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Volumn 1249, Issue , 2009, Pages 9-18

Subcellular stress response and induction of molecular chaperones and folding proteins after transient global ischemia in rats

Author keywords

Brain ischemia; CA1 hippocampus; Chaperone and folding protein; Herp GRP78 GRP94 calnexin PDI HSP70 HSP60; Protein aggregation

Indexed keywords

CALNEXIN; CHAPERONE; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HOMOCYSTEINE; MESSENGER RNA; PROTEIN DISULFIDE ISOMERASE;

EID: 58149168845     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2008.10.032     Document Type: Article
Times cited : (68)

References (41)
  • 1
    • 0026665975 scopus 로고
    • The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression
    • Abravaya K., Myers M.P., Murphy S.P., and Morimoto R.I. The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression. Genes Dev. 6 (1992) 1153-1164
    • (1992) Genes Dev. , vol.6 , pp. 1153-1164
    • Abravaya, K.1    Myers, M.P.2    Murphy, S.P.3    Morimoto, R.I.4
  • 3
    • 23044498270 scopus 로고    scopus 로고
    • Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins
    • Corydon T.J., Hansen J., Bross P., and Jensen T.G. Down-regulation of Hsp60 expression by RNAi impairs folding of medium-chain acyl-CoA dehydrogenase wild-type and disease-associated proteins. Mol. Genet. Metab. 85 (2005) 260-270
    • (2005) Mol. Genet. Metab. , vol.85 , pp. 260-270
    • Corydon, T.J.1    Hansen, J.2    Bross, P.3    Jensen, T.G.4
  • 4
    • 34247524717 scopus 로고    scopus 로고
    • Irreversible translation arrest in the reperfused brain
    • DeGracia D.J., and Hu B.R. Irreversible translation arrest in the reperfused brain. J. Cereb. Blood Flow Metab. 27 (2007) 875-893
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 875-893
    • DeGracia, D.J.1    Hu, B.R.2
  • 5
    • 36448993027 scopus 로고    scopus 로고
    • Protein aggregation and proteasome dysfunction after brain ischemia
    • Ge P., Luo Y., Liu C.L., and Hu B. Protein aggregation and proteasome dysfunction after brain ischemia. Stroke 38 (2007) 3230-3236
    • (2007) Stroke , vol.38 , pp. 3230-3236
    • Ge, P.1    Luo, Y.2    Liu, C.L.3    Hu, B.4
  • 8
    • 11844282198 scopus 로고    scopus 로고
    • Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons
    • Hayashi T., Saito A., Okuno S., Ferrand-Drake M., Dodd R.L., and Chan P.H. Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons. J. Cereb. Blood Flow Metab. 25 (2005) 41-53
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 41-53
    • Hayashi, T.1    Saito, A.2    Okuno, S.3    Ferrand-Drake, M.4    Dodd, R.L.5    Chan, P.H.6
  • 9
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • Hebert D.N., and Molinari M. In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87 (2007) 1377-1408
    • (2007) Physiol. Rev. , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 10
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • Holcik M., and Sonenberg N. Translational control in stress and apoptosis. Nat. Rev. Mol. Cell. Biol. 6 (2005) 318-327
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 11
    • 58149144977 scopus 로고    scopus 로고
    • Co-translational protein folding and aggregation after brain ischemia
    • Chan P. (Ed), Springer-Verlag, Berlin Heidelberg New York
    • Hu B. Co-translational protein folding and aggregation after brain ischemia. In: Chan P. (Ed). Acute ischemic Injury and Repair in the Nervous System (2007), Springer-Verlag, Berlin Heidelberg New York 109-120
    • (2007) Acute ischemic Injury and Repair in the Nervous System , pp. 109-120
    • Hu, B.1
  • 12
    • 4644284329 scopus 로고    scopus 로고
    • Protein aggregation, unfolded protein response and delayed neuronal death after brain ischemia
    • Buchan V.A., and Ito U. (Eds), Springer-Verlog, Berlin, Heidelberg
    • Hu B.R., Martone M.E., and Liu C.L. Protein aggregation, unfolded protein response and delayed neuronal death after brain ischemia. In: Buchan V.A., and Ito U. (Eds). Maturation phenomenon in cerebral ischemis (2004), Springer-Verlog, Berlin, Heidelberg 225-237
    • (2004) Maturation phenomenon in cerebral ischemis , pp. 225-237
    • Hu, B.R.1    Martone, M.E.2    Liu, C.L.3
  • 13
    • 0034192398 scopus 로고    scopus 로고
    • Protein aggregation after transient cerebral ischemia
