–448.
  • •Review
  • HULL M, LIEB K, FIEBICH BL: Anti-inflammatory drugs: a hope for Alzheimer's disease? Expert. Opin. Investig. Drugs (2000) 9:671–683.
  • •Review
  • BIRO K, JEDNAKOVITS A, KUKORELLI T et al.: Bimoclomol (BRLP-42) ameliorates peripheral neuropathy in streptozotocin-induced diabetic rats. Brain Res. Bull. (1997) 44:259–263.
  • ••This and subsequent papers [157-160] describe the potentialbenefits of bimoclomol, an Hsp70-potentiating drug currently under clinical trials by Biorex.
  • BIRO K, PALHALMI J, TOTH AJ et al.: Bimoclomol improves early electrophysiological signs of retino-pathy in diabetic rats. Neuroreport (1998) 9:2029–2033.
  • VIGH L, LITERATI PN, HORVATH I et al.: Bimoclomol: a nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects. Nature Med. (1997) 3:1150–1154.
  • JEDNAKOVITS A, KURUCZ I, NANASI PP: Effect of subchronic bimoclomol treatment on vascular responsiveness and heat shock protein production in spontaneously hypertensive rats. Life Sci. (2000) 67:1791–1797.
  • ERDO F, ERDO SL: Bimoclomol protects against vascular consequences of experimental subarachnoid hemorrhage in rats. Brain Res. Bull. (1998) 45:163–166.
  • FUDABA Y, TASHIRO H, MIYATA Y et al.: Oral admini-stration of geranylgeranylacetone protects rat livers from warm ischemic injury. Transplant. Proc. (1999) 31:2918–2919.
  • ROKUTAN K, HIRAKAWA T, TESHIMA S et al.: Implica-tions of heat shock/stress proteins for medicine and disease. J. Med. Invest (1998) 44:137–147.
  • ••Good review of potential clinical applications of Hsps.
  • VOLLOCH V, RITS S: A natural ex tr acellular factor that induces Hsp72, inhibits apoptosis and restores stress resistance in aged human cells. Exp. Cell Res. (1999) 253:483–492.
  • HOSOKAWA N, HIRAYOSHI K, KUDO H et al.: Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids. Mol. Cell Biol. (1992) 12:3490–3498.
  • •Bioflavonoids may be natural inhibitors of the stress response.
  • TOSI P, VISANI G, OTTAVIANI E et al.: Reduction of heat-shock protein-70 after prolonged treatment with retinoids: biological and clinical implications. Am. J. Hematol (1997) 56:143–150.
  • LAROCCA LM, RANELLETTI FO, MAGGIANO N et al.: Differential sensitivity of leukemic and normal hematopoietic progenitors to the killing effect of hyperthermia and quercetin used in combination: role of heat-shock protein-70. Int. J. Cancer (1997) 73:75–83.
  • KUDO M, NAITO Z, YOKOYAMA M et al.: Effects of quercetin and sunphenon on responses of cancer cells to heat shock damage. Exp. Mol. Pathol. (1999) 66:66–75.
  • ASEA A, ARA G, TEICHER BA et al: Effects of the flavnoid quercetin on the response of human prostate tumors to hyperthermia in vivo. Cell Stress Chaperones (2000) 5:500.
  • POWELL BL: Acute progranulocytic leukemia. CUIT. Opin. Oncol (2001) 13:8–13.
  • NYLANDSTED J, BRAND K, JAATTELA M: Heat shock protein 70 is required for the survival of cancer cells. Ann. NY Acad. Sci. (2000) 926:122–125.
  • •Important observation on Hsp70 and cancer.
  • KING KL, LI AF, CHAU GY et al: Prognostic significance of heat shock protein-27 expression in hepatocellular carcinoma and its relation to histologic grading and survival. Cancer (2000) 88:2464–2470.
  • GEISLER JP, GEISLER HE, TAMMELA J et al.: A study of heat shock protein 27 in endometrial carcinoma. Gynecol. Oncol. (1999) 72:347–350.
  • TYTELL M, GREENBERG SG, LASEK RJ: Heat shock-like protein is transferred from glia to axon. Brain Res. (1986) 363:161–164.
  • ••First documentation of cell-to-cell transfer of Hsps.
  • JOHNSON AD, BERBERIAN PA, BOND MG: Effect of heat shock proteins on survival of isolated aortic cells from normal and atherosclerotic cynomolg-us macaques. Atheroscl (1990) 84:111–119.
  • ••First report linking Hsps and atherosclerosis.
  • JOHNSON AD, TYTELL M: Exogenous Hsp70 becomes cell associated, but not internalized, by stressed arterial smooth muscle cells. In vitro Cell. Dev. (1993) 29A:807–812.
  • ••First report indicating that Hsc70 added to the extracellularfluid can protect cells from metabolic stress.
  • HOUENOU LJ, LI L, LEI M et al.: Exogenous heat shock cognate protein Hsc70 prevents axotomy-induced death of spinal sensory neurons. Cell Stress Chaperones (1996) 1:161–166.
  • ••First report showing that administration of Hsc70 canprevent neuronal death after traumatic injury in vivo.
  • GUZHOVA IV, ARNHOLDT ACV, DARIEVA ZA et al.: Effects of exogenous stress protein 70 on the functional properties of human promonocytes through binding to cell surface and internalization. Cell Stress & Chaperones (1998) 3:67–77.
  • ••First detailed observations on the uptake of exogenouslyadministered Hsp70 by cultured cells.
  • YU Q, KENT CR, TYTELL M: Retinal uptake of intravitr e-ally injected Hsc/Hsp70 and its effect on susceptibility to light damage. Mol. Vis. (2001) 7:48–56.
