Abstract
The accumulation of aggregated, misfolded proteins and the appearance of neurotoxic aggregates of Aβ and tau proteins play a key role in the development of Alzheimer’s disease. HSP70 can inhibit neurodegeneration associated with Alzheimer’s disease because this protein can: (i) aid in the degradation of intracellular and extracellular Aβ aggregates; (ii) restrict tau protein hyperphosphorylation and facilitate the degradation of dysfunctional tau proteins; (iii) limit NO overproduction; and (iv) regulate apoptosis. It is also likely that HSP70 may delay the development of Alzheimer’s disease by limiting insulin receptor desensitization. HSP70 can limit ischemia myocardial injury by: (i) maintaining protein homeostasis in cells; (ii) stabilizing lysosomal membranes; (iii) inhibiting the excessive activation of ADP-ribose polymerase; and (iv) blocking ischemia-induced apoptosis. During the excessive systemic inflammatory response syndrome (SIRS) that occurs in heart surgery, extracellular HSP70 initiates inflammatory effects through the stimulation of immune cell receptors. In contrast, intracellular HSP70, exerts anti-inflammatory effects on the inflammatory balance of SIRS by inhibiting proinflammatory signaling in immune cells.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Ammirante M, Rosati A, Gentilella A et al (2008) The activity of hsp90 alpha promoter is regulated by NF-kappa B transcription factors. Oncogene 27(8):1175–1178
Ansar S, Burlison JA, Hadden MK et al (2007) A non-toxic Hsp90 inhibitor protects neurons from Abeta-induced toxicity. Bioorg Med Chem Lett 17(7):1984–1990
Archbold RA, Curzen NP (2003) Off-pump coronary artery bypass graft surgery: the incidence of postoperative atrial fibrillation. Heart 89(10):1134–1137
Arispe N, Doh M, Simakova O, Kurganov B, De Maio A (2004) Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J 18(14):1636–1645
Asea A, Rehli M, Kabingu E et al (2002) Novel signal transduction pathway utilized by extracellular HSP70: role of toll-like receptor (TLR) 2 and TLR4. J Biol Chem 277(17):15028–15034
Basu S, Binder RJ, Suto R, Anderson KM, Srivastava PK (2000) Necrotic but not apoptotic cell death releases heat shock proteins, which deliver a partial maturation signal to dendritic cells and activate the NF-kappa B pathway. Int Immunol 12(11):1539–1546
Bogoyevitch MA, Gillespie-Brown J, Ketterman AJ et al (1996) Stimulation of the stress-activated mitogen-activated protein kinase subfamilies in perfused heart p38/RK mitogen-activated protein kinases and c-Jun N-terminal kinases are activated by ischemia/reperfusion. Circ Res 79(2):162–173
Bonini NM (2002) Chaperoning brain degeneration. Proc Natl Acad Sci U S A 99(Suppl 4):16407–16411
Borchelt DR, Ratovitski T, van Lare J et al (1997) Accelerated amyloid deposition in the brains of transgenic mice coexpressing mutant presenilin 1 and amyloid precursor proteins. Neuron 19:939–945
Brown IR, Gozes I (1998) Stress genes in the nervous system during development and aging diseases. Ann N Y Acad Sci 851:123–128
Calabrese V, Copani A, Testa D et al (2000) Nitric oxide synthase induction in astroglial cell cultures: effect on heat shock protein 70 synthesis and oxidant/antioxidant balance. J Neurosci Res 60(5):613–622
Campion D, Flaman JM, Brice A et al (1995) Mutations of the presenilin I gene in families with early-onset Alzheimer’s disease. Hum Mol Genet 4:2373–2377
Campisi J, Leem TH, Fleshner M (2003) Stress-induced extracellular Hsp72 is a functionally significant danger signal to the immune system. Cell Stress Chaperones 8(3):272–286
Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267–298
