메뉴 건너뛰기




Volumn 84, Issue 3, 2003, Pages 514-521

Alterations in inducible 72-kDa heat shock protein and the chaperone cofactor BAG-1 in human brain after head injury

Author keywords

Apoptosis; Bcl 2; Head injury; Hsc70; Hsp70; Trauma

Indexed keywords

BAG 1 PROTEIN; CHAPERONE; HEAT SHOCK COGNATE PROTEIN 70; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; PROTEIN BCL 2; UNCLASSIFIED DRUG;

EID: 0037316678     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01547.x     Document Type: Article
Times cited : (37)

References (52)
  • 1
    • 0033963212 scopus 로고    scopus 로고
    • Localization of heat-shock protein Hsp70 to the synapse following hyperthermic stress in brain
    • Bechtold D. A., Rush S. J. and Brown I. R. (2000) Localization of heat-shock protein Hsp70 to the synapse following hyperthermic stress in brain. J. Neurochem. 74, 641-646.
    • (2000) J. Neurochem. , vol.74 , pp. 641-646
    • Bechtold, D.A.1    Rush, S.J.2    Brown, I.R.3
  • 2
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann R. P., Mizzen L. E. and Welch W. J. (1990) Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 3
    • 0024677259 scopus 로고
    • Induction of a heat shock gene at the site of tissue injury in the rat brain
    • Brown I. R., Rush S. and Ivy G. O. (1989) Induction of a heat shock gene at the site of tissue injury in the rat brain. Neuron 2, 1559-1564.
    • (1989) Neuron , vol.2 , pp. 1559-1564
    • Brown, I.R.1    Rush, S.2    Ivy, G.O.3
  • 5
    • 0027218599 scopus 로고
    • Heat shock proteins in relation to medicine
    • Burdon R. H. (1993) Heat shock proteins in relation to medicine. Mol. Aspects Med. 14, 83-165.
    • (1993) Mol. Aspects Med. , vol.14 , pp. 83-165
    • Burdon, R.H.1
  • 6
    • 0032993870 scopus 로고    scopus 로고
    • Protection against necrosis but not apoptosis by heat-stress proteins in vascular smooth muscle cells: Evidence for distinct modes of cell death
    • Champagne M. J., Dumas P., Orlov S. N., Bennett M. R., Hamet P. and Tremblay J. (1999) Protection against necrosis but not apoptosis by heat-stress proteins in vascular smooth muscle cells: evidence for distinct modes of cell death. Hypertension 33, 906-913.
    • (1999) Hypertension , vol.33 , pp. 906-913
    • Champagne, M.J.1    Dumas, P.2    Orlov, S.N.3    Bennett, M.R.4    Hamet, P.5    Tremblay, J.6
  • 7
    • 0027196609 scopus 로고
    • Temperature modulation of cerebral depolarization during focal cerebral ischemia in rats: Correlation with ischemic injury
    • Chen Q., Chopp M., Bodzin G. and Chen H. (1993) Temperature modulation of cerebral depolarization during focal cerebral ischemia in rats: Correlation with ischemic injury. J. Cereb. Blood Flow Metab. 13, 389-394.
    • (1993) J. Cereb. Blood Flow Metab. , vol.13 , pp. 389-394
    • Chen, Q.1    Chopp, M.2    Bodzin, G.3    Chen, H.4
  • 10
    • 0031744415 scopus 로고    scopus 로고
    • Patterns of heat-shock protein 70 biosynthesis following human traumatic brain injury
    • Dutcher S. A., Underwood B. D., Walker P. D., Diaz F. G. and Michael D. B. (1998a) Patterns of heat-shock protein 70 biosynthesis following human traumatic brain injury. J. Neurotrauma 15, 411-420.
    • (1998) J. Neurotrauma , vol.15 , pp. 411-420
    • Dutcher, S.A.1    Underwood, B.D.2    Walker, P.D.3    Diaz, F.G.4    Michael, D.B.5
  • 11
    • 0031798954 scopus 로고    scopus 로고
    • Heat-shock protein 72 expression in excitotoxic versus penetrating injuries of the rodent cerebral cortex
    • Dutcher S. A., Underwood B. D., Michael D. B., Diaz F. G. and Walker P. D. (1998b) Heat-shock protein 72 expression in excitotoxic versus penetrating injuries of the rodent cerebral cortex. J. Neurotrauma 15, 421-432.
