메뉴 건너뛰기




Volumn 67, Issue 5, 1996, Pages 2005-2012

Global brain ischemia and reperfusion: Modifications in eukaryotic initiation factors associated with inhibition of translation initiation

Author keywords

Brain ischemia; Initiation factors; Protein synthesis; Translation initiation

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; INITIATION FACTOR;

EID: 0029838333     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67052005.x     Document Type: Article
Times cited : (115)

References (41)
  • 1
    • 0029083820 scopus 로고
    • Purification and characterization of guanine nucleotide-exchange factor, eIF-2B, and p37 calmodulin-binding protein from calf brain
    • Alcázar A., Martín M. E., Soria E., Rodríguez S., Fando J. L., and Salinas M. (1995) Purification and characterization of guanine nucleotide-exchange factor, eIF-2B, and p37 calmodulin-binding protein from calf brain. J. Neurochem. 65, 754-761.
    • (1995) J. Neurochem. , vol.65 , pp. 754-761
    • Alcázar, A.1    Martín, M.E.2    Soria, E.3    Rodríguez, S.4    Fando, J.L.5    Salinas, M.6
  • 2
    • 0023264868 scopus 로고
    • The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells
    • Buckley B. and Ehrenfeld E. (1987) The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 262, 13599-13606.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13599-13606
    • Buckley, B.1    Ehrenfeld, E.2
  • 3
    • 0027992399 scopus 로고
    • Phosphorylation of the α subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischemia in the rat
    • Burda J., Martin M. E., Garcia A., Alcazar A., Fando J. L., and Salinas M. (1994) Phosphorylation of the α subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischemia in the rat. Biochem. J. 302, 335-338.
    • (1994) Biochem. J. , vol.302 , pp. 335-338
    • Burda, J.1    Martin, M.E.2    Garcia, A.3    Alcazar, A.4    Fando, J.L.5    Salinas, M.6
  • 4
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58, 453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 5
    • 0017411657 scopus 로고
    • The effect of ischemia and recirculation on protein synthesis in the rat brain
    • Cooper H. K., Zalewska T., Kawakami S., and Hossman K. A. (1977) The effect of ischemia and recirculation on protein synthesis in the rat brain. J. Neurochem. 28, 929-934.
    • (1977) J. Neurochem. , vol.28 , pp. 929-934
    • Cooper, H.K.1    Zalewska, T.2    Kawakami, S.3    Hossman, K.A.4
  • 6
    • 0022998256 scopus 로고
    • Preparation of a cell-free extract from rat brain which can initiate protein synthesis in vitro
    • Cosgrove J. and Rapoport S. I. (1986) Preparation of a cell-free extract from rat brain which can initiate protein synthesis in vitro. Neurochem. Res. 11, 1289-1301.
    • (1986) Neurochem. Res. , vol.11 , pp. 1289-1301
    • Cosgrove, J.1    Rapoport, S.I.2
  • 7
    • 0021854747 scopus 로고
    • Mechanism of activation of the heme-stabilized translational inhibitor of reticulocyte lysates by calcium ions and phospholipid
    • DeHerreros A. G., DeHaro C., and Ochoa S. (1985) Mechanism of activation of the heme-stabilized translational inhibitor of reticulocyte lysates by calcium ions and phospholipid. Proc. Nail. Acad. Sci. USA 82, 3119-3123.
    • (1985) Proc. Nail. Acad. Sci. USA , vol.82 , pp. 3119-3123
    • DeHerreros, A.G.1    DeHaro, C.2    Ochoa, S.3
  • 8
    • 0019156813 scopus 로고
    • Regional protein synthesis in rat brain following acute hemispheric ischemia
    • Dienel G. A., Pulsinelli W. A., and Duffy T. E. (1980) Regional protein synthesis in rat brain following acute hemispheric ischemia. J. Neurochem. 35, 1216-1226.
    • (1980) J. Neurochem. , vol.35 , pp. 1216-1226
    • Dienel, G.A.1    Pulsinelli, W.A.2    Duffy, T.E.3
  • 9
    • 0001908392 scopus 로고
    • Cerebroprotective effects of a parenteral flunarizine formulation
    • (Hartmann A. and Kuchinsky W., eds), Springer-Verlag, Berlin