Cavaillon JM, Adrie C, Fitting C, Adib-Conquy M (2005) Reprogramming of circulatory cells in sepsis and SIRS. J Endotoxin Res 11(5):311–320
Chabrier PE, Demerlé-Pallardy C, Auguet M (1999) Nitric oxide synthases: targets for therapeutic strategies in neurological diseases. Cell Mol Life Sci 55(8–9):1029–1035
Chartier-Harlin MC, Crawford F, Houlden H et al (1991) Early-onset Alzheimer’s disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene. Nature 353:844–846
Chase MA, Wheeler DS, Lierl KM, Hughes VS, Wong HR, Page K (2007) Hsp72 induces inflammation and regulates cytokine production in airway epithelium through a TLR4- and NF-kappaB-dependent mechanism. J Immunol 179(9):6318–6324
Chen S, Brown IR (2007) Neuronal expression of constitutive heat shock proteins: implications for neurodegenerative diseases. Cell Stress Chaperones 12:51–58
Christen Y (2000) Oxidative stress and Alzheimer disease. Am J Clin Nutr 71(2):621–629
Cleary JP, Walsh DM, Hofmeister JJ et al (2005) Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci 8:79–84
Clippingdale AB, Wade JD, Barrow CJ (2001) The amyloid-beta peptide and its role in Alzheimer’s disease. J Pept Sci 7(5):227–249
Cottrell BA, Galvan V, Banwait S et al (2005) A pilot proteomic study of amyloid precursor interactors in Alzheimer’s disease. Ann Neurol 58(2):277–289
Currie RW, Karmazyn M, Kloc M, Mailer K (1998) Heat-shock response is associated with enhanced postischemic ventricular recovery. Circ Res 3:543–549
D’Andrea MR, Nagele RG, Wang HY, Peterson PA, Lee DH (2001) Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer’s disease. Histopathology 38(2):120–134
de la Monte SM (2009) Insulin resistance and Alzheimer’s disease. BMB Rep 42(8):475–481
Demidov ON, Tyrenko VV, Svistov AS et al (1999) Heat shock proteins in cardiosurgery patients. Eur J Cardiothorac Surg 16(4):444–449
Dewji NN (2005) The structure and functions of the presenilins. Cell Mol Life Sci 62:1109–1119
Dewji NN (2006) Presenilin structure in mechanisms leading to Alzheimer’s disease. J Alzheimers Dis 10:277–290
Dewji NN, Do C, Bayney RM (1995) Transcriptional activation of Alzheimer’s beta-amyloid precursor protein gene by stress. Brain Res Mol Brain 33:245–253
Dickey CA, Dunmore J, Lu B et al (2006) HSP induction mediates selective clearance of tau phosphorylated at proline-directed Ser/Thr sites but not KXGS (MARK) sites. FASEB J 20(6):753–755
Dickey CA, Koren J, Zhang YJ et al (2008) (2008) Akt and CHIP coregulate tau degradation through coordinated interactions. Proc Natl Acad Sci U S A. 105(9):3622–3627
Dou F, Netzer WJ, Tanemura K et al (2003) Chaperones increase association of tau protein with microtubules. Proc Natl Acad Sci U S A 100(2):721–726
Duff K, Eckman C, Zehr C et al (1996) Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. Nature 383:710–713
Dybdahl B, Slørdahl SA, Waage A, Kierulf P, Espevik T, Sundan A (2005) Myocardial ischaemia and the inflammatory response: release of heat shock protein 70 after myocardial infarction. Heart 91(3):299–304
Dybdahl B, Wahba A, Haaverstad R et al (2004) On-pump versus off-pump coronary artery bypass grafting: more heat-shock protein 70 is released after on-pump surgery. Eur J Cardiothorac Surg 25(6):985–992
Dybdahl B, Wahba A, Lien E et al (2002) Inflammatory response after open heart surgery: release of heat-shock protein 70 and signaling through toll-like receptor-4. Circulation 105(6):685–690
Elliott E, Tsvetkov P, Ginzburg I (2007) BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. J Biol Chem 51:37276–37284
Estus S, Golde TE, Kunishita T et al (1992) Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor. Science 255:726–728
