메뉴 건너뛰기




Volumn 19, Issue 11, 1999, Pages 4360-4369

Neuroprotection at Drosophila synapses conferred by prior heat shock

Author keywords

Drosophila; Heat hock proteins; Neuromuscular; Postsynaptic; Presynaptic; Quanta; Thermal stress

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 0033151567     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-11-04360.1999     Document Type: Article
Times cited : (93)

References (50)
  • 1
    • 0026731880 scopus 로고
    • Evidence for reversible non-microtubule and non-microfilament dependent nuclear translocation of hsp90 after heat shock in human fibroblasts
    • Akner G, Mossberg K, Sundqvist KG, Gustafsson JA, Wikstrom AC (1992) Evidence for reversible non-microtubule and non-microfilament dependent nuclear translocation of hsp90 after heat shock in human fibroblasts. Eur J Cell Biol 58:356-364.
    • (1992) Eur J Cell Biol , vol.58 , pp. 356-364
    • Akner, G.1    Mossberg, K.2    Sundqvist, K.G.3    Gustafsson, J.A.4    Wikstrom, A.C.5
  • 2
    • 0027325492 scopus 로고
    • Differential ultrastructure of synaptic terminals on ventral longitudinal abdominal muscles in Drosophila larvae
    • Atwood HL, Govind CK, Wu C-F (1993) Differential ultrastructure of synaptic terminals on ventral longitudinal abdominal muscles in Drosophila larvae. J Neurobiol 24:1008-1024.
    • (1993) J Neurobiol , vol.24 , pp. 1008-1024
    • Atwood, H.L.1    Govind, C.K.2    Wu, C.-F.3
  • 3
    • 0023732689 scopus 로고
    • Hyperthermia protects against light damage in the rat retina
    • Barbe MF, Tytell M, Gower DJ, Welch WJ (1988) Hyperthermia protects against light damage in the rat retina. Science 241:1817-1820.
    • (1988) Science , vol.241 , pp. 1817-1820
    • Barbe, M.F.1    Tytell, M.2    Gower, D.J.3    Welch, W.J.4
  • 5
    • 0031465969 scopus 로고    scopus 로고
    • The molecular chaperone function of the secretory vesicle cysteine string proteins
    • Chamberlain LH, Burgoyne RD (1997a) The molecular chaperone function of the secretory vesicle cysteine string proteins. J Biol Chem 272:31420-31426.
    • (1997) J Biol Chem , vol.272 , pp. 31420-31426
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 6
    • 0030991023 scopus 로고    scopus 로고
    • Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein
    • Chamberlain LH, Burgoyne RD (1997b) Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein. Biochem J 322:853-858.
    • (1997) Biochem J , vol.322 , pp. 853-858
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 7
    • 0020647615 scopus 로고
    • Effects of low temperature and terminal membrane potential on quantal size at frog neuromuscular junction
    • Cohen IS, Van der Kloot W (1983) Effects of low temperature and terminal membrane potential on quantal size at frog neuromuscular junction. J Physiol (Lond) 336:335-344.
    • (1983) J Physiol (Lond) , vol.336 , pp. 335-344
    • Cohen, I.S.1    Van Der Kloot, W.2
  • 8
    • 0028806102 scopus 로고
    • Quantal measurement and analysis methods compared for crayfish and Drosophila neuromuscular junctions, and rat hippocampus
    • Cooper RL, Stewart BA, Wojtowicz JM, Wang S, Atwood HL (1995) Quantal measurement and analysis methods compared for crayfish and Drosophila neuromuscular junctions, and rat hippocampus. J Neurosci Methods 61:67-78.
    • (1995) J Neurosci Methods , vol.61 , pp. 67-78
    • Cooper, R.L.1    Stewart, B.A.2    Wojtowicz, J.M.3    Wang, S.4    Atwood, H.L.5
  • 9
    • 0032479938 scopus 로고    scopus 로고
    • Heat shock protects synaptic transmission in flight motor circuitry of locusts
    • Dawson-Scully K, Robertson RM (1998) Heat shock protects synaptic transmission in flight motor circuitry of locusts. NeuroReport 9:2589-2593.
    • (1998) NeuroReport , vol.9 , pp. 2589-2593
    • Dawson-Scully, K.1    Robertson, R.M.2
  • 10
    • 0019504744 scopus 로고
    • The effect of reduced calcium on quantal unit current and release at the crayfish neuromuscular junction
    • Dudel J (1981) The effect of reduced calcium on quantal unit current and release at the crayfish neuromuscular junction. Pflügers Arch 391:35-40.