    • Edmonds H. L. Jr., Raque G. M. Jr., Zhang P. Y., Jenkins S. A., and Sheilds C. B. (1989) Cerebroprotective effects of a parenteral flunarizine formulation, in Cerebral Ischemia and Calcium (Hartmann A. and Kuchinsky W., eds), pp. 494-500. Springer-Verlag, Berlin.
    • (1989) Cerebral Ischemia and Calcium , pp. 494-500
    • Edmonds Jr., H.L.1    Raque Jr., G.M.2    Zhang, P.Y.3    Jenkins, S.A.4    Sheilds, C.B.5
  • 10
    • 0020356106 scopus 로고
    • Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eukaryotic initiation factor 3 and a cap binding protein complex
    • Etchison D., Milburn S. C., Edery I., Sonenberg N., and Hershey J. W. (1982) Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eukaryotic initiation factor 3 and a cap binding protein complex. J. Biol. Chem. 257, 14806-14810.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14806-14810
    • Etchison, D.1    Milburn, S.C.2    Edery, I.3    Sonenberg, N.4    Hershey, J.W.5
  • 11
    • 0017171765 scopus 로고
    • Initiation of the polypeptide chain by reticulocyte cell-free systems: Survey of different inhibitors of translation
    • Fresno M., Carrasco L., and Vazquez D. (1976) Initiation of the polypeptide chain by reticulocyte cell-free systems: survey of different inhibitors of translation. Eur. J. Biochem. 68, 353-364.
    • (1976) Eur. J. Biochem. , vol.68 , pp. 353-364
    • Fresno, M.1    Carrasco, L.2    Vazquez, D.3
  • 12
    • 0025668191 scopus 로고
    • Overview: Phosphorylation and translation control
    • Hershey J. W. B. (1990) Overview: phosphorylation and translation control. Enzyme 44, 17-27.
    • (1990) Enzyme , vol.44 , pp. 17-27
    • Hershey, J.W.B.1
  • 13
    • 0015719003 scopus 로고
    • Reversibility of ischemic brain damage
    • Hossman K. A. and Kleihues P. (1973) Reversibility of ischemic brain damage. Arch. Neurol. 29, 375-384.
    • (1973) Arch. Neurol. , vol.29 , pp. 375-384
    • Hossman, K.A.1    Kleihues, P.2
  • 14
    • 0027476419 scopus 로고
    • Stress-induced inhibition of protein synthesis initiation: Modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient ischemia in the rat
    • Hu B. and Wieloch T. (1993) Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient ischemia in the rat. J. Neurosci. 13, 1830-1838.
    • (1993) J. Neurosci. , vol.13 , pp. 1830-1838
    • Hu, B.1    Wieloch, T.2
  • 15
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities
    • Ingebritsen T. S. and Cohen P. (1983) The protein phosphatases involved in cellular regulation. 1. Classification and substrate specificities. Eur. J. Biochem. 132, 255-261.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 16
    • 0026733511 scopus 로고
    • Preferential translation of heat shock mRNAs in HeLa cells deficient in protein synthesis initiation factors eIF-4E and eIF-4γ
    • Joshi-Barve S., DeBenedetti A., and Rhoads R. E. (1992) Preferential translation of heat shock mRNAs in HeLa cells deficient in protein synthesis initiation factors eIF-4E and eIF-4γ. J. Biol. Chem. 267, 21038-21043.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21038-21043
    • Joshi-Barve, S.1    DeBenedetti, A.2    Rhoads, R.E.3
  • 17
    • 0026072956 scopus 로고
    • Mechanism of inhibition of peptide chain initiation by amino acid deprivation in perfused rat liver
    • Kimball S. R., Antonetti D. A., Brawley R. M., and Jefferson L. S. (1991) Mechanism of inhibition of peptide chain initiation by amino acid deprivation in perfused rat liver. J. Biol. Chem. 266, 1969-1976.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1969-1976
    • Kimball, S.R.1    Antonetti, D.A.2    Brawley, R.M.3    Jefferson, L.S.4
  • 18
    • 0027284925 scopus 로고
    • Suppression of protein synthesis in the reperfused brain
    • Krause G. S. and Tiffany B. R. (1993) Suppression of protein synthesis in the reperfused brain. Stroke 24, 747-756.
    • (1993) Stroke , vol.24 , pp. 747-756
    • Krause, G.S.1    Tiffany, B.R.2