Evans CG, Wisén S, Gestwicki JE (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1–42) aggregation in vitro. J Biol Chem 281(44):33182–33191
Feinstein DL, Galea E, Aquino DA, Li GC, Xu H, Reis DJ (1996) Heat shock protein 70 suppresses astroglial-inducible nitric-oxide synthase expression by decreasing NFkappaB activation. J Biol Chem 271(30):17724–17732
Fonte J, Bates KA, Robertson TA, Martins RN, Harvey AR (2002) Chronic gliosis triggers Alzheimer’s disease-like processing of amyloid precursor protein. Neuroscience 113(4):785–796
Gabai VL, Kabakov AE (1993) Rise in heat-shock protein level confers tolerance to energy deprivation. FEBS Lett 327(3):247–250
Gabai VL, Mosina VA, Budagova KR, Kabakov AE (1995) Spontaneous overexpression of heat-shock proteins in Ehrlich ascites carcinoma cells during in vivo growth. Biochem Mol Biol Int 35(1):95–102
Getchell TV, Kulkarni-Narla A, Schmitt FA, Getchell ML (1996) Manganese and copper-zinc superoxide dismutases in the human olfactory mucosa: increased immunoreactivity in Alzheimer’s disease. Exp Neurol 140(2):115–125
Giannessi D, Caselli C, Vitale RL et al (2003) Possible cardioprotective effect of heat shock proteins during cardiac surgery in pediatric patients. Pharmacol Res 48(5):519–529
Goate A, Chartier-Harlin MC, Mullan M et al (1991) Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer’s disease. Nature 349:704–706
Golde TE, Estus S, Younkin LH, Selkoe DJ, Younkin SG (1992) Processing of the amyloid protein precursor to potentially amyloidogenic derivatives. Science 255:728–730
Gong Y, Chang L, Viola KL et al (2003) Alzheimer’s disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc Natl Acad Sci USA 100:10417–10422
Gouras GK, Tsai J, Naslund J et al (2000) Intraneuronal Abeta42 accumulation in human brain. Am J Pathol 156(1):15–20
Gross C, Hansch D, Gastpar R, Multhoff G (2003) Interaction of heat shock protein 70 peptide with NK cells involves the NK receptor CD94. Biol Chem 384(2):267–279
Guillozet-Bongaarts AL, Garcia-Sierra F, Reynolds MR et al (2005) Tau truncation during neurofibrillary tangle evolution in Alzheimer’s disease. Neurobiol Aging 26(7):1015–1022
Halverson K, Fraser PE, Kirschner DA, Lansbury PT Jr (1990) Molecular determinants of amyloid deposition in Alzheimer’s disease: conformational studies of synthetic beta-protein fragments. Biochem 29:2639–2644
Hamilton KL, Gupta S, Knowlton AA (2004) Estrogen and regulation of heat shock protein expression in female cardiomyocytes: cross-talk with NF kappa B signaling. J Mol Cell Cardiol 36(4):577–584
Hayashi Y, Sawa Y, Fukuyama N, Nakazawa H, Matsuda H (2002) Preoperative glutamine administration induces heat-shock protein 70 expression and attenuates cardiopulmonary bypass-induced inflammatory response by regulating nitric oxide synthase activity. Circulation 106(20):2601–2607
Hiesmayr MJ, Spittler A, Lassnigg A et al (1999) Alterations in the number of circulating leucocytes, phenotype of monocyte and cytokine production in patients undergoing cardiothoracic surgery. Clin Exp Immunol 2:315–323
Hock C, Konietzko U, Streffer JR et al (2003) Papassotiropoulos A, Nitsch RM. Antibodies against beta-amyloid slow cognitive decline in Alzheimer’s disease. Neuron 38:547–554
Holcomb L, Gordon MN, McGowan E et al (1998) Accelerated Alzheimer-type phenotype in transgenic mice carrying both mutant amyloid precursor protein and presenilin 1 transgenes. Nat Med 4:97–100
Holcomb LA, Gordon MN, Jantzen P, Hsiao K, Duff K, Morgan D (1999) Behavioral changes in transgenic mice expressing both amyloid precursor protein and presenilin-1 mutations: lack of association with amyloid deposits. Behav Genet 29:177–185
