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Volumn 8, Issue 7, 2013, Pages

The Role of Heat Shock Protein 70 in the Protective Effect of YC-1 on β-Amyloid-Induced Toxicity in Differentiated PC12 Cells

Author keywords

[No Author keywords available]

Indexed keywords

1H 1,2,4 OXADIAZOLO[4,3 A]QUINOXALIN 1 ONE; AMYLOID BETA PROTEIN[25-35]; CALPAIN 1; HEAT SHOCK PROTEIN 70; LIFICIGUAT; PROTEIN P25; QUERCETIN; SMALL INTERFERING RNA; TAU PROTEIN;

EID: 84880794115     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0069320     Document Type: Article
Times cited : (19)

References (42)
  • 2
    • 33745140951 scopus 로고    scopus 로고
    • Tau phosphorylation and aggregation in Alzheimer's disease pathology
    • Avila J, (2006) Tau phosphorylation and aggregation in Alzheimer's disease pathology. FEBS Lett 580: 2922-2927.
    • (2006) FEBS Lett , vol.580 , pp. 2922-2927
    • Avila, J.1
  • 3
    • 0036672695 scopus 로고    scopus 로고
    • Calpain inhibitors: a treatment for Alzheimer's disease
    • Di Rosa G, Odrijin T, Nixon RA, Arancio O, (2002) Calpain inhibitors: a treatment for Alzheimer's disease. J Mol Neurosci 19: 135-141.
    • (2002) J Mol Neurosci , vol.19 , pp. 135-141
    • Di Rosa, G.1    Odrijin, T.2    Nixon, R.A.3    Arancio, O.4
  • 4
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J, Craig EA, (1994) Heat-shock proteins as molecular chaperones. Eur J Biochem 219: 11-23.
    • (1994) Eur J Biochem , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 5
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto RI, Kline MP, Bimston DN, Cotto JJ, (1997) The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem 32: 17-29.
    • (1997) Essays Biochem , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 6
    • 33746330168 scopus 로고    scopus 로고
    • Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators
    • Brodsky JL, Chiosis G, (2006) Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Curr Top Med Chem 6: 1215-1225.
    • (2006) Curr Top Med Chem , vol.6 , pp. 1215-1225
    • Brodsky, J.L.1    Chiosis, G.2
  • 7
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer MP, Bukau B, (2005) Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62: 670-684.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 8
    • 0026091893 scopus 로고
    • Increased synthesis and accumulation of heat shock 70 proteins in Alzheimer's disease
    • Perez N, Sugar J, Charya S, Johnson G, Merril C, et al. (1991) Increased synthesis and accumulation of heat shock 70 proteins in Alzheimer's disease. Brain Res Mol Brain Res 11: 249-254.
    • (1991) Brain Res Mol Brain Res , vol.11 , pp. 249-254
    • Perez, N.1    Sugar, J.2    Charya, S.3    Johnson, G.4    Merril, C.5
  • 10
    • 0028136879 scopus 로고
    • Heat shock proteins protect against stress-related phosphorylation of tau in neuronal PC12 cells that have acquired thermotolerance
    • 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: 5687-5693.
    • (1994) J Neurosci , vol.14 , pp. 5687-5693
    • Kirby, B.A.1    Merril, C.R.2    Ghanbari, H.3    Wallace, W.C.4
  • 11
    • 0028109332 scopus 로고
    • YC-1, a novel activator of platelet guanylate cyclase
    • Ko FN, Wu CC, Kuo SC, Lee FY, Teng CM, (1994) YC-1, a novel activator of platelet guanylate cyclase. Blood 84: 4226-4233.
    • (1994) Blood , vol.84 , pp. 4226-4233
    • Ko, F.N.1    Wu, C.C.2    Kuo, S.C.3    Lee, F.Y.4    Teng, C.M.5
  • 12
    • 33748312096 scopus 로고    scopus 로고
    • NO-independent stimulators and activators of soluble guanylate cyclase: discovery and therapeutic potential