    • (1981) Pflügers Arch , vol.391 , pp. 35-40
    • Dudel, J.1
  • 11
    • 0030634892 scopus 로고    scopus 로고
    • Ecological and evolutionary physiology of heat shock proteins and the stress response in Drosophila: Complementary insights from genetic engineering and natural variation
    • (Bijlsma R, Loeschoke V, eds), Basel: Birkhäuser
    • Feder ME, Krebs RA (1997) Ecological and evolutionary physiology of heat shock proteins and the stress response in Drosophila: complementary insights from genetic engineering and natural variation. In: Environmental stress, adaptation and evolution (Bijlsma R, Loeschoke V, eds), pp 155-173. Basel: Birkhäuser.
    • (1997) Environmental Stress, Adaptation and Evolution , pp. 155-173
    • Feder, M.E.1    Krebs, R.A.2
  • 12
    • 0004581102 scopus 로고    scopus 로고
    • Natural and genetic engineering of the heat-shock protein Hsp70 in Drosophila melanogaster: Consequences for thermotolerance
    • Feder ME, Krebs RA (1998) Natural and genetic engineering of the heat-shock protein Hsp70 in Drosophila melanogaster: consequences for thermotolerance. Am Zool 38:503-517.
    • (1998) Am Zool , vol.38 , pp. 503-517
    • Feder, M.E.1    Krebs, R.A.2
  • 13
    • 0030217968 scopus 로고    scopus 로고
    • Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster
    • Feder ME, Cartaño NV, Milos L, Krebs RA, Lindquist SL (1996) Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster. J Exp Biol 199:1837-1844.
    • (1996) J Exp Biol , vol.199 , pp. 1837-1844
    • Feder, M.E.1    Cartaño, N.V.2    Milos, L.3    Krebs, R.A.4    Lindquist, S.L.5
  • 14
    • 0031020041 scopus 로고    scopus 로고
    • Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock
    • Fink SL, Chang LK, Ho DY, Sapolsky RM (1997) Defective herpes simplex virus vectors expressing the rat brain stress-inducible heat shock protein 72 protect cultured neurons from severe heat shock. J Neurochem 68:961-969.
    • (1997) J Neurochem , vol.68 , pp. 961-969
    • Fink, S.L.1    Chang, L.K.2    Ho, D.Y.3    Sapolsky, R.M.4
  • 15
    • 0019470237 scopus 로고
    • Selective effects of LSD and hyperthermia on the synthesis of synaptic proteins and glycoproteins
    • Freedman MS, Clark BD, Cruz TF, Gurd JW, Brown IR (1981) Selective effects of LSD and hyperthermia on the synthesis of synaptic proteins and glycoproteins. Brain Res 207:129-145.
    • (1981) Brain Res , vol.207 , pp. 129-145
    • Freedman, M.S.1    Clark, B.D.2    Cruz, T.F.3    Gurd, J.W.4    Brown, I.R.5
  • 16
    • 0031853114 scopus 로고    scopus 로고
    • Effects of heat stress on axonal conduction in the locust flight system
    • in press
    • Gray JR, Robertson RM (1999) Effects of heat stress on axonal conduction in the locust flight system. Comp Biochem Physiol [A], in press.
    • (1999) Comp Biochem Physiol [A]
    • Gray, J.R.1    Robertson, R.M.2
  • 17
    • 0029081932 scopus 로고
    • Recordings of glutamate-gated ion channels in outside-out patches from Drosophila larval muscle
    • Heckmann M, Dudel J (1995) Recordings of glutamate-gated ion channels in outside-out patches from Drosophila larval muscle. Neurosci Lett 196:53-56.
    • (1995) Neurosci Lett , vol.196 , pp. 53-56
    • Heckmann, M.1    Dudel, J.2
  • 18
    • 0030979135 scopus 로고    scopus 로고
    • Desensitization and resensitization kinetics of glutamate receptor channels from Drosophila larval muscle
    • Heckmann M, Dudel J (1997) Desensitization and resensitization kinetics of glutamate receptor channels from Drosophila larval muscle. Biophys J 72:2160-2169.