    • (1998) J. Neurotrauma , vol.15 , pp. 421-432
    • Dutcher, S.A.1    Underwood, B.D.2    Michael, D.B.3    Diaz, F.G.4    Walker, P.D.5
  • 12
    • 0024365739 scopus 로고
    • The role of excitatory amino acids and NMDA receptors in traumatic brain injury
    • Faden A. I., Demediuk P., Panter S. S. and Vink R. (1989) The role of excitatory amino acids and NMDA receptors in traumatic brain injury. Science 244, 798-800.
    • (1989) Science , vol.244 , pp. 798-800
    • Faden, A.I.1    Demediuk, P.2    Panter, S.S.3    Vink, R.4
  • 13
    • 0029954682 scopus 로고    scopus 로고
    • Heat shock protein 70 suppresses astroglial-inducible nitric-oxide synthase expression by decreasing NFkappaB activation
    • Feinstein D. L., Galea E., Aquino D. A., Li G. C., Xu H. and Reis D. J. (1996) Heat shock protein 70 suppresses astroglial-inducible nitric-oxide synthase expression by decreasing NFkappaB activation. J. Biol. Chem. 271, 17724-17732.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17724-17732
    • Feinstein, D.L.1    Galea, E.2    Aquino, D.A.3    Li, G.C.4    Xu, H.5    Reis, D.J.6
  • 14
    • 0032496242 scopus 로고    scopus 로고
    • BAG-1L protein enhances androgen receptor function
    • Froesch B. A., Takayama S. and Reed J. C. (1998) BAG-1L protein enhances androgen receptor function. J. Biol. Chem. 273, 11660-11666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11660-11666
    • Froesch, B.A.1    Takayama, S.2    Reed, J.C.3
  • 16
    • 0027298139 scopus 로고
    • Disturbances of cerebral protein synthesis and ischemic cell death
    • Hossmann K. A. (1993) Disturbances of cerebral protein synthesis and ischemic cell death. Prog. Brain Res. 96, 161-177.
    • (1993) Prog. Brain Res. , vol.96 , pp. 161-177
    • Hossmann, K.A.1
  • 17
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • Jaattela M., Wissing D., Bauer P. A. and Li G. C. (1992) Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity. EMBO J. 11, 3507-3512.
    • (1992) EMBO J. , vol.11 , pp. 3507-3512
    • Jaattela, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 18
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P. J., Ostermann J., Shilling J., Neupert W., Craig E. A. and Pfanner N. (1990) Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 348, 137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 19
    • 0026560855 scopus 로고
    • Expression of stress-response (heat-shock) protein 27 in human brain tumors: An immunohistochemical study
    • Kato M., Herz F., Kato S. and Hirano A. (1992) Expression of stress-response (heat-shock) protein 27 in human brain tumors: an immunohistochemical study. Acta Neuropathol. 83, 420-422.
    • (1992) Acta Neuropathol. , vol.83 , pp. 420-422
    • Kato, M.1    Herz, F.2    Kato, S.3    Hirano, A.4
  • 20
    • 0033574789 scopus 로고    scopus 로고
    • Control of mRNA decay by heat shock-ubiquitin-proteasome pathway
    • Laroia G., Cuesta R., Brewer G. and Schneider R. J. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284, 499-502.
    • (1999) Science , vol.284 , pp. 499-502
    • Laroia, G.1    Cuesta, R.2    Brewer, G.3    Schneider, R.J.4
  • 21
    • 0020130877 scopus 로고
    • Correlation between synthesis of heat shock proteins and development of themotolerance in Chinese hamster fibroblasts
    • Li G. C. and Werb Z. (1982) Correlation between synthesis of heat shock proteins and development of themotolerance in Chinese hamster fibroblasts. Proc. Natl Acad. Sci. USA 79, 3218-3222.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3218-3222
    • Li, G.C.1    Werb, Z.2
  • 22
    • 0026632673 scopus 로고
    • Distribution of 72-kDa heat-shock protein in rat brain after hyperthermia
    • Li Y., Chopp M., Yoshida Y. and Levine S. R. (1992) Distribution of 72-kDa heat-shock protein in rat brain after hyperthermia. Acta Neuropathol. 84, 94-99.