Hsiao K, Chapman P, Nilsen S et al (1996) Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 274:99–102
Hu J, LaDu MJ, Van Eldik LJ (1998) Apolipoprotein E attenuates beta-amyloid-induced astrocyte activation. J Neurochem 71(4):1626–1634
Hutton M, Lendon CL, Rizzu P et al (1998) Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393:702–705
Jayakumar J, Suzuki K, Khan M et al (2000) Gene therapy for myocardial protection: transfection of donor hearts with heat shock protein 70 gene protects cardiac function against ischemia-reperfusion injury. Circulation 102(19 Suppl 3):III302-6
Jayakumar J, Suzuki K, Sammut IA et al (2001) Heat shock protein 70 gene transfection protects mitochondrial and ventricular function against ischemia-reperfusion injury. Circulation 104(12 Suppl 1):303–307
Johnson G, Refolo LM, Wallace W (1993) Heat-shocked neuronal PC12 cells reveal Alzheimer’s disease–associated alterations in amyloid precursor protein and tau. Ann N Y Acad Sci 695:194–197
Kabakov AE, Gabai VL (1995) Heat shock-induced accumulation of 70-kDa stress protein (HSP70) can protect ATP-depleted tumor cells from necrosis. Exp Cell Res 217(1):15–21
Kakimura J, Kitamura Y, Takata K et al (2002) Possible involvement of ER chaperone Grp78 on reduced formation of amyloid-beta deposits. Ann N Y Acad Sci 977:327–332
Kalawski R, Bugajski P, Smielecki J et al (1998) Soluble adhesion molecules in reperfusion during coronary bypass grafting. Eur J Cardiothorac Surg 14(3):290–295
Kirby BA, Merril CR, Ghanbari H, Wallace WC (1994) Heat shock proteins protect against stress-related phosphorylation of tau in neuronal PC12 cells that have acquired thermotolerance. J Neurosci 14(9):5687–5693
Klucken J, Shin Y, Masliah E, Hyman BT, McLean PJ (2004) Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J Biol Chem 279(24):25497–25502
Koren J 3rd, Jinwal UK, Lee DC et al (2009) Chaperone signalling complexes in Alzheimer’s disease. J Cell Mol Med 13(4):619–630
Kosik KS, Ahn J, Stein R, Yeh LA (2002) Discovery of compounds that will prevent tau pathology. J Mol Neurosci 19(3):261–266
Kumar-Singh S, De Jonghe C, Cruts M et al (2000) Nonfibrillar diffuse amyloid deposition due to a gamma (42)-secretase site mutation points to an essential role for N-truncated A beta(42) in Alzheimer’s disease. Hum Mol Genet 18:2589–2598
Laderoute KR, Webster KA (1997) Hypoxia/reoxygenation stimulates Jun kinase activity through redox signaling in cardiac myocytes. Circ Res 80(3):336–344
Lau SS, Griffin TM, Mestril R (2000) Protection against endotoxemia by HSP70 in rodent cardiomyocytes. Am J Physiol Heart Circ Physiol 278(5):1439–1445
Lepore DA, Knight KR, Anderson RL, Morrison WA (2001) Role of priming stresses and Hsp70 in protection from ischemia-reperfusion injury in cardiac and skeletal muscle. Cell Stress Chaperones 6(2):93–96
Lester-Coll N, Rivera EJ, Soscia SJ, Doiron K, Wands JR, de la Monte SM (2006) Intracerebral streptozotocin model of type 3 diabetes: relevance to sporadic Alzheimer’s disease. J Alzheimers Dis 9(1):13–33
Magrané J, Smith RC, Walsh K, Querfurth HW (2004) Heat shock protein 70 partici- pates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons. J Neurosci 24:1700–1706
Marucci A, Miscio G, Padovano L et al (2009) The role of HSP70 on ENPP1 expression and insulin-receptor activation. J Mol Med (Berl) 87(2):139–144
McCarty MF (2005) Induction of heat shock proteins may combat insulin resistance. Med Hypotheses 66(3):527–534
Meyer-Luehmann M, Spires-Jones TL, Prada C et al (2008) Rapid appearance and local toxicity of amyloid-beta plaques in a mouse model of Alzheimer’s disease. Nature 451:720–724
