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Volumn 29, Issue 9, 2004, Pages 1767-1777

Life-long effects of perinatal asphyxia on stress-induced proteins and dynamin 1 in rat brain

Author keywords

Dynamin 1; perinatal asphyxia; protein disulfide isomerase; rat; stress induced phosphoprotein 1

Indexed keywords

DYNAMIN I; PHOSPHOPROTEIN; PROTEIN DERIVATIVE; PROTEIN DISULFIDE ISOMERASE;

EID: 4143148654     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000035813.73790.b5     Document Type: Article
Times cited : (10)

References (37)
  • 3
    • 0029944965 scopus 로고    scopus 로고
    • Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1
    • Jiang, B. H., Rue, E., Wang, G. L., Roe, R., and Semenza, G. L. 1996. Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. J. Biol. Chem. 271:17771-17778.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17771-17778
    • Jiang, B.H.1    Rue, E.2    Wang, G.L.3    Roe, R.4    Semenza, G.L.5
  • 4
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero, P., Okamoto, K., Coumailleau, P., O'Brien, S., Tanaka, H., and Poellinger, L. 2000. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell. Biol. 20:402-415.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 402-415
    • Carrero, P.1    Okamoto, K.2    Coumailleau, P.3    O'Brien, S.4    Tanaka, H.5    Poellinger, L.6
  • 5
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema, M., Hirota, K., Mimura, J., Abe, H., Yodoi, J., Sogawa, K., Poellinger, L., and Fujii-Kuriyama, Y. 1999. Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 18:1905-1914.
    • (1999) EMBO J. , vol.18 , pp. 1905-1914
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 6
    • 0032880215 scopus 로고    scopus 로고
    • Transitional change in interaction between HIF-1 and HFN-4 in response to hypoxia
    • Zhang, W., Tsuchiya, T., and Yasukochi, Y. 1999. Transitional change in interaction between HIF-1 and HFN-4 in response to hypoxia. J. Human Gen. 44:293-299.
    • (1999) J. Human Gen. , vol.44 , pp. 293-299
    • Zhang, W.1    Tsuchiya, T.2    Yasukochi, Y.3
  • 7
    • 0029789568 scopus 로고    scopus 로고
    • Functional interference between hypoxia and dioxin signal transduction pathways: Competition for recruitment of the Arnt transcription factor
    • Gradin, K., McGuire, J., Wenger, R. H., Kvietikova, I., Whiteflaw, M. L., Toftgard, R., Tora, L., Gassmann, M., and Poellinger, L. 1996. Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor. Mol. Cell. Biol. 16:5221-5231.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5221-5231
    • Gradin, K.1    McGuire, J.2    Wenger, R.H.3    Kvietikova, I.4    Whiteflaw, M.L.5    Toftgard, R.6    Tora, L.7    Gassmann, M.8    Poellinger, L.9
  • 8
    • 0030887045 scopus 로고    scopus 로고
    • Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway
    • Hogenesch, J. B., Chan, W. K., Jackiwh, V. H., Brown, R. C., Gu, Y. Z., Pray-Grant, M., Predew, G. H., and Bradfield, C. A. 1997. Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. J. Biol. Chem. 272:8581-8593.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8581-8593
    • Hogenesch, J.B.1    Chan, W.K.2    Jackiwh, V.H.3    Brown, R.C.4    Gu, Y.Z.5    Pray-Grant, M.6    Predew, G.H.7    Bradfield, C.A.8
  • 13
    • 0034805931 scopus 로고    scopus 로고
    • Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease
    • Yoo, B. C., Kim, S. H., Cairns, N., Fountoulakis, M., and Lubec, G. 2001. Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease. Biochem. Biophys. Res. Commun. 280:249-258.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 249-258
    • Yoo, B.C.1    Kim, S.H.2    Cairns, N.3    Fountoulakis, M.4    Lubec, G.5
  • 14
    • 0036288814 scopus 로고    scopus 로고
    • Reduction of actin-related protein complex 2/3 in fetal Down Syndrome brain
    • Weitzdoerfer, R., Fountoulakis, M., and Lubec, G. 2002. Reduction of actin-related protein complex 2/3 in fetal Down Syndrome brain. Biochem. Biophys. Res. Commun. 293:836-841.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 836-841
    • Weitzdoerfer, R.1    Fountoulakis, M.2    Lubec, G.3
  • 15
    • 0036148535 scopus 로고    scopus 로고
    • Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1 in fetal Down syndrome brain (trisomy 21)
