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Volumn 130, Issue 1-2, 2004, Pages 30-38

Induction of murine HRD1 in experimental cerebral ischemia

Author keywords

Endoplasmic reticulum; Endoplasmic reticulum associated degradation; Hrd1p; Hypoxia; Ischemia

Indexed keywords

GLUCOSE REGULATED PROTEIN 78; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 153; GROWTH ARREST AND DNA DAMAGE INDUCIBLE PROTEIN 34; HYDROXYMETHYLGLUTARYL REDUCTASE DEGRADATION 1P; MEMBRANE PROTEIN; MESSENGER RNA; TRANSCRIPTION FACTOR; TUNICAMYCIN; UNCLASSIFIED DRUG;

EID: 7444252877     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2004.07.013     Document Type: Article
Times cited : (21)

References (31)
  • 1
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • R.J. Kaufman Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls Genes Dev. 13 1999 1211 1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 2
    • 0035190132 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction - A common denominator for cell injury in acute and degenerative diseases of the brain
    • W. Paschen, and A. Frandsen Endoplasmic reticulum dysfunction-a common denominator for cell injury in acute and degenerative diseases of the brain J. Neurochem. 79 2001 719 725
    • (2001) J. Neurochem. , vol.79 , pp. 719-725
    • Paschen, W.1    Frandsen, A.2
  • 3
    • 0037386064 scopus 로고    scopus 로고
    • Dysfunction of the unfolded protein response during global brain ischemia and reperfusion
    • R. Kumar, G.S. Krause, and H. Yoshida Dysfunction of the unfolded protein response during global brain ischemia and reperfusion J. Cereb. Blood Flow Metab. 23 2003 462 471
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 462-471
    • Kumar, R.1    Krause, G.S.2    Yoshida, H.3
  • 4
    • 0038354461 scopus 로고    scopus 로고
    • Shutdown of translation: Lethal or protective? Unfolded protein response versus apoptosis
    • W. Paschen Shutdown of translation: lethal or protective? Unfolded protein response versus apoptosis J. Cereb. Blood Flow Metab. 23 2003 773 779
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 773-779
    • Paschen, W.1
  • 5
    • 0034996080 scopus 로고    scopus 로고
    • Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK
    • R. Kumar, S. Azam, and J.M. Sullivan Brain ischemia and reperfusion activates the eukaryotic initiation factor 2α kinase, PERK J. Neurochem. 77 2001 1418 1421
    • (2001) J. Neurochem. , vol.77 , pp. 1418-1421
    • Kumar, R.1    Azam, S.2    Sullivan, J.M.3
  • 6
    • 0036433578 scopus 로고    scopus 로고
    • Mechanisms underlying suppression of protein synthesis induced by transient focal cerebral ischemia in mouse brain
    • T. Mengesdorf, C.G. Proud, and W. Paschen Mechanisms underlying suppression of protein synthesis induced by transient focal cerebral ischemia in mouse brain Exp. Neurol. 177 2002 538 546
    • (2002) Exp. Neurol. , vol.177 , pp. 538-546
    • Mengesdorf, T.1    Proud, C.G.2    Paschen, W.3
  • 7
    • 0035500702 scopus 로고    scopus 로고
    • Hypothermic treatment restores glucose regulated protein 78 (GRP78) expression in ischemic brain
    • M. Aoki, M. Tamatani, and M. Taniguchi Hypothermic treatment restores glucose regulated protein 78 (GRP78) expression in ischemic brain Mol. Brain Res. 95 2001 117 128
    • (2001) Mol. Brain Res. , vol.95 , pp. 117-128
    • Aoki, M.1    Tamatani, M.2    Taniguchi, M.3
  • 8
    • 0033534592 scopus 로고    scopus 로고
    • Activation of MYD116 expression following transient forebrain ischemia in rat: Implications for a role of disturbances of endoplasmic reticulum calcium homeostasis
    • J. Doutheil, S. Althausen, and C. Gissel Activation of MYD116 expression following transient forebrain ischemia in rat: implications for a role of disturbances of endoplasmic reticulum calcium homeostasis Mol. Brain Res. 63 1999 225 232
    • (1999) Mol. Brain Res. , vol.63 , pp. 225-232