Millar DG, Garza KM, Odermatt B, Elford AR, Ono N, Li Z, Ohashi PS (2003) Hsp70 promotes antigen-presenting cell function and converts T-cell tolerance to autoimmunity in vivo. Nat Med 9(12):1469–1476
Morino S, Kondo T, Sasaki K et al (2008) Mild electrical stimulation with heat shock ameliorates insulin resistance via enhanced insulin signaling. PLoS ONE 3(12):4068
Mullan M, Houlden H, Windelspecht M et al (1992) A locus for familial early-onset Alzheimer’s disease on the long arm of chromosome 14, proximal to the alpha 1-antichymotrypsin gene. Nat Genet 2:340–342
Nathan N, Preux PM, Feiss P, Denizot Y (2000) Plasma interleukin-4, interleukin-10, and interleukin-13 concentrations and complications after coronary artery bypass graft surgery. J Cardiothorac Vasc Anesth 14(2):156–160
Nitsch RM, Hock C (2008) Targeting beta-amyloid pathology in Alzheimer’s Disease with Abeta immunotherapy. Neurotherapeutics 5:415–420
Noble W, Planel E, Zehr C et al (2005) Inhibition of glycogen synthase kinase-3 by lithium correlates with reduced tauopathy and degeneration in vivo. Proc Natl Acad Sci U S A 102(19):6990–6995
Oehler R, Pusch E, Zellner M et al (2001) Cell type-specific variations in the induction of hsp70 in human leukocytes by fever like whole body hyperthermia. Cell Stress Chaperones 6(4):306–315
Ohtsuka K, Suzuki T (2000) Roles of molecular chaperones in the nervous system. Brain Res Bull 53(2):141–146
Okubo S, Wildner O, Shah MR, Chelliah JC, Hess ML, Kukreja RC (2001) Gene transfer of heat-shock protein 70 reduces infarct size in vivo after ischemia/reperfusion in the rabbit heart. Circulation 103(6):877–881
Opar A (2008) Mixed results for disease-modification strategies for Alzheimer’s disease. Nat Rev Drug Discov 7(9):717–718
Osborne R (2008) Myriad stumbles, Wyeth closes on Alzheimer’s. Nat Biotechnol 26(8):841–843
Pappolla MA, Sos M, Omar RA, Sambamurti K (1996) The heat shock/oxidative stress connection. Relevance to Alzheimer disease. Mol Chem Neuropathol 28(1–3):21–34
Pei JJ, Khatoon S, An WL, Nordlinder M et al (2003) Role of protein kinase B in Alzheimer’s neurofibrillary pathology. Acta Neuropathol 105(4):381–392
Perez-Tur J, Croxton R, Wright K et al (1996) A further presenilin 1 mutation in the exon 8 cluster in familial Alzheimer’s disease. Neurodegeneration 5:207–212
Petrucelli L, Dickson D, Kehoe K et al (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum Mol Genet 13(7):703–714
Piccoletti R, Schiaffonati L, Maroni P, Bendinelli P, Tiberio L (2001) Hyperthermia induces gene expression of heat shock protein 70 and phosphorylation of mitogen activated protein kinases in the rat cerebellum. Neurosci Lett 312(2):75–78
Pickering-Brown S, Baker M, Yen SH et al (2000) Pick’s disease is associated with mutations in the tau gene. Ann Neurol 48(6):859–867
Pockley AG, Muthana M, Calderwood SK (2008) The dual immunoregulatory roles of stress proteins. Trends Biochem Sci 33(2):71–79
Ramsden M, Kotilinek L, Forster C et al (2005) Age-dependent neurofibrillary tangle formation, neuron loss, and memory impairment in a mouse model of human tauopathy (P301L). J Neurosci 25(46):10637–10647
Ran R, Lu A, Zhang L et al (2004) Hsp70 promotes TNF-mediated apoptosis by binding IKK gamma and impairing NF-kappa B survival signaling. Genes Dev 18(12):1466–1481
Reger MA, Watson GS, Green PS et al (2008) Intranasal insulin improves cognition and modulates β-amyloid in early AD. Neurology 70(6):440–448
Renkawek K, Bosman GJ, de Jong WW (1994) Expression of small heat-shock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia. Acta Neuropathol 87(5):511–519