  • ••First report that exogenously administered Hsp70 caninhibit death of damaged retinal cells.
  • TIDWELL JL, TYTELL M and HOUENOU LJ: Regulation of motoneuron survival by exogenous Hsp7 O. Mol.Biol.Cell (1998) 9:367a.
  • FUJIHARA SM, NADLER SG: Intranuclear targeted delivery of functional NF-kB by 70 kDa heat shock protein. EMBO J. (1999) 18:411–419.
  • •Shows that Hsp70 can serve as a carrier to transport other proteins into a cell from the outside.
  • ALDER GM, AUSTEN BM, BASHFORD CL et al.: Heat shock proteins induce pores in membranes. Biosci. Rep. (1990) 10:509–518.
  • ••The first report that Hsp70 can insert into a lipid bilayer.
  • ARISPE N, DE MAIO A: ATP and ADP modulate a cation channel formed by Hsc70 in acidic phospholipid membranes. J. Biol. Chem. (2000) 275:30839–30843.
  • •Further study of the ability of Hsp70 form ion channels in a lipid bilayer.
  • SMITH PJS, DUTHIE GG, SHIPLEY A et al.: Steady-state calcium efflux from Aplysia neurons: Perturbation by 11.202 and protection by stress protein, Hsp70. Bull. (1993) 185:293–294.
  • SU C-Y, CHONG K-Y, EDELSTEIN K et al.: Constitutive Hsp7 0 attenuates hydrogen peroxide-induced membrane lipid peroxidation. Biochem. Biophys. Res. Comm. (1999) 265:279–284.
  • VIGH L, MARESCA B, HARWOOD JL: Does the membra-ne's physical state control the expression of heat shock and other genes? Trends Biochem. (1998) 23:369–374.
  • •Interesting hypothesis that the cell membrane may be a key site of regulation and action of Hsps.
  • PFANNER N, CRAIG EA, MEIJER M: The protein import machinery of the mitochondrial inner membrane. Trends Biochem. (1994) 19:368–372.
  • TERLECKY SR: Hsp7Os and lysosomal proteolysis. Experientia (1994) 50:1021–1025.
  • •One of the first reports suggesting a role for Hsp70 in lysosome function.
  • VANBUSKIRK A, CRUMP BL, MARGOLIASH E et al: A peptide binding protein having a role in antigen presentation is a member of the Hsp70 heat shock family. J. Exp. Med. (1989) 170:1799–1809.
  • PIERCE SK: Molecular chaperones in the processing and presentation of antigen to helper T cells. Experi-entia (1994) 50:1026–1030.
  • ••This and the next paper are two of the first illustrating theroles of Hsps in the immune response.
  • SRIVASTAVA PK, UDONO H, BLACHERE NE et al: Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics (1994) 39:93–98.
  • SUZUE K, YOUNG RA: Heat shock proteins as immuno-logical carriers and vaccines. EXS (1996) 77:451–465.
  • MELCHER A, MURPHY S, VILE R: Heat shock protein expression in target cells infected with low levels of replication-competent virus contributes to the immunogenicity of adenoviral vectors. Hum. Gene Ther. (1999) 10:1431–1442.
  • BLACHERE NE, LI Z, CHANDAWARKAR RY et al.: Heat shock protein-peptide complexes, reconstituted in vitro, elicit peptide-specific cytotoxic T lymphocyte response and tumor immunity. J. Exp. Med. (1997) 186:1315–1322.
  • BARRIOS C, GEORGOPOULOS C, LAMBERT P-H et al: Heat shock proteins as carrier molecules: In vivo helper effect mediated by Escherichia coli Gr oEL and DnaK proteins requires cross-linking with antigen. Clin. Exp. Immunol. (1994) 98:229–233.
  • UDONO H, SRIVASTAVA PK: Heat shock protein 70-associated peptides elicit specific cancer immunity. J. Exp. Med. (1993) 178:1391–1396.
  • ASEA A, KRAEFT S-K, KURT-JONES EA et al: Hsp70 stimulates cytokine production through a CD14-dependentpathway, demonstrating its dual role as a chaperone and cytokine. Nature Med. (2000) 6:435–442.
  • •An important paper on the immunomodulatory effects of exogenous Hsp70.
  • BINDER RJ, HARRIS ML, MENORET A et al: Saturation, competition and specificity in interaction of heat shock proteins (Hsp) gp96, Hsp90 and Hsp70 with CD11b+ cells. J. Immunol. (2000) 165:2582–2587.
  • ••Key characterisation of an Hsp receptor on immune systemcells
  • HALL TJ: Role of Hsp70 in cytokine production. Experi-entia (1994) 50:1048–1053.
  • CALLAHAN TE, MARINS J, WELCH WJ et al: Heat shock attenuates oxidation and accelerates apoptosis in human neutrophils. j Surg. Res. (1999) 85:317–322.
  • Y00 CG, LEES, LEE CT et al.:Anti-inflammatory effect of heat shock protein induction is related to stabilization of I kappa B alpha through preventing I kappa B kinase activation in respiratory epithelial cells. J Immunol (2000) 1 6 4:5416–5423.
  • •This and the next paper illustrate potential anti-inflammatory functions of the Hsp response.
  • HIGHTOWER LE, PERDRIZET GA, REINSKI M et al.: The heat shock response: a brake on inflammation. Cell Stress Chaperones (2000) 5:376–377.

Websites

  • www.biorex.hu A pharmaceutical research company in Hungary.
  • www.stressgen.com StressGen Biotechnologies Corp. Victoria, British Columbia, Canada.
  • www.antigenics.com Antigenics, LLC, Woburn, MA.

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