    • Peyril, A., Weitzdoerfer, R., Gulesserian, T., Fountoulakis, M., and Lubec, G. 2002. Aberrant expression of signaling-related proteins 14-3-3 gamma and RACK1 in fetal Down syndrome brain (trisomy 21). Electrophoresis 23:152-157.
    • (2002) Electrophoresis , vol.23 , pp. 152-157
    • Peyril, A.1    Weitzdoerfer, R.2    Gulesserian, T.3    Fountoulakis, M.4    Lubec, G.5
  • 16
    • 0031159177 scopus 로고    scopus 로고
    • Decrease of brain protein kinase C, protein kinase A, and cyclin-dependent kinase correlating with pH precedes neuronal death in neonatal asphyxia
    • Lubec, B., Dell'Anna, E., Fang-Kircher, S., Marx, M., Herrera-Marschitz, M., and Lubec, G. 1997. Decrease of brain protein kinase C, protein kinase A, and cyclin-dependent kinase correlating with pH precedes neuronal death in neonatal asphyxia. J. Investig. Med. 45:284-294.
    • (1997) J. Investig. Med. , vol.45 , pp. 284-294
    • Lubec, B.1    Dell'Anna, E.2    Fang-Kircher, S.3    Marx, M.4    Herrera-Marschitz, M.5    Lubec, G.6
  • 18
    • 0033618878 scopus 로고    scopus 로고
    • Cholinergic, monoaminergic and glutamatergic changes following perinatal asphyxia in the rat
    • Kohlhauser, C., Mosgoeller, W., Hoeger, H., Lubec, G., and Lubec, B. 1999. Cholinergic, monoaminergic and glutamatergic changes following perinatal asphyxia in the rat. Cell. Mol. Life Sci. 55:1491-1501.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 1491-1501
    • Kohlhauser, C.1    Mosgoeller, W.2    Hoeger, H.3    Lubec, G.4    Lubec, B.5
  • 19
    • 0036918231 scopus 로고    scopus 로고
    • Manifold decreased protein levels of matrin 3, reduced motor protein HMP and hlark in fetal Down's syndrome brain
    • Bernert, G., Fountoulakis, M., and Lubec, G. 2002. Manifold decreased protein levels of matrin 3, reduced motor protein HMP and hlark in fetal Down's syndrome brain. Proteomics 2:1752-1757.
    • (2002) Proteomics , vol.2 , pp. 1752-1757
    • Bernert, G.1    Fountoulakis, M.2    Lubec, G.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 21
    • 0036086620 scopus 로고    scopus 로고
    • Aberrant expression of centractin and capping proteins, integral constituents of the dynactin complex, in fetal down syndrome brain
    • Gulesserian, T., Kim, S. H., Fountoulakis, M., and Lubec, G. 2002. Aberrant expression of centractin and capping proteins, integral constituents of the dynactin complex, in fetal down syndrome brain. Biochem. Biophys. Res. Commun. 291:62-67.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 62-67
    • Gulesserian, T.1    Kim, S.H.2    Fountoulakis, M.3    Lubec, G.4
  • 22
    • 0031214574 scopus 로고    scopus 로고
    • Identification of proteins by matrix-assisted laser desorption ionization-mass spectrometry following in-gel digestion in low-salt, nonvolatile buffer and simplified peptide-recovery
    • Fountoulakis, M., and Langen, H. 1997, Identification of proteins by matrix-assisted laser desorption ionization-mass spectrometry following in-gel digestion in low-salt, nonvolatile buffer and simplified peptide-recovery. Anal. Biochem. 250:153-156.
    • (1997) Anal. Biochem. , vol.250 , pp. 153-156
    • Fountoulakis, M.1    Langen, H.2
  • 23
    • 0033456265 scopus 로고    scopus 로고
    • Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints
    • Berndt, P., Hobohm, U., and Langen, H. 1999. Reliable automatic protein identification from matrix-assisted laser desorption/ionization mass spectrometric peptide fingerprints. Electrophoresis 20:3521-3526.
    • (1999) Electrophoresis , vol.20 , pp. 3521-3526
    • Berndt, P.1    Hobohm, U.2    Langen, H.3
  • 25
    • 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
    • Tanaka, S., Uehara, T., and Nomura, Y. 2000. Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death. J. Biol. Chem. 275:10388-10393.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10388-10393
    • Tanaka, S.1    Uehara, T.2    Nomura, Y.3
  • 27
    • 0037164751 scopus 로고    scopus 로고
    • The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability
    • Lee, P., Rao, J., Fliss, A., Yang, E., Garrett, S., and Caplan, A. J. 2002. The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J. Cell. Biol. 159: 1051-1059.
    • (2002) J. Cell. Biol. , vol.159 , pp. 1051-1059