Renkawek K, Bosman GJ, Gaestel M (1993) Increased expression of heat-shock protein 27 kDa in Alzheimer disease: a preliminary study. Neuroreport 5(1):14–16
Rizzini C, Goedert M, Hodges JR et al (2000) Tau gene mutation K257T causes a tauopathy similar to Pick’s disease. J Neuropathol Exp Neurol 59:990–1001
Rothenburger M, Tjan TD, Schneider M et al (2003) The impact of the pro- and anti-inflammatory immune response on ventilation time after cardiac surgery. Cytometry B Clin Cytom 53(1):70–74
Sablotzki A, Friedrich I, Mühling J et al (2002) The systemic inflammatory response syndrome following cardiac surgery: different expression of proinflammatory cytokines and procalcitonin in patients with and without multiorgan dysfunctions. Perfusion 17(2):103–109
Sadik K, Wilcock G (2003) The increasing burden of Alzheimer disease. Alzheimer Dis Assoc Disord 17(Suppl 3):75–79
Saito K, Dai Y, Ohtsuka K (2005) Enhanced expression of heat shock proteins in gradually dying cells and their release from necrotically dead cells. Exp Cell Res 310(1):229–236
Salbaum JM, Weidemann A, Lemaire HG, Masters CL, Beyreuther K (1998) The promoter of Alzheimer’s disease amyloid A4 precursor gene. EMBO J 7(9):2807–2813
Santacruz K, Lewis J, Spires T et al (2005) Tau suppression in a neurodegenerative mouse model improves memory function. Science 309(5733):476–481
Sarkar M, Kuret J, Lee G (2008) Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone. J Neurosci Res 86(12):2763–2773
Sasaki A, Yamaguchi H, Ogawa A, Sugihara S, Nakazato Y (1997) Microglial activation in early stages of amyloid beta protein deposition. Acta Neuropathol 94(4):316–322
Satoh M, Shimoda Y, Akatsu T, Ishikawa Y, Minami Y, Nakamura M (2006) Elevated circulating levels of heat shock protein 70 are related to systemic inflammatory reaction through monocyte Toll signal in patients with heart failure after acute myocardial infarction. Eur J Heart Fail 8(8):810–815
Schenk DB, Seubert P, Grundman M, Black R (2005) A beta immunotherapy: lessons learned for potential treatment of Alzheimer’s disease. Neurodegener Dis 2:255–260
Schröder O, Schulte KM, Ostermann P et al (2003) Heat shock protein 70 genotypes HSPA1B and HSPA1L influence cytokine concentrations and interfere with outcome after major injury. Crit Care Med 31(1):73–79
Shankar GM, Bloodgood BL, Townsend M et al (2007) Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci 27:2866–2875
Shankar GM, Li S, Mehta TH et al (2008) Amyloid-beta protein dimers isolated directly from Alzheimer’s brains impair synaptic plasticity and memory. Nat Med 14(8):837–842
Sherrington R, Rogaev EI, Liang Y et al (1995) Cloning of a gene bearing missense mutations in early-onset familial Alzheimer’s disease. Nature 375:754–760
Shimura H, Miura-Shimura Y, Kosik KS (2004) Binding of tau to heat shock protein 27 leads to decreased concentration of hyperphosphorylated tau and enhanced cell survival. J Biol Chem 279(17):17957–17962
Shoji M, Golde TE, Ghiso J et al (1992) Production of the Alzheimer amyloid beta protein by normal proteolytic processing. Science 258:126–129
Simard AR, Soulet D, Gowing G, Julien JP, Rivest S (2006) Bone marrow-derived microglia play a critical role in restricting senile plaque formation in Alzheimer’s disease. Neuron 49(4):489–502
Singleton KD, Serkova N, Beckey VE, Wischmeyer PE (2005) Glutamine attenuates lung injury and improves survival after sepsis: role of enhanced heat shock protein expression. Crit Care Med 33(6):1206–1213
Singleton KD, Wischmeyer PE (2006) Effects of HSP70.1/3 gene knockout on acute respiratory distress syndrome and the inflammatory response following sepsis. Am J Physiol Lung Cell Mol Physiol 290(5):956–961