    • (1992) Acta Neuropathol. , vol.84 , pp. 94-99
    • Li, Y.1    Chopp, M.2    Yoshida, Y.3    Levine, S.R.4
  • 23
    • 0022555843 scopus 로고
    • The heat-shock response
    • Lindquist S. (1986) The heat-shock response. Annu. Rev. Biochem. 55, 1151-1191.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 1151-1191
    • Lindquist, S.1
  • 24
    • 0032532127 scopus 로고    scopus 로고
    • HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status
    • Ling J., Wells D. R., Tanguay R. L., Dickey L. F., Thompson W. F. and Gallie D. R. (1998) HSP101 functions as a specific translational regulatory protein whose activity is regulated by nutrient status. Genes Dev. 12, 3236-3251.
    • (1998) Genes Dev. , vol.12 , pp. 3236-3251
    • Ling, J.1    Wells, D.R.2    Tanguay, R.L.3    Dickey, L.F.4    Thompson, W.F.5    Gallie, D.R.6
  • 25
    • 0026328490 scopus 로고
    • The stress protein response in cultured neurons: Characterization and evidence for a protective role in excitotoxicity
    • Lowenstein D. H., Chan P. H. and Miles M. F. (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
  • 26
    • 0028044860 scopus 로고
    • Increased expression of mRNA encoding calbindin-D28K, the glucose-brain regulated proteins, or the 72 kDa heat-shock protein in three models of acute CNS injury
    • Lowenstein D. H., Gwinn R. P., Seren M. S., Simon R. P. and McIntosh T. K. (1994) Increased expression of mRNA encoding calbindin-D28K, the glucose-brain regulated proteins, or the 72 kDa heat-shock protein in three models of acute CNS injury. Res. Mol. Brain Res. 22, 299-308.
    • (1994) Res. Mol. Brain Res. , vol.22 , pp. 299-308
    • Lowenstein, D.H.1    Gwinn, R.P.2    Seren, M.S.3    Simon, R.P.4    McIntosh, T.K.5
  • 27
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/ Hsp70 and the proteasome
    • Luders J., Demand J. and Hohfeld J. (2000a) The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/ Hsp70 and the proteasome. J. Biol. Chem. 275, 4513-4617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4513-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 28
    • 0039598518 scopus 로고    scopus 로고
    • Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function
    • Luders J., Demand J., Papp O. and Hohfeld J. (2000b) Distinct isoforms of the cofactor BAG-1 differentially affect Hsc70 chaperone function. J. Biol. Chem. 275, 14817-14823.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14817-14823
    • Luders, J.1    Demand, J.2    Papp, O.3    Hohfeld, J.4
  • 29
    • 0027260315 scopus 로고
    • Heat shock protects neuronal cells from programmed cell death by apoptosis
    • Mailhos C., Howard M. K. and Latchman D. S. (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
  • 31
    • 0029975348 scopus 로고    scopus 로고
    • Induction of HSP70 in rat brain following subarachnoid hemorrhage produced by endovascular perforation
    • Matz P. G., Sundaresan S., Sharp F. R. and Weinstein P. R. (1996) Induction of HSP70 in rat brain following subarachnoid hemorrhage produced by endovascular perforation. J. Neurosurg. 85, 138-145.
    • (1996) J. Neurosurg. , vol.85 , pp. 138-145
    • Matz, P.G.1    Sundaresan, S.2    Sharp, F.R.3    Weinstein, P.R.4
  • 32
    • 0024990864 scopus 로고
    • Effect of noncompetitive blockade of N-methyl-D-Aspartate receptors on the neurochemical sequelae of experimental brain injury
    • McIntosh T. K., Vink R., Soares H., Hayes R. and Simon R. (1990) Effect of noncompetitive blockade of N-methyl-D-Aspartate receptors on the neurochemical sequelae of experimental brain injury. J. Neurochem. 55, 1170-1179.
    • (1990) J. Neurochem. , vol.55 , pp. 1170-1179
    • McIntosh, T.K.1    Vink, R.2    Soares, H.3    Hayes, R.4    Simon, R.5
  • 33
    • 0028801661 scopus 로고
    • Heat-shock 70 messenger RNA levels in human brain: Correlation with agonal fever
    • Morrison-Bogorad M., Zimmerman A. L. and Pardue S. (1995) Heat-shock 70 messenger RNA levels in human brain: correlation with agonal fever. J. Neurochem. 64, 235-246.