    • (1997) Biophys J , vol.72 , pp. 2160-2169
    • Heckmann, M.1    Dudel, J.2
  • 19
    • 0030953092 scopus 로고    scopus 로고
    • Evoked transmitter release at neuromuscular junctions in wild type and cysteine string protein null mutant larvae of Drosophila
    • Heckmann M, Adelsberger H, Dudel J (1997) Evoked transmitter release at neuromuscular junctions in wild type and cysteine string protein null mutant larvae of Drosophila. Neurosci Lett 228:167-170.
    • (1997) Neurosci Lett , vol.228 , pp. 167-170
    • Heckmann, M.1    Adelsberger, H.2    Dudel, J.3
  • 20
    • 0028842612 scopus 로고
    • Statistics of quantal secretion during long trains of sympathetic nerve impulses in mouse vas deferens
    • Karunanithi S, Phipps MC, Robinson J, Bennett MR (1995) Statistics of quantal secretion during long trains of sympathetic nerve impulses in mouse vas deferens. J Physiol (Lond) 489:171-181.
    • (1995) J Physiol (Lond) , vol.489 , pp. 171-181
    • Karunanithi, S.1    Phipps, M.C.2    Robinson, J.3    Bennett, M.R.4
  • 21
    • 0029926999 scopus 로고    scopus 로고
    • The Drosophila neuromuscular junction: A model system for studying synaptic development and function
    • Keshishian H, Broadie K, Chiba A, Bate M (1996) The Drosophila neuromuscular junction: a model system for studying synaptic development and function. Annu Rev Neurosci 19:545-575.
    • (1996) Annu Rev Neurosci , vol.19 , pp. 545-575
    • Keshishian, H.1    Broadie, K.2    Chiba, A.3    Bate, M.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the heat of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the heat of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0026768860 scopus 로고
    • Probabilistic secretion of quanta from visualized sympathetic nerve varicosities in mouse vas deferens
    • Lavidis NA, Bennett MR (1992) Probabilistic secretion of quanta from visualized sympathetic nerve varicosities in mouse vas deferens. J Physiol (Lond) 454:9-26.
    • (1992) J Physiol (Lond) , vol.454 , pp. 9-26
    • Lavidis, N.A.1    Bennett, M.R.2
  • 24
    • 0026328490 scopus 로고
    • The stress protein response in cultured neurons: Characterization and evidence for a protective role in excitotoxicity
    • Lowenstein DH, Chan PH, Miles MF (1991) The stress protein response in cultured neurons: characterization and evidence for a protective role in excitotoxicity. Neuron 7:1053-1060.
    • (1991) Neuron , vol.7 , pp. 1053-1060
    • Lowenstein, D.H.1    Chan, P.H.2    Miles, M.F.3
  • 25
    • 0027260315 scopus 로고
    • Heat shock protects neuronal cells from programmed cell death by apoptosis
    • Mailhos C, Howard MK, Latchman DS (1993) Heat shock protects neuronal cells from programmed cell death by apoptosis. Neuroscience 55:621-627.
    • (1993) Neuroscience , vol.55 , pp. 621-627
    • Mailhos, C.1    Howard, M.K.2    Latchman, D.S.3
  • 26
    • 0026110318 scopus 로고
    • Nerve terminal excitability and neuromuscular transmission in T(X;Y)V7 and Shaker mutants of Drosophila melanogaster
    • Mallart A, Angaut-Petit D, Bourret-Poulain C, Ferrus A (1991) Nerve terminal excitability and neuromuscular transmission in T(X;Y)V7 and Shaker mutants of Drosophila melanogaster. J Neurogenet 7:75-84.
    • (1991) J Neurogenet , vol.7 , pp. 75-84
    • Mallart, A.1    Angaut-Petit, D.2    Bourret-Poulain, C.3    Ferrus, A.4
  • 29
    • 0001824746 scopus 로고
    • Progress and perspectives on the biology of heat shock proteins and molecular chaperones
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
    • Morimoto RI, Tissiers A, Georgopoulos C (1994) Progress and perspectives on the biology of heat shock proteins and molecular chaperones. In: The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones
    • Morimoto, R.I.1    Tissiers, A.2    Georgopoulos, C.3
  • 30
    • 0027135501 scopus 로고
    • The function of heat-shock proteins in stress tolerance: Degradation and reactivation of damaged proteins
    • Parsell DA, Lindquist S (1993) The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annu Rev Genet 27:437-496.