    • Hu B.R., Martone M.E., Jones Y.Z., and Liu C.L. Protein aggregation after transient cerebral ischemia. J. Neurosci. 20 (2000) 3191-3199
    • (2000) J. Neurosci. , vol.20 , pp. 3191-3199
    • Hu, B.R.1    Martone, M.E.2    Jones, Y.Z.3    Liu, C.L.4
  • 15
    • 0016743902 scopus 로고
    • Experimental cerebral ischemia in mongolian gerbils. I. Light microscopic observations
    • Ito U., Spatz M., Walker Jr. J.T., and Klatzo I. Experimental cerebral ischemia in mongolian gerbils. I. Light microscopic observations. Acta. Neuropathol. 32 (1975) 209-223
    • (1975) Acta. Neuropathol. , vol.32 , pp. 209-223
    • Ito, U.1    Spatz, M.2    Walker Jr., J.T.3    Klatzo, I.4
  • 16
    • 0033780693 scopus 로고    scopus 로고
    • Delayed neuronal death
    • Kirino T. Delayed neuronal death. Neuropathology 20 Suppl (2000) S95-S97
    • (2000) Neuropathology , vol.20 SUPPL
    • Kirino, T.1
  • 17
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame K., Agarwala K.L., Kato H., and Miyata T. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J. Biol. Chem. 275 (2000) 32846-32853
    • (2000) J. Biol. Chem. , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 18
    • 0035937721 scopus 로고    scopus 로고
    • Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response
    • Kokame K., Kato H., and Miyata T. Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response. J. Biol. Chem. 276 (2001) 9199-9205
    • (2001) J. Biol. Chem. , vol.276 , pp. 9199-9205
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 19
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee A.S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 35 (2005) 373-381
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 20
    • 5444241464 scopus 로고    scopus 로고
    • Protein ubiquitination in postsynaptic densities after transient cerebral ischemia
    • Liu C.L., Martone M.E., and Hu B.R. Protein ubiquitination in postsynaptic densities after transient cerebral ischemia. J. Cereb. Blood Flow Metab. 24 (2004) 1219-1225
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 1219-1225
    • Liu, C.L.1    Martone, M.E.2    Hu, B.R.3
  • 21
    • 21744453627 scopus 로고    scopus 로고
    • Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia
    • Liu C., Chen S., Kamme F., and Hu B.R. Ischemic preconditioning prevents protein aggregation after transient cerebral ischemia. Neuroscience 134 (2005) 69-80
    • (2005) Neuroscience , vol.134 , pp. 69-80
    • Liu, C.1    Chen, S.2    Kamme, F.3    Hu, B.R.4
  • 22
    • 23944494072 scopus 로고    scopus 로고
    • Co-translational protein aggregation after transient cerebral ischemia
    • Liu C.L., Ge P., Zhang F., and Hu B.R. Co-translational protein aggregation after transient cerebral ischemia. Neuroscience 134 (2005) 1273-1284
    • (2005) Neuroscience , vol.134 , pp. 1273-1284
    • Liu, C.L.1    Ge, P.2    Zhang, F.3    Hu, B.R.4
  • 24
    • 0031055338 scopus 로고    scopus 로고
    • Molecular chaperones and mitochondrial protein folding
    • Martin J. Molecular chaperones and mitochondrial protein folding. J. Bioenerg. Biomembr. 29 (1997) 35-43
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 35-43
    • Martin, J.1
  • 26
    • 0030228708 scopus 로고    scopus 로고
    • Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway
    • Mori K., Kawahara T., Yoshida H., Yanagi H., and Yura T. Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway. Genes Cells 1 (1996) 803-817
    • (1996) Genes Cells , vol.1 , pp. 803-817
    • Mori, K.1    Kawahara, T.2    Yoshida, H.3    Yanagi, H.4    Yura, T.5
  • 27
    • 0035238206 scopus 로고    scopus 로고
    • Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells
    • Naylor D.J., and Hartl F.U. Contribution of molecular chaperones to protein folding in the cytoplasm of prokaryotic and eukaryotic cells. Biochem. Soc. Symp. (2001) 45-68
    • (2001) Biochem. Soc. Symp. , pp. 45-68
    • Naylor, D.J.1    Hartl, F.U.2
  • 28
    • 0025793665 scopus 로고
    • Localization of 70 kDa stress protein mRNA induction in gerbil brain after ischemia
    • Nowak Jr. T.S. Localization of 70 kDa stress protein mRNA induction in gerbil brain after ischemia. J. Cereb. Blood Flow Metab. 11 (1991) 432-439
    • (1991) J. Cereb. Blood Flow Metab. , vol.11 , pp. 432-439
    • Nowak Jr., T.S.1
  • 29
    • 0042473927 scopus 로고    scopus 로고
    • Mechanisms of neuronal cell death: diverse roles of calcium in the various subcellular compartments