    • Evgenov OV, Pacher P, Schmidt PM, Haskó G, Schmidt HH, et al. (2006) NO-independent stimulators and activators of soluble guanylate cyclase: discovery and therapeutic potential. Nat Rev Drug Discov 5: 755-768.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 755-768
    • Evgenov, O.V.1    Pacher, P.2    Schmidt, P.M.3    Haskó, G.4    Schmidt, H.H.5
  • 13
    • 4444348385 scopus 로고    scopus 로고
    • Salutary properties of YC-1 in the cardiovascular and hematological systems
    • Tulis DA, (2004) Salutary properties of YC-1 in the cardiovascular and hematological systems. Curr Med Chem Cardiovasc Hematol Agents 2: 343-359.
    • (2004) Curr Med Chem Cardiovasc Hematol Agents , vol.2 , pp. 343-359
    • Tulis, D.A.1
  • 14
    • 52649137743 scopus 로고    scopus 로고
    • YC-1 induces heat shock protein 70 expression and prevents oxidized LDL-mediated apoptosis in vascular smooth muscle cells
    • Liu YN, Pan SL, Peng CY, Huang DY, Guh JH, et al. (2008) YC-1 induces heat shock protein 70 expression and prevents oxidized LDL-mediated apoptosis in vascular smooth muscle cells. Shock 30: 274-279.
    • (2008) Shock , vol.30 , pp. 274-279
    • Liu, Y.N.1    Pan, S.L.2    Peng, C.Y.3    Huang, D.Y.4    Guh, J.H.5
  • 15
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe DJ, (1999) Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399: A23-A31.
    • (1999) Nature , vol.399
    • Selkoe, D.J.1
  • 17
    • 0028118846 scopus 로고
    • Inhibition of PC 12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death
    • Shearman MS, Ragan CI, Iversen LL, (1994) Inhibition of PC 12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death. Proc Natl Acad Sci U S A 91: 1470-1474.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 18
    • 0034733220 scopus 로고    scopus 로고
    • Inhibitory effect of Artemisia asiatica alkaloids on acetyl-cholinesterase activity from rat PC12 cells
    • Heo HJ, Yang HC, Cho HY, Hong B, Lim ST, et al. (2000) Inhibitory effect of Artemisia asiatica alkaloids on acetyl-cholinesterase activity from rat PC12 cells. Mol Cells 10: 253-262.
    • (2000) Mol Cells , vol.10 , pp. 253-262
    • Heo, H.J.1    Yang, H.C.2    Cho, H.Y.3    Hong, B.4    Lim, S.T.5
  • 19
    • 33646050056 scopus 로고    scopus 로고
    • Heme oxygenase-1 contributes to the cytoprotection of alpha-lipoic acid via activation of p44/42 mitogen-activated protein kinase in vascular smooth muscle cells
    • Cheng PY, Lee YM, Shih NL, Chen YC, Yen MH, (2006) Heme oxygenase-1 contributes to the cytoprotection of alpha-lipoic acid via activation of p44/42 mitogen-activated protein kinase in vascular smooth muscle cells. Free Radic Biol Med 40: 1313-1322.
    • (2006) Free Radic Biol Med , vol.40 , pp. 1313-1322
    • Cheng, P.Y.1    Lee, Y.M.2    Shih, N.L.3    Chen, Y.C.4    Yen, M.H.5
  • 21
    • 0028986916 scopus 로고
    • Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding
    • Busciglio J, Lorenzo A, Yeh J, Yankner BA, (1995) Beta-amyloid fibrils induce tau phosphorylation and loss of microtubule binding. Neuron 14: 879-888.
    • (1995) Neuron , vol.14 , pp. 879-888
    • Busciglio, J.1    Lorenzo, A.2    Yeh, J.3    Yankner, B.A.4
  • 22
    • 0028980795 scopus 로고
    • Aminoterminal region of beta-amyloid precursor protein activates mitogenactivated protein kinase
    • Greenberg SM, Qiu WQ, Selkoe DJ, Ben-Itzhak A, Kosik KS, (1995) Aminoterminal region of beta-amyloid precursor protein activates mitogenactivated protein kinase. Neurosci Lett 198: 52-56.
    • (1995) Neurosci Lett , vol.198 , pp. 52-56
    • Greenberg, S.M.1    Qiu, W.Q.2    Selkoe, D.J.3    Ben-Itzhak, A.4    Kosik, K.S.5
  • 23
    • 0033957692 scopus 로고    scopus 로고
    • PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid inmature hippocampalneurons