    • (1993) Annu Rev Genet , vol.27 , pp. 437-496
    • Parsell, D.A.1    Lindquist, S.2
  • 31
    • 0031916186 scopus 로고    scopus 로고
    • Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling
    • Ranjan R, Bronk P, Zinsmaier KE (1998) Cysteine string protein is required for calcium secretion coupling of evoked neurotransmission in Drosophila but not for vesicle recycling. J Neurosci 18:956-964.
    • (1998) J Neurosci , vol.18 , pp. 956-964
    • Ranjan, R.1    Bronk, P.2    Zinsmaier, K.E.3
  • 32
    • 0347011021 scopus 로고
    • Molecular and genetic approaches to neurotransmitter and neuromodulator systems in Drosophila
    • Restifo LL, White K (1990) Molecular and genetic approaches to neurotransmitter and neuromodulator systems in Drosophila. Adv Insect Physiol 22:115-218.
    • (1990) Adv Insect Physiol , vol.22 , pp. 115-218
    • Restifo, L.L.1    White, K.2
  • 33
    • 34250561475 scopus 로고
    • A new puffing pattern induced by a temperature shock and DNP in Drosophila
    • Ritossa FM (1962) A new puffing pattern induced by a temperature shock and DNP in Drosophila. Experientia 18:571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.M.1
  • 34
    • 0030025688 scopus 로고    scopus 로고
    • Exposure to heat shock affects thermosensitivity of the locust flight system
    • Robertson RM, Xu H, Shoemaker KL, Dawson-Scully K (1996) Exposure to heat shock affects thermosensitivity of the locust flight system. J Neurobiol 29:367-383.
    • (1996) J Neurobiol , vol.29 , pp. 367-383
    • Robertson, R.M.1    Xu, H.2    Shoemaker, K.L.3    Dawson-Scully, K.4
  • 35
    • 0026336621 scopus 로고
    • Heat shock protects culture neurons from glutamate toxicity
    • Rordorf G, Koroshetz WJ, Bonventre JV (1991) Heat shock protects culture neurons from glutamate toxicity. Neuron 7:1043-1051.
    • (1991) Neuron , vol.7 , pp. 1043-1051
    • Rordorf, G.1    Koroshetz, W.J.2    Bonventre, J.V.3
  • 36
    • 0024502083 scopus 로고
    • Amplitude fluctuations in small EPSPs recorded from CAl pyramidal cells in guinea pig hippocampal slice
    • Sayer RJ, Redman SJ, Andersen P (1989) Amplitude fluctuations in small EPSPs recorded from CAl pyramidal cells in guinea pig hippocampal slice. J Neurosci 9:840-850.
    • (1989) J Neurosci , vol.9 , pp. 840-850
    • Sayer, R.J.1    Redman, S.J.2    Andersen, P.3
  • 37
    • 0032557826 scopus 로고    scopus 로고
    • Heat-shock proteins in axoplasm: High constitutive levels and transfer of inducible isoforms from glia
    • Sheller RA, Smyers ME, Grossfeld RM, Ballinger ML, Bittner GD (1998) Heat-shock proteins in axoplasm: high constitutive levels and transfer of inducible isoforms from glia. J Comp Neurol 396:1-11.
    • (1998) J Comp Neurol , vol.396 , pp. 1-11
    • Sheller, R.A.1    Smyers, M.E.2    Grossfeld, R.M.3    Ballinger, M.L.4    Bittner, G.D.5
  • 38
    • 0028483237 scopus 로고
    • Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions
    • Stewart BA, Atwood HL, Renger JJ, Wang J, WuC-F (1994) Improved stability of Drosophila larval neuromuscular preparations in haemolymph-like physiological solutions. J Comp Physiol [A] 175:179-191.
    • (1994) J Comp Physiol [A] , vol.175 , pp. 179-191
    • Stewart, B.A.1    Atwood, H.L.2    Renger, J.J.3    Wang, J.4    Wu, C.-F.5
  • 39
    • 0029948786 scopus 로고    scopus 로고
    • Homeostasis of synaptic transmission in Drosophila with genetically altered nerve terminal morphology
    • Stewart BA, Schuster CM, Goodman CS, Atwood HL (1996) Homeostasis of synaptic transmission in Drosophila with genetically altered nerve terminal morphology. J Neurosci 16:3877-3886.