Smith RC, Rosen KM, Pola R, Magrané J (2005) Stress proteins in Alzheimer’s disease. Int J Hyperthermia 21(5):421–431
Spillantini MG, Murrell JR, Goedert M, Farlow MR, Klug A, Ghetti B (1998) Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci USA 95:7737–7741
Spires-Jones TL, de Calignon A, Matsui T et al (2008) In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons. J Neurosci 28:862–867
St Rammos K, Koullias GJ, Hassan MO et al (2002) Low preoperative HSP70 atrial myocardial levels correlate significantly with high incidence of postoperative atrial fibrillation after cardiac surgery. Cardiovasc Surg 10(3):228–232
Stalder AK, Ermini F, Bondolfi L et al (2005) Invasion of hematopoietic cells into the brain of amyloid precursor protein transgenic mice. J Neurosci 25(48):11125–11132
Sun YX, Wright HT, Janciauskiene S (2002) Glioma cell activation by Alzheimer’s peptide Abeta1-42, alpha1-antichymotrypsin, and their mixture. Cell Mol Life Sci 59(10):1734–1743
Szerafin T, Hoetzenecker K, Hacker S et al (2008) Heat shock proteins 27, 60, 70, 90alpha, and 20S proteasome in on-pump versus off-pump coronary artery bypass graft patients. Ann Thorac Surg 85(1):80–87
Taggart DP, Bakkenist CJ, Biddolph SC, Graham AK, McGee JO (1997) Induction of myocardial heat shock protein 70 during cardiac surgery. J Pathol 182(3):362–366
Takeuchi A, Irizarry MC, Duff K et al (2000) Age-related amyloid beta deposition in transgenic mice overexpressing both Alzheimer mutant presenilin 1 and amyloid beta precursor protein Swedish mutant is not associated with global neuronal loss. Am J Pathol 157:331–339
Tang D, Kang R, Xiao W, Wang H, Calderwood SK, Xiao X (2007) The anti-inflammatory effects of heat shock protein 72 involve inhibition of high-mobility-group box 1 release and proinflammatory function in macrophages. J Immunol 179(2):1236–1244
Temple SE, Cheong KY, Ardlie KG, Sayer D, Waterer GW (2004) The septic shock associated HSPA1B1267 polymorphism influences production of HSPA1A and HSPA1B. Intensive Care Med 30(9):1761–1767
Thériault JR, Mambula SS, Sawamura T, Stevenson MA, Calderwood SK (2005) Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett 579(9):1951–1960
Tomic V, Russwurm S, Möller E et al (2005) Transcriptomic and proteomic patterns of systemic inflammation in on-pump and off-pump coronary artery bypass grafting. Circulation 112(19):2912–2920
Tytell M, Greenberg SG, Lasek RJ (1986) Heat shock-like protein is transferred from glia to axon. Brain Res 363:161–164
Vabulas RM, Ahmad-Nejad P, Ghose S et al (2002) HSP70 as endogenous stimulus of the Toll/interleukin-1 receptor signal pathway. J Biol Chem 277(17):15107–15112
Van Broeckhoven C, Haan J, Bakker E et al (1990) Amyloid beta protein precursor gene and hereditary cerebral hemorrhage with amyloidosis (Dutch). Science 248:1120–1122
Van Molle W, Wielockx B, Mahieu T et al (2002) HSP70 protects against TNF-induced lethal inflammatory shock. Immunity 16(5):685–695
Vega VL, Rodríguez-Silva M, Frey T et al (2008) Hsp70 translocates into the plasma membrane after stress and is released into the extracellular environment in a membrane-associated form that activates macrophages. J Immunol 180(6):4299–4307
Vincent SR, Kimura H (1992) Histochemical mapping of nitric oxide synthase in the rat brain. Neuroscience 46(4):755–784
Wakutani Y, Urakami K, Shimomura T, Takahashi K (1995) Heat shock protein 70 mRNA levels in mononuclear blood cells from patients with dementia of the Alzheimer type. Dementia 6(6):301–305