    • Rapoport M, Ferreira A, (2000) PD98059 prevents neurite degeneration induced by fibrillar beta-amyloid inmature hippocampalneurons. J Neurochem 74: 125-133.
    • (2000) J Neurochem , vol.74 , pp. 125-133
    • Rapoport, M.1    Ferreira, A.2
  • 24
    • 0031695652 scopus 로고    scopus 로고
    • Activation of tau protein kinase I/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons
    • Takashima A, Honda T, Yasutake K, Michel G, Murayama O, et al. (1998) Activation of tau protein kinase I/glycogen synthase kinase-3beta by amyloid beta peptide (25-35) enhances phosphorylation of tau in hippocampal neurons. Neurosci Res 31: 317-323.
    • (1998) Neurosci Res , vol.31 , pp. 317-323
    • Takashima, A.1    Honda, T.2    Yasutake, K.3    Michel, G.4    Murayama, O.5
  • 25
    • 0037110601 scopus 로고    scopus 로고
    • Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures
    • Zheng WH, Bastianetto S, Mennicken F, Ma W, Kar S, (2002) Amyloid beta peptide induces tau phosphorylation and loss of cholinergic neurons in rat primary septal cultures. Neuroscience 115: 201-211.
    • (2002) Neuroscience , vol.115 , pp. 201-211
    • Zheng, W.H.1    Bastianetto, S.2    Mennicken, F.3    Ma, W.4    Kar, S.5
  • 26
    • 0037070606 scopus 로고    scopus 로고
    • Direct interaction of soluble human recombinant Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II
    • Rank KB, Pauley AM, Bhattacharya K, Wang Z, Evans DB, et al. (2002) Direct interaction of soluble human recombinant Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II. FEBS Lett 514: 263-268.
    • (2002) FEBS Lett , vol.514 , pp. 263-268
    • Rank, K.B.1    Pauley, A.M.2    Bhattacharya, K.3    Wang, Z.4    Evans, D.B.5
  • 27
    • 34248222732 scopus 로고    scopus 로고
    • Inverse and distinct modulation of tau-dependent neurodegeneration by presenilin 1 and amyloid-beta in cultured cortical neurons: evidence that tau phosphorylation is the limiting factor in amyloid-beta-induced cell death
    • Leschik J, Welzel A, Weissmann C, Eckert A, Brandt R, (2007) Inverse and distinct modulation of tau-dependent neurodegeneration by presenilin 1 and amyloid-beta in cultured cortical neurons: evidence that tau phosphorylation is the limiting factor in amyloid-beta-induced cell death. J Neurochem 101: 1303-1315.
    • (2007) J Neurochem , vol.101 , pp. 1303-1315
    • Leschik, J.1    Welzel, A.2    Weissmann, C.3    Eckert, A.4    Brandt, R.5
  • 28
    • 33744818219 scopus 로고    scopus 로고
    • Assessments of the accumulation severities of amyloid beta-protein and hyperphosphorylated tau in the medial temporal cortex of control and Alzheimer's brains
    • Zhou XW, Li X, Bjorkdahl C, Sjogren MJ, Alafuzoff I, et al. (2006) Assessments of the accumulation severities of amyloid beta-protein and hyperphosphorylated tau in the medial temporal cortex of control and Alzheimer's brains. Neurobiol Dis 22: 657-668.
    • (2006) Neurobiol Dis , vol.22 , pp. 657-668
    • Zhou, X.W.1    Li, X.2    Bjorkdahl, C.3    Sjogren, M.J.4    Alafuzoff, I.5
  • 29
    • 27844553889 scopus 로고    scopus 로고
    • Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain
    • Liu F, Grundke-Iqbal I, Iqbal K, Oda Y, Tomizawa K, et al. (2005) Truncation and activation of calcineurin A by calpain I in Alzheimer disease brain. J Biol Chem 280: 37755-37762.
    • (2005) J Biol Chem , vol.280 , pp. 37755-37762
    • Liu, F.1    Grundke-Iqbal, I.2    Iqbal, K.3    Oda, Y.4    Tomizawa, K.5
  • 30
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration
    • Saito K, Elce JS, Hamos JE, Nixon RA, (1993) Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc Natl Acad Sci U S A 90: 2628-2632.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 31