    • (1996) J Neurosci , vol.16 , pp. 3877-3886
    • Stewart, B.A.1    Schuster, C.M.2    Goodman, C.S.3    Atwood, H.L.4
  • 40
    • 0028345107 scopus 로고
    • Induction of heat shock (stress) protein 70 and its mRNA in the normal and light-damaged retina after whole body hyperthermia
    • Tytell M, Barbe MF, Brown IR (1994) Induction of heat shock (stress) protein 70 and its mRNA in the normal and light-damaged retina after whole body hyperthermia. J Neurosci Res 38:19-31.
    • (1994) J Neurosci Res , vol.38 , pp. 19-31
    • Tytell, M.1    Barbe, M.F.2    Brown, I.R.3
  • 42
    • 0032080204 scopus 로고    scopus 로고
    • Attenuated influx of calcium ions at nerve endings of csp and shibire mutant Drosophila
    • Umbach JA, Saitoe M, Kidokoro Y, Gundersen CB (1998) Attenuated influx of calcium ions at nerve endings of csp and shibire mutant Drosophila. J Neurosci 18:3233-3240.
    • (1998) J Neurosci , vol.18 , pp. 3233-3240
    • Umbach, J.A.1    Saitoe, M.2    Kidokoro, Y.3    Gundersen, C.B.4
  • 43
    • 0032240732 scopus 로고    scopus 로고
    • Development of the quantal properties of evoked and spontaneous synaptic currents at a brain synapse
    • Wall MJ, Usowicz MM (1998) Development of the quantal properties of evoked and spontaneous synaptic currents at a brain synapse. Natu Neurosci 1:675-682.
    • (1998) Natu Neurosci , vol.1 , pp. 675-682
    • Wall, M.J.1    Usowicz, M.M.2
  • 44
    • 0023270857 scopus 로고
    • Heat shock and thermotolerance during early rat embryo development
    • Walsh DA, Klein NW, Hightower LE, Edwards MJ (1987) Heat shock and thermotolerance during early rat embryo development. Teratology 36:181-191.
    • (1987) Teratology , vol.36 , pp. 181-191
    • Walsh, D.A.1    Klein, N.W.2    Hightower, L.E.3    Edwards, M.J.4
  • 45
    • 0024424910 scopus 로고
    • Regulation of the inducible heat shock 71 genes in early neural development of cultured rat embryos
    • Walsh DA, Li K, Speirs J, Crowther CE, Edwards MJ (1989) Regulation of the inducible heat shock 71 genes in early neural development of cultured rat embryos. Teratology 40:321-334.
    • (1989) Teratology , vol.40 , pp. 321-334
    • Walsh, D.A.1    Li, K.2    Speirs, J.3    Crowther, C.E.4    Edwards, M.J.5
  • 47
    • 0026418319 scopus 로고
    • Regulation of kainate receptors by cAMP-dependent protein kinase and phosphatases
    • Wang L-Y, Salter MW, MacDonald JF (1991) Regulation of kainate receptors by cAMP-dependent protein kinase and phosphatases. Science 253:1132-1135.
    • (1991) Science , vol.253 , pp. 1132-1135
    • Wang, L.-Y.1    Salter, M.W.2    MacDonald, J.F.3
  • 48
    • 0027407112 scopus 로고
    • Phosphorylation and modulation of a kainate receptor (GluR6) by cAMP-dependent protein kinase
    • Wang L-Y, Taverna FA, Huang X-P, MacDonald JF, Hampson DR (1993) Phosphorylation and modulation of a kainate receptor (GluR6) by cAMP-dependent protein kinase. Science 259:1173-1175.
    • (1993) Science , vol.259 , pp. 1173-1175
    • Wang, L.-Y.1    Taverna, F.A.2    Huang, X.-P.3    MacDonald, J.F.4    Hampson, D.R.5
  • 49
    • 0011873030 scopus 로고    scopus 로고
    • The possible origin of variability in miniature PSC amplitude in cultured amacrine neurons
    • (Faber DS, Korn H, Redman SJ, Thompson SM, Altman JS, eds), Strasbourg, France: Human Frontier Science Program
    • Wilson M, Frerking M (1998) The possible origin of variability in miniature PSC amplitude in cultured amacrine neurons. In: Central synapses: quantal mechanisms and plasticity (Faber DS, Korn H, Redman SJ, Thompson SM, Altman JS, eds), pp 99-108. Strasbourg, France: Human Frontier Science Program.
    • (1998) Central Synapses: Quantal Mechanisms and Plasticity , pp. 99-108
    • Wilson, M.1    Frerking, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.