  • 19
    • 0029117427 scopus 로고
    • Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G with picornaviral proteases
    • Lamphear B. J., Kirchweger R., Skern T., and Rhoades R. E. (1995) Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G with picornaviral proteases. J. Biol. Chem. 270, 21975-21983.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21975-21983
    • Lamphear, B.J.1    Kirchweger, R.2    Skern, T.3    Rhoades, R.E.4
  • 20
    • 0024331965 scopus 로고
    • Evaluation of protein phosphorylation state by a combination of vertical slab gel isoelectric focusing and immunoblotting
    • Maurides P. A., Giridhar R. A., and Jagus R. (1989) Evaluation of protein phosphorylation state by a combination of vertical slab gel isoelectric focusing and immunoblotting. Anal. Biochem. 183, 144-151.
    • (1989) Anal. Biochem. , vol.183 , pp. 144-151
    • Maurides, P.A.1    Giridhar, R.A.2    Jagus, R.3
  • 21
    • 0028245588 scopus 로고
    • Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2α kinase
    • Mellor H., Flowers K. M., Kimball S. R., and Jefferson L. S. (1994) Cloning and characterization of cDNA encoding rat hemin-sensitive initiation factor-2α kinase. J. Biol. Chem. 269, 10201-10204.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10201-10204
    • Mellor, H.1    Flowers, K.M.2    Kimball, S.R.3    Jefferson, L.S.4
  • 24
    • 0025617461 scopus 로고
    • Protein synthesis and the heat shock/stress response after ischemia
    • Nowak T. S. Jr. (1990) Protein synthesis and the heat shock/stress response after ischemia. Cerebrovasc. Brain Metab. Rev. 2, 345-366.
    • (1990) Cerebrovasc. Brain Metab. Rev. , vol.2 , pp. 345-366
    • Nowak Jr., T.S.1
  • 25
    • 0021357264 scopus 로고
    • An in vitro amino acid incorporation method for assessing the status of in vivo protein synthesis
    • Nowak T. S. Jr., Carty E. R., Lust W. D., and Passonneau J. V. (1984) An in vitro amino acid incorporation method for assessing the status of in vivo protein synthesis. Anal. Biochem. 136, 285-292.
    • (1984) Anal. Biochem. , vol.136 , pp. 285-292
    • Nowak Jr., T.S.1    Carty, E.R.2    Lust, W.D.3    Passonneau, J.V.4
  • 26
    • 0025190058 scopus 로고
    • Heat shock RNA levels in brain and other tissues after hyperthermia and transient ischemia
    • Nowak T. S. Jr., Bond U., and Schlesinger M. J. (1990) Heat shock RNA levels in brain and other tissues after hyperthermia and transient ischemia. J. Neurochem. 54, 451-458.
    • (1990) J. Neurochem. , vol.54 , pp. 451-458
    • Nowak Jr., T.S.1    Bond, U.2    Schlesinger, M.J.3
  • 27
    • 0028938425 scopus 로고
    • Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores
    • Prostko C. R., Dholakia J. N., Brostrom M. A., and Brostrom C. O. (1995) Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores. J. Biol. Chem. 270, 6211-6215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6211-6215
    • Prostko, C.R.1    Dholakia, J.N.2    Brostrom, M.A.3    Brostrom, C.O.4
  • 28
    • 0029007407 scopus 로고
    • PKR: A new name and new roles
    • Proud C. G. (1995) PKR: a new name and new roles. Trends Biol. Sci. 20, 241-246.
    • (1995) Trends Biol. Sci. , vol.20 , pp. 241-246
    • Proud, C.G.1
  • 30
    • 0025250558 scopus 로고
    • Activity of protein phosphatases against initiation factor-2 and elongation factor-2
    • Redpath N. T. and Proud C. G. (1990) Activity of protein phosphatases against initiation factor-2 and elongation factor-2. Biochem. J. 272, 175-180.
    • (1990) Biochem. J. , vol.272 , pp. 175-180
    • Redpath, N.T.1    Proud, C.G.2
  • 31
    • 0028008882 scopus 로고
    • Molecular mechanisms in the control of translation by hormones and growth factors
    • Redpath N. T. and Proud C. G. (1994) Molecular mechanisms in the control of translation by hormones and growth factors. Biochim. Biophys. Acta 1220, 147-162.
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 147-162