    • Doutheil, J.1    Althausen, S.2    Gissel, C.3
  • 9
    • 0032544514 scopus 로고    scopus 로고
    • Activation of gadd153 expression through transient cerebral ischemia: Evidence that ischemia causes endoplasmic reticulum dysfunction
    • W. Paschen, C. Gissel, and T. Linden Activation of gadd153 expression through transient cerebral ischemia: evidence that ischemia causes endoplasmic reticulum dysfunction Mol. Brain Res. 60 1998 115 122
    • (1998) Mol. Brain Res. , vol.60 , pp. 115-122
    • Paschen, W.1    Gissel, C.2    Linden, T.3
  • 10
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded protein response
    • R. Friedlander, E. Jarosch, J. Urban, C. Volkwein, and T. Sommer A regulatory link between ER-associated protein degradation and the unfolded protein response Nat. Cell Biol. 2 2000 379 384
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 11
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • R.Y. Hampton ER-associated degradation in protein quality control and cellular regulation Curr. Opin. Cell Biol. 14 2002 476 482
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 12
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • J. Bordallo, R.K. Plemper, A. Finger, and D.H. Wolf Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins Mol. Biol. Cell 9 1998 209 222
    • (1998) Mol. Biol. Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 13
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • K.J. Travers, C.K. Patil, and L. Wodicka Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation Cell 101 2000 249 258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3
  • 14
    • 0034971386 scopus 로고    scopus 로고
    • In vivo action of the HRD ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation
    • R.G. Gardner, A.G. Shearer, and R.Y. Hampton In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation Mol. Cell. Biol. 21 2001 4276 4291
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4276-4291
    • Gardner, R.G.1    Shearer, A.G.2    Hampton, R.Y.3
  • 15
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane anchored ubiquitin ligase required for ER-associated degradation
    • N.W. Bays, R.G. Gardner, and L.P. Seelig Hrd1p/Der3p is a membrane anchored ubiquitin ligase required for ER-associated degradation Nat. Cell Biol. 3 2001 24 29
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3
  • 16
    • 0037021416 scopus 로고    scopus 로고
    • Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
    • M. Kaneko, M. Ishiguro, and Y. Niinuma Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation FEBS Lett. 532 2002 147 152
    • (2002) FEBS Lett. , vol.532 , pp. 147-152
    • Kaneko, M.1    Ishiguro, M.2    Niinuma, Y.3
  • 17
    • 0019366919 scopus 로고
    • The influence of immaturity on hypoxic-ischemic brain damage in the rat
    • J.E. Rice III, R.C. Vannucci, and J.B. Brierley The influence of immaturity on hypoxic-ischemic brain damage in the rat Ann. Neurol. 9 1981 131 141
    • (1981) Ann. Neurol. , vol.9 , pp. 131-141
    • Rice III, J.E.1    Vannucci, R.C.2    Brierley, J.B.3
  • 18
    • 0030051010 scopus 로고    scopus 로고
    • Effects of hypoxia-ischemia on GLUT1 and GLUT3 glucose transporters in immature rat brain
    • S.J. Vannucci, L.B. Seaman, and R.C. Vannucci Effects of hypoxia-ischemia on GLUT1 and GLUT3 glucose transporters in immature rat brain J. Cereb. Blood Flow Metab. 16 1996 77 81
    • (1996) J. Cereb. Blood Flow Metab. , vol.16 , pp. 77-81
    • Vannucci, S.J.1    Seaman, L.B.2    Vannucci, R.C.3
  • 20
    • 0036628509 scopus 로고    scopus 로고
    • IGF-I and microglia/macrophage proliferation in the ischemic mouse brain
    • S.L. O'Donnell, T.J. Frederick, and J.K. Krady IGF-I and microglia/macrophage proliferation in the ischemic mouse brain Glia 38 2002 85 97
    • (2002) Glia , vol.38 , pp. 85-97
    • O'Donnell, S.L.1    Frederick, T.J.2    Krady, J.K.3
  • 21