    • (1995) J. Neurochem. , vol.64 , pp. 235-246
    • Morrison-Bogorad, M.1    Zimmerman, A.L.2    Pardue, S.3
  • 34
    • 0029868794 scopus 로고    scopus 로고
    • Over-expression of HSP-70 protects astrocytes from combined oxygen-glucose deprivation
    • Papadopoulos M. C., Sun X. Y., Cao J., Mivechi N. F. and Giffard R. G. (1996) Over-expression of HSP-70 protects astrocytes from combined oxygen-glucose deprivation. Neuroreport 7, 429-432.
    • (1996) Neuroreport. , vol.7 , pp. 429-432
    • Papadopoulos, M.C.1    Sun, X.Y.2    Cao, J.3    Mivechi, N.F.4    Giffard, R.G.5
  • 35
    • 0028639450 scopus 로고
    • Selective postmortem degradation of inducible heat shock protein 70 mRNAs in rat brain
    • Pardue S. and Morrison-Bogorad M. (1994) Selective postmortem degradation of inducible heat shock protein 70 mRNAs in rat brain. Cell Mol. Neurobiol. 14, 341-357.
    • (1994) Cell Mol. Neurobiol. , vol.14 , pp. 341-357
    • Pardue, S.1    Morrison-Bogorad, M.2
  • 36
    • 0031007324 scopus 로고    scopus 로고
    • The heat shock stress response after brain lesions: Induction of 72 kDa heat shock protein (cell types involved, axonal transport, transcriptional regulation) and protein synthesis inhibition
    • Planas A. M., Soriano M. A., Estrada A., Sanz O., Martin F. and Ferrer I. (1997) The heat shock stress response after brain lesions: induction of 72 kDa heat shock protein (cell types involved, axonal transport, transcriptional regulation) and protein synthesis inhibition. Prog. Neurobiol. 51, 607-636.
    • (1997) Prog. Neurobiol. , vol.51 , pp. 607-636
    • Planas, A.M.1    Soriano, M.A.2    Estrada, A.3    Sanz, O.4    Martin, F.5    Ferrer, I.6
  • 37
    • 0028927339 scopus 로고
    • Regional induction of c-fos and heat shock protein-72 mRNA following fluid-percussion brain injury in the rat
    • Raghupathi R., Welsh F. A., Lowenstein D. H., Gennarelli T. A. and Mclntosh T. K. (1995) Regional induction of c-fos and heat shock protein-72 mRNA following fluid-percussion brain injury in the rat. J. Cereb. Blood Flow Metab. 15, 467-473.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 467-473
    • Raghupathi, R.1    Welsh, F.A.2    Lowenstein, D.H.3    Gennarelli, T.A.4    Mclntosh, T.K.5
  • 38
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • Ritossa F. A. (1962) A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia 18, 571-573.
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.A.1
  • 39
    • 0026336621 scopus 로고
    • Heat shock protects cultured neurons from glutamate toxicity
    • Rordorf G., Koroshetz W. J. and Bonventre J. V. (1991) Heat shock protects cultured 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
  • 40
    • 0035145555 scopus 로고    scopus 로고
    • Excitatory amino acid concentrations in ventricular cerebrospinal fluid after severe traumatic brain injury in infants and children: The role of child abuse
    • Ruppel R. A., Kochanek P. M., Adelson P. D., Rose M. E., Wisniewski S. R., Bell M. J., Clark R. S., Marion D. W. and Graham S. H. (2001) Excitatory amino acid concentrations in ventricular cerebrospinal fluid after severe traumatic brain injury in infants and children: the role of child abuse. J. Pediatr. 138, 18-25.
    • (2001) J. Pediatr. , vol.138 , pp. 18-25
    • Ruppel, R.A.1    Kochanek, P.M.2    Adelson, P.D.3    Rose, M.E.4    Wisniewski, S.R.5    Bell, M.J.6    Clark, R.S.7    Marion, D.W.8    Graham, S.H.9
  • 42
    • 0344200100 scopus 로고    scopus 로고
    • A nuclear action of the eurkaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity
    • Schneikert J., Hubner S., Martin E. and Cato A. C. B. (1999) A nuclear action of the eurkaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity. J. Cell Biol. 146, 929-940.