    • Paschen W. Mechanisms of neuronal cell death: diverse roles of calcium in the various subcellular compartments. Cell Calcium 34 (2003) 305-310
    • (2003) Cell Calcium , vol.34 , pp. 305-310
    • Paschen, W.1
  • 30
    • 3042730216 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction in brain pathology: critical role of protein synthesis
    • Paschen W. Endoplasmic reticulum dysfunction in brain pathology: critical role of protein synthesis. Curr. Neurovasc. Res. 1 (2004) 173-181
    • (2004) Curr. Neurovasc. Res. , vol.1 , pp. 173-181
    • Paschen, W.1
  • 31
    • 0020069661 scopus 로고
    • Regional cerebral blood flow and glucose metabolism following transient forebrain ischemia
    • Pulsinelli W.A., Levy D.E., and Duffy T.E. Regional cerebral blood flow and glucose metabolism following transient forebrain ischemia. Ann. Neurol. 11 (1982) 499-502
    • (1982) Ann. Neurol. , vol.11 , pp. 499-502
    • Pulsinelli, W.A.1    Levy, D.E.2    Duffy, T.E.3
  • 33
    • 0021225723 scopus 로고
    • The density and distribution of ischemic brain injury in the rat following 2-10 min of forebrain ischemia
    • Smith M.L., Auer R.N., and Siesjo B.K. The density and distribution of ischemic brain injury in the rat following 2-10 min of forebrain ischemia. Acta. Neuropathol. 64 (1984) 319-332
    • (1984) Acta. Neuropathol. , vol.64 , pp. 319-332
    • Smith, M.L.1    Auer, R.N.2    Siesjo, B.K.3
  • 34
    • 0024204164 scopus 로고
    • Localization of 70-kDa stress protein induction in gerbil brain after ischemia
    • Vass K., Welch W.J., and Nowak Jr. T.S. Localization of 70-kDa stress protein induction in gerbil brain after ischemia. Acta. Neuropathol. 77 (1988) 128-135
    • (1988) Acta. Neuropathol. , vol.77 , pp. 128-135
    • Vass, K.1    Welch, W.J.2    Nowak Jr., T.S.3
  • 35
    • 3542991477 scopus 로고    scopus 로고
    • On mechanisms that control heat shock transcription factor activity in metazoan cells
    • Voellmy R. On mechanisms that control heat shock transcription factor activity in metazoan cells. Cell Stress Chaperones 9 (2004) 122-133
    • (2004) Cell Stress Chaperones , vol.9 , pp. 122-133
    • Voellmy, R.1
  • 36
    • 0027517597 scopus 로고
    • Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia
    • Wang S., Longo F.M., Chen J., Butman M., Graham S.H., Haglid K.G., and Sharp F.R. Induction of glucose regulated protein (grp78) and inducible heat shock protein (hsp70) mRNAs in rat brain after kainic acid seizures and focal ischemia. Neurochem. Int. 23 (1993) 575-582
    • (1993) Neurochem. Int. , vol.23 , pp. 575-582
    • Wang, S.1    Longo, F.M.2    Chen, J.3    Butman, M.4    Graham, S.H.5    Haglid, K.G.6    Sharp, F.R.7
  • 37
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE, and ERSE-II
    • Yamamoto K.Y.H., Kokame K., Kaufman R.J., and Mori K. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE, and ERSE-II. J. Biochem. 136 (2004) 343-350
    • (2004) J. Biochem. , vol.136 , pp. 343-350
    • Yamamoto, K.Y.H.1    Kokame, K.2    Kaufman, R.J.3    Mori, K.4
  • 38
    • 34249661030 scopus 로고    scopus 로고
    • Differential response to ischemia in adjacent hippocampalsectors: neuronal death in CA1 versus neurogenesis in dentate gyrus
    • Yamashima T., Tonchev A.B., and Borlongan C.V. Differential response to ischemia in adjacent hippocampalsectors: neuronal death in CA1 versus neurogenesis in dentate gyrus. Biotechnol. J. 2 (2007) 596-607
    • (2007) Biotechnol. J. , vol.2 , pp. 596-607
    • Yamashima, T.1    Tonchev, A.B.2    Borlongan, C.V.3
  • 39
    • 4944234936 scopus 로고    scopus 로고
    • Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones
    • Yoneda T., Benedetti C., Urano F., Clark S.G., Harding H.P., and Ron D. Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J. Cell Sci. 117 (2004) 4055-4066
    • (2004) J. Cell Sci. , vol.117 , pp. 4055-4066
    • Yoneda, T.1    Benedetti, C.2    Urano, F.3    Clark, S.G.4    Harding, H.P.5    Ron, D.6
  • 40
    • 33745104438 scopus 로고    scopus 로고
    • Irreversible aggregation of protein synthesis machinery after focal brain ischemia
    • Zhang F., Liu C.L., and Hu B.R. Irreversible aggregation of protein synthesis machinery after focal brain ischemia. J. Neurochem. 98 (2006) 102-112
    • (2006) J. Neurochem. , vol.98 , pp. 102-112
    • Zhang, F.1    Liu, C.L.2    Hu, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.