    • 0032577543 scopus 로고    scopus 로고
    • m-Calpain (calcium- activated neutral proteinase) in Alzheimer's disease brains
    • Tsuji T, Shimohama S, Kimura J, Shimizu K, (1998) m-Calpain (calcium- activated neutral proteinase) in Alzheimer's disease brains. Neurosci Lett 248: 109-112.
    • (1998) Neurosci Lett , vol.248 , pp. 109-112
    • Tsuji, T.1    Shimohama, S.2    Kimura, J.3    Shimizu, K.4
  • 32
    • 16244410153 scopus 로고    scopus 로고
    • Mu-calpain is functionally required for alpha-processing of Alzheimer's beta-amyloid precursor protein
    • Chen M, Fernandez HL, (2005) Mu-calpain is functionally required for alpha-processing of Alzheimer's beta-amyloid precursor protein. Biochem Biophys Res Commun 330: 714-721.
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 714-721
    • Chen, M.1    Fernandez, H.L.2
  • 33
    • 33644853371 scopus 로고    scopus 로고
    • Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3
    • Fifre A, Sponne I, Koziel V, Kriem B, Yen Potin FT, et al. (2006) Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3. J Biol Chem 281: 229-240.
    • (2006) J Biol Chem , vol.281 , pp. 229-240
    • Fifre, A.1    Sponne, I.2    Koziel, V.3    Kriem, B.4    Yen Potin, F.T.5
  • 34
    • 0034682414 scopus 로고    scopus 로고
    • Neurotoxicity induces cleavage of p35 to p25 by calpain
    • Lee MS, Kwon YT, Li M, Peng J, Friedlander RM, et al. (2000) Neurotoxicity induces cleavage of p35 to p25 by calpain. Nature 405: 360-364.
    • (2000) Nature , vol.405 , pp. 360-364
    • Lee, M.S.1    Kwon, Y.T.2    Li, M.3    Peng, J.4    Friedlander, R.M.5
  • 35
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • Park SY, Ferreira A, (2005) The generation of a 17 kDa neurotoxic fragment: an alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci 25: 5365-5375.
    • (2005) J Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 36
    • 0033540060 scopus 로고    scopus 로고
    • Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration
    • Patrick GN, Zukerberg L, Nikolic M, de la Monte S, Dikkes P, et al. (1999) Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration. Nature 402: 615-622.
    • (1999) Nature , vol.402 , pp. 615-622
    • Patrick, G.N.1    Zukerberg, L.2    Nikolic, M.3    de la Monte, S.4    Dikkes, P.5
  • 37
    • 3542995049 scopus 로고    scopus 로고
    • Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection
    • Morimoto RI, Santoro MG, (1998) Stress-inducible responses and heat shock proteins: new pharmacologic targets for cytoprotection. Nat Biotechnol 16: 833-838.
    • (1998) Nat Biotechnol , vol.16 , pp. 833-838
    • Morimoto, R.I.1    Santoro, M.G.2
  • 39
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J, (2001) Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70: 603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 40
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL, (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6: 11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 41
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman MY, Goldberg AL, (2001) Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29: 15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 42
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock protein 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro
    • Evans CG, Wisén S, Gestwicki JE, (2006) Heat shock protein 70 and 90 inhibit early stages of amyloid β-(1-42) aggregation in vitro. J Biol Chem 281: 33182-33191.
    • (2006) J Biol Chem , vol.281 , pp. 33182-33191
    • Evans, C.G.1    Wisén, S.2    Gestwicki, J.E.3


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