    • (1999) J. Cell Biol. , vol.146 , pp. 929-940
    • Schneikert, J.1    Hubner, S.2    Martin, E.3    Cato, A.C.B.4
  • 43
    • 0026042945 scopus 로고
    • The temporal profile of 72-kDa heat-shock protein expression following global ischemia
    • Simon R. P., Cho H., Gwinn R. and Lowenstein D. H. (1991) The temporal profile of 72-kDa heat-shock protein expression following global ischemia. J. Neurosci. 11, 881-889.
    • (1991) J. Neurosci. , vol.11 , pp. 881-889
    • Simon, R.P.1    Cho, H.2    Gwinn, R.3    Lowenstein, D.H.4
  • 44
    • 0028919555 scopus 로고
    • Heat shock protein 70 overexpression affects the response to ultraviolet light in murine fibroblasts. Evidence for increased cell viability and suppression of cytokine release
    • Simon M. M., Reikerstorfer A., Schwarz A., Krone C., Luger T. A., Jaattela M. and Schwarz T. (1995) 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. 95, 926-933.
    • (1995) J. Clin. Invest. , vol.95 , pp. 926-933
    • Simon, M.M.1    Reikerstorfer, A.2    Schwarz, A.3    Krone, C.4    Luger, T.A.5    Jaattela, M.6    Schwarz, T.7
  • 45
    • 0033554044 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 increase calcineurin activity in vitro through calmodulin-dependent and independent mechanisms
    • Someren J. S., Faber L. E., Klein J. D. and Tumlin J. A. (1999) Heat shock proteins 70 and 90 increase calcineurin activity in vitro through calmodulin-dependent and independent mechanisms. Biochem. Biophys. Res. Commun. 260, 619-625.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 619-625
    • Someren, J.S.1    Faber, L.E.2    Klein, J.D.3    Tumlin, J.A.4
  • 48
    • 0027393388 scopus 로고
    • Immunolocalization of heat shock protein after fluid percussive brain injury and relationship to breakdown of the blood-brain barrier
    • Tanno H., Nockels R. P., Pitts L. H. et al. (1993) Immunolocalization of heat shock protein after fluid percussive brain injury and relationship to breakdown of the blood-brain barrier. J. Cereb. Blood Flow Metab. 13, 116-124.
    • (1993) J. Cereb. Blood Flow Metab. , vol.13 , pp. 116-124
    • Tanno, H.1    Nockels, R.P.2    Pitts, L.H.3
  • 49
    • 0032936977 scopus 로고    scopus 로고
    • Immunohistochemical assessment of constitutive and inducible heat-shock protein 70 and ubiquitin inhuman cerebellum and caudate nucleus
    • Tytell M., Brown W. R., Moody D. M. and Challa V. R. (1998) Immunohistochemical assessment of constitutive and inducible heat-shock protein 70 and ubiquitin inhuman cerebellum and caudate nucleus. Mol. Chem. Neuropathol. 35, 97-117.
    • (1998) Mol. Chem. Neuropathol. , vol.35 , pp. 97-117
    • Tytell, M.1    Brown, W.R.2    Moody, D.M.3    Challa, V.R.4
  • 50
    • 0024590250 scopus 로고
    • Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat
    • Vass K., Berger M. L., Nowak T. S. Jr, Welch W. J. and Lassmann H. (1989) Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat. Neurosci. Lett. 100, 259-264.
    • (1989) Neurosci. Lett. , vol.100 , pp. 259-264
    • Vass, K.1    Berger, M.L.2    Nowak T.S., Jr.3    Welch, W.J.4    Lassmann, H.5
  • 51
    • 16044374495 scopus 로고    scopus 로고
    • Heat shock response inhibits cytokine-inducible nitric oxide synthase expression in rat hepatocytes
    • de Vera M. E., Kim Y. M., Wong H. R., Wang Q., Billiar T. R. and Geller D. A. (1996) Heat shock response inhibits cytokine-inducible nitric oxide synthase expression in rat hepatocytes. Hepatology 24, 1238-1245.
    • (1996) Hepatology , vol.24 , pp. 1238-1245
    • De Vera, M.E.1    Kim, Y.M.2    Wong, H.R.3    Wang, Q.4    Billiar, T.R.5    Geller, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.