    • Redpath, N.T.1    Proud, C.G.2
  • 32
    • 0026602663 scopus 로고
    • Prevention of post-ischemic brain lipid conjugated diene production and neurological injury by hydroxyethyl starch-conjugated deferoxamine
    • Rosenthal R. E., Chanderbhan R., Marshall G., and Fiskum G. (1992) Prevention of post-ischemic brain lipid conjugated diene production and neurological injury by hydroxyethyl starch-conjugated deferoxamine. Free Radic. Biol. Med. 12, 29-33.
    • (1992) Free Radic. Biol. Med. , vol.12 , pp. 29-33
    • Rosenthal, R.E.1    Chanderbhan, R.2    Marshall, G.3    Fiskum, G.4
  • 33
    • 0026513367 scopus 로고
    • Inhibition of protein synthesis in intact mammalian cells by arachidonic acid
    • Rotman E. I., Brostrom M. A., and Brostrom C. O. (1992) Inhibition of protein synthesis in intact mammalian cells by arachidonic acid. Biochem. J. 282, 487-494.
    • (1992) Biochem. J. , vol.282 , pp. 487-494
    • Rotman, E.I.1    Brostrom, M.A.2    Brostrom, C.O.3
  • 34
    • 0023878562 scopus 로고
    • The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2
    • Rowlands A. G., Panniers R., and Henshaw E. (1988) The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263, 5526-5533.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5526-5533
    • Rowlands, A.G.1    Panniers, R.2    Henshaw, E.3
  • 35
    • 0029067408 scopus 로고
    • Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis
    • Srivastava S. P., Davies M. V., and Kaufman R. F. (1995) Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J. Biol. Chem. 270, 16619-16624.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16619-16624
    • Srivastava, S.P.1    Davies, M.V.2    Kaufman, R.F.3
  • 36
    • 0014981144 scopus 로고
    • Aurintricarboxylic acid: Inhibitor of initiation of protein synthesis
    • Stewart M. L., Grollman A. P., and Huang M. T. (1971) Aurintricarboxylic acid: inhibitor of initiation of protein synthesis. Proc. Natl. Acad. Sci. USA 68, 97-101.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 97-101
    • Stewart, M.L.1    Grollman, A.P.2    Huang, M.T.3
  • 37
    • 0025221754 scopus 로고
    • Regional difference in free fatty acid release and the action of phospholipase during ischemia in rat brain
    • Umemura A. (1990) Regional difference in free fatty acid release and the action of phospholipase during ischemia in rat brain. No To Shinkei 42, 979-986.
    • (1990) No to Shinkei , vol.42 , pp. 979-986
    • Umemura, A.1
  • 38
    • 0024410243 scopus 로고
    • Long-term neurological assessment of the post-resuscitation effects of flunarizine, verapamil and nimodipine in a new model of global complete ischaemia
    • Wauquier A., Melis W., and Janssen P. A. J. (1989) Long-term neurological assessment of the post-resuscitation effects of flunarizine, verapamil and nimodipine in a new model of global complete ischaemia. Neuropharmacology 28, 837-846.
    • (1989) Neuropharmacology , vol.28 , pp. 837-846
    • Wauquier, A.1    Melis, W.2    Janssen, P.A.J.3
  • 40
    • 0025007320 scopus 로고
    • The p220 component of eukaryotic initiation factor 4F is a substrate for multiple calcium-dependent enzymes
    • Wyckoff E. E., Croall D. E., and Ehrenfeld E. (1990) The p220 component of eukaryotic initiation factor 4F is a substrate for multiple calcium-dependent enzymes. Biochemistry 29, 10055-10061.
    • (1990) Biochemistry , vol.29 , pp. 10055-10061
    • Wyckoff, E.E.1    Croall, D.E.2    Ehrenfeld, E.3
  • 41
    • 0026463868 scopus 로고
    • Amino acid sequence of the human protein synthesis initiation factor eIF-4γ
    • Yan R., Rychlik W., Etchison D., and Rhoads R. (1992) Amino acid sequence of the human protein synthesis initiation factor eIF-4γ. J. Biol. Chem. 267, 23226-23231.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23226-23231
    • Yan, R.1    Rychlik, W.2    Etchison, D.3    Rhoads, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.