    • Lee, P.1    Rao, J.2    Fliss, A.3    Yang, E.4    Garrett, S.5    Caplan, A.J.6
  • 29
    • 0034954215 scopus 로고    scopus 로고
    • Differential neuroprotection from human heat shock protein 70 overexpression in in vitro and in vivo models of ischemia and ischemia-like conditions
    • Lee, J. E., Yenari, M. A., Sun, G. H., Xu, L., Edmond, M. R., Cheng, D., Steinberg, G. K., and Giffard, R. G. 2001. Differential neuroprotection from human heat shock protein 70 overexpression in in vitro and in vivo models of ischemia and ischemia-like conditions. Exp. Neurol. 170:129-139.
    • (2001) Exp. Neurol. , vol.170 , pp. 129-139
    • Lee, J.E.1    Yenari, M.A.2    Sun, G.H.3    Xu, L.4    Edmond, M.R.5    Cheng, D.6    Steinberg, G.K.7    Giffard, R.G.8
  • 30
    • 0034019166 scopus 로고    scopus 로고
    • Hypothermia during reperfusion after asphyxial cardiac arrest improves functional recovery and selectively alters stress-induced protein expression
    • Hicks, S. D., DeFranco, D. B., and Callaway, C. W. 2000. Hypothermia during reperfusion after asphyxial cardiac arrest improves functional recovery and selectively alters stress-induced protein expression. J. Cerebr. Blood Flow. Metab. 20:520-530.
    • (2000) J. Cerebr. Blood Flow. Metab. , vol.20 , pp. 520-530
    • Hicks, S.D.1    DeFranco, D.B.2    Callaway, C.W.3
  • 31
    • 0030964214 scopus 로고    scopus 로고
    • Prenatal ischemia reduces neuronal injury caused by neonatal hypoxia-ischemia in rats
    • Cai, Z., Fratkin, J. D., and Rhodes, P. G. 1997. Prenatal ischemia reduces neuronal injury caused by neonatal hypoxia-ischemia in rats. Neuroreport 8:1393-1398.
    • (1997) Neuroreport , vol.8 , pp. 1393-1398
    • Cai, Z.1    Fratkin, J.D.2    Rhodes, P.G.3
  • 33
    • 0032716682 scopus 로고    scopus 로고
    • Moderate hypoxia increases heat shock protein 90 expression in exercised rat aorta
    • Almgren, C. M. and Olson, L. E. 1999. Moderate hypoxia increases heat shock protein 90 expression in exercised rat aorta. J. Vasc. Res. 36:363-371.
    • (1999) J. Vasc. Res. , vol.36 , pp. 363-371
    • Almgren, C.M.1    Olson, L.E.2
  • 34
    • 0033998845 scopus 로고    scopus 로고
    • Effects of hypothermia on hypoxia-induced apoptosis in cultured neurons from developing rat forebrain: Comparison with preconditioning
    • Bossenmeyer-Pourie, C., Koziel, V., and Daval, J. L. 2000. Effects of hypothermia on hypoxia-induced apoptosis in cultured neurons from developing rat forebrain: comparison with preconditioning. Pediatr. Res. 47:385-391.
    • (2000) Pediatr. Res. , vol.47 , pp. 385-391
    • Bossenmeyer-Pourie, C.1    Koziel, V.2    Daval, J.L.3
  • 35
    • 0032999246 scopus 로고    scopus 로고
    • Heat shock protein 72 expression and microtubule-associated protein 2 disappearance after hypoxia-ischemia in the developing rat brain
    • Xia, X. Y., Ikeda, T., Ota, A., Xia, Y. X., Sameshima, H., Ikenoue, T., and Toshimori, K. 1999. Heat shock protein 72 expression and microtubule-associated protein 2 disappearance after hypoxia-ischemia in the developing rat brain. Am. J. Obstet. Gynecol. 180:1254-1262.
    • (1999) Am. J. Obstet. Gynecol. , vol.180 , pp. 1254-1262
    • Xia, X.Y.1    Ikeda, T.2    Ota, A.3    Xia, Y.X.4    Sameshima, H.5    Ikenoue, T.6    Toshimori, K.7
  • 36
    • 0032929002 scopus 로고    scopus 로고
    • Ischemic preconditioning depends on interaction between mitochondrial KATP channels and actin cytoskeleton
    • Baines, C. P., Liu, G. S., Birincioglu, M., Critz, S. D., Cohen, M. V., Downey, and J. M. 1999. Ischemic preconditioning depends on interaction between mitochondrial KATP channels and actin cytoskeleton. Am. J. Physiol. 276:H1361-H1368.
    • (1999) Am. J. Physiol. , vol.276
    • Baines, C.P.1    Liu, G.S.2    Birincioglu, M.3    Critz, S.D.4    Cohen, M.V.5    Downey, M.J.6
  • 37
    • 33750857016 scopus 로고    scopus 로고
    • Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes
    • Bluhm, W. F., Martin, J. L., Mestril, R., and Dillmann, W. H. 1998. Specific heat shock proteins protect microtubules during simulated ischemia in cardiac myocytes. Am. J. Physiol. 275: H2243-H2249.
    • (1998) Am. J. Physiol. , vol.275
    • Bluhm, W.F.1    Martin, J.L.2    Mestril, R.3    Dillmann, W.H.4


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