    • 0141994809 scopus 로고    scopus 로고
    • DNA microarry analysis of hippocampal gene expression measured twelve hours after hypoxia-ischemia in the mouse
    • R.W. Gilbert, W.J. Costain, and M.E. Blanchard DNA microarry analysis of hippocampal gene expression measured twelve hours after hypoxia-ischemia in the mouse J. Cereb. Blood Flow Metab. 23 2003 1195 1211
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1195-1211
    • Gilbert, R.W.1    Costain, W.J.2    Blanchard, M.E.3
  • 22
    • 0034709620 scopus 로고    scopus 로고
    • Expression of leptin receptors and induction of IL-1β transcript in glial cells
    • T. Hosoi, Y. Okuma, and Y. Nomura Expression of leptin receptors and induction of IL-1β transcript in glial cells Biochem. Biophys. Res. Commun. 273 2000 312 315
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 312-315
    • Hosoi, T.1    Okuma, Y.2    Nomura, Y.3
  • 23
    • 0037144597 scopus 로고    scopus 로고
    • Role of ubiquitin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death
    • H.S. Ko, T. Uehara, and Y. Nomura Role of ubiquitin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death J. Biol. Chem. 277 2002 35386 35392
    • (2002) J. Biol. Chem. , vol.277 , pp. 35386-35392
    • Ko, H.S.1    Uehara, T.2    Nomura, Y.3
  • 24
    • 0034615941 scopus 로고    scopus 로고
    • Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death
    • S. Tanaka, T. Uehara, and Y. Nomura Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death J. Biol. Chem. 275 2000 10388 10393
    • (2000) J. Biol. Chem. , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 25
    • 0036720939 scopus 로고    scopus 로고
    • Brain stem is a direct target for leptin's action in the central nervous system
    • T. Hosoi, T. Kawagishi, Y. Okuma, and Y. Nomura Brain stem is a direct target for leptin's action in the central nervous system Endocrinology 143 2002 3498 3504
    • (2002) Endocrinology , vol.143 , pp. 3498-3504
    • Hosoi, T.1    Kawagishi, T.2    Okuma, Y.3    Nomura, Y.4
  • 26
    • 8944259440 scopus 로고    scopus 로고
    • Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein
    • X.Z. Wang, B. Lawson, and J.W. Brewer Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein Mol. Cell. Biol. 16 1996 4273 4280
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4273-4280
    • Wang, X.Z.1    Lawson, B.2    Brewer, J.W.3
  • 27
    • 0035875397 scopus 로고    scopus 로고
    • 2+-ATPase: Relationship between global protein synthesis and expression and translation of individual genes
    • 2+-ATPase: relationship between global protein synthesis and expression and translation of individual genes Biochem. J. 356 2001 805 812
    • (2001) Biochem. J. , vol.356 , pp. 805-812
    • Mengesdorf, T.1    Althausen, S.2    Oberndorfer, I.3
  • 28
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: Elucidation by GADD34-deficient mice
    • E. Kojima, A. Takeuchi, and M. Haneda The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice FASEB 17 2003 1573 1575
    • (2003) FASEB , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3
  • 29
    • 0020067965 scopus 로고
    • Temporal profile of neuronal damage in a model of transient forebrain ischemia
    • W.A. Pulsinelli, J.B. Brierley, and F. Pulm Temporal profile of neuronal damage in a model of transient forebrain ischemia Ann. Neurol. 11 1982 491 498
    • (1982) Ann. Neurol. , vol.11 , pp. 491-498
    • Pulsinelli, W.A.1    Brierley, J.B.2    Pulm, F.3
  • 30
    • 0029806516 scopus 로고    scopus 로고
    • 2+-ATPase mRNA levels in transient cerebral ischemia of rat: A quantitative polymerase chain reaction study
    • 2+-ATPase mRNA levels in transient cerebral ischemia of rat: a quantitative polymerase chain reaction study Neurosci. Lett. 217 1996 41 44
    • (1996) Neurosci. Lett. , vol.217 , pp. 41-44
    • Paschen, W.1    Doutheil, J.2    Uto, A.3


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