Walsh DM, Klyubin I, Fadeeva JV et al (2002) Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416:535–539
Wang R, Kovalchin JT, Muhlenkamp P, Chandawarkar RY (2006) Exogenous heat shock protein 70 binds macrophage lipid raft microdomain and stimulates phagocytosis, processing, and MHC-II presentation of antigens. Blood 107(4):1636–1642
Wang S, Diller KR, Aggarwal SJ (2003) Kinetics study of endogenous heat shock protein 70 expression. J Biomech Eng 125(6):794–797
Wang Y, Su B, Sah VP, Brown JH, Han J, Chien KR (1998) Cardiac hypertrophy induced by mitogen-activated protein kinase kinase 7, a specific activator for c-Jun NH2-terminal kinase in ventricular muscle cells. J Biol Chem 273(10):5423–5426
Weaver CL, Espinoza M, Kress Y, Davies P (2000) Conformational change as one of the earliest alterations of tau in Alzheimer’s disease. Neurobiol Aging 21(5):719–727
Weiss YG, Bromberg Z, Raj N et al (2007) Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Crit Care Med 35(9):2128–2138
Wilcock DM, Alamed J, Gottschall PE et al (2006) Deglycosylated anti-amyloid-beta antibodies eliminate cognitive deficits and reduce parenchymal amyloid with minimal vascular consequences in aged amyloid precursor protein transgenic mice. J Neurosci 26:5340–5346
Wilcock DM, Rojiani A, Rosenthal A et al (2004) Passive immunotherapy against Abeta in aged APP-transgenic mice reverses cognitive deficits and depletes parenchymal amyloid deposits in spite of increased vascular amyloid and microhemorrhage. J Neuroinflammation 1:24
Williams RS, Benjamin IJ (2000) Protective responses in the ischemic myocardium. J Clin Invest 106(7):813–818
Wirths O, Multhaup G, Czech C et al (2001) Reelin in plaques of beta-amyloid precursor protein and presenilin-1 double-transgenic mice. Neurosci Lett 316(3):145–148
Xiao X, Zuo X, Davis AA et al (1999) HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice. EMBO J 18(21):5943–5952
Yan SD, Fu J, Soto C et al (1997) An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer’s disease. Nature 389(6652):689–695
Yang SN, Hsieh WY, Liu DD, Tsai LM, Tung CS, Wu JN (1998) The involvement of nitric oxide in synergistic neuronal damage induced by beta-amyloid peptide and glutamate in primary rat cortical neurons. Chin J Physiol 41(3):175–179
Yoo BC, Seidl R, Cairns N, Lubec G (1999) Heat-shock protein 70 levels in brain of patients with Down syndrome and Alzheimer’s disease. J Neural Transm Suppl 57:315–322
Yoo CG, Lee S, Lee CT, Kim YW, Han SK, Shim YS (2000a) 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 164(10):5416–5423
Yoo JC, Pae HO, Choi BM et al (2000b) Lonizing radiation potentiates the induction of nitric oxide synthase by interferon-gamma (Ifn-gamma) or Ifn-gamma and lipopolysaccharide in bnl cl.2 murine embryonic liver cells: role of hydrogen peroxide. Free Radic Biol Med 28(3):390–396
Zachayus JL, Benatmane S, Plas C (1996) Role of Hsp70 synthesis in the fate of the insulin-receptor complex after heat shock in cultured fetal hepatocytes. J Cell Biochem 61(2):216–229
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
Copyright information
© 2013 The Author(s)
About this chapter
Cite this chapter
Malyshev, I. (2013). The Role of HSP70 in the Protection of: (A) The Brain in Alzheimer’s Disease and (B) The Heart in Cardiac Surgery. In: Immunity, Tumors and Aging: The Role of HSP70. SpringerBriefs in Biochemistry and Molecular Biology, vol 6. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5943-5_8
Download citation
DOI: https://doi.org/10.1007/978-94-007-5943-5_8
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-007-5942-8
Online ISBN: 978-94-007-5943-5
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)