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Volumn 11, Issue 6, 1997, Pages 482-492

Decrease of heart protein kinase C and cyclin-dependent kinase precedes death in perinatal asphyxia of the rat

Author keywords

Antioxidant enzymes; Catalase; Electron spin resonance; Glulathione peroxidase; Lipid peroxidation; Malondialdehyde; Neonatal; Oxidative stress; Protein carbonyls; Superoxide dismutase

Indexed keywords

ANTIOXIDANT; CATALASE; CYCLIN DEPENDENT KINASE; GLUTATHIONE PEROXIDASE; PROTEIN KINASE C; SUPEROXIDE DISMUTASE;

EID: 0030925253     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.11.6.9194529     Document Type: Article
Times cited : (32)

References (65)
  • 1
    • 0022179371 scopus 로고
    • Cardiac output in newborn infants with transient niyocardial dysfunction
    • Walther, F. J., Siassi, B., Ramadan N. A., and Wu, P. Y. K. (1985) Cardiac output in newborn infants with transient niyocardial dysfunction. J. Pediatr. 107, 781-785
    • (1985) J. Pediatr. , vol.107 , pp. 781-785
    • Walther, F.J.1    Siassi, B.2    Ramadan, N.A.3    Wu, P.Y.K.4
  • 2
    • 0025611759 scopus 로고
    • Time course and mechanisms of endothelial dysfunction in isolated ischemic and hypoxic perfused rat hearts
    • Tsao, P. S., and Lefer, A. M. (1990) Time course and mechanisms of endothelial dysfunction in isolated ischemic and hypoxic perfused rat hearts. Am. J. Physiol. 259, H1660-H1666
    • (1990) Am. J. Physiol. , vol.259
    • Tsao, P.S.1    Lefer, A.M.2
  • 4
    • 0019256564 scopus 로고
    • Excessive cellular acidosis: An important mechanism of neuronal damage in the brain? Acta Physiol
    • Rehncrona, S., Rosen, I., and Siesjoe, B. K. (1980) Excessive cellular acidosis: an important mechanism of neuronal damage in the brain? Acta Physiol. Scand. 110, 435-437
    • (1980) Scand. , vol.110 , pp. 435-437
    • Rehncrona, S.1    Rosen, I.2    Siesjoe, B.K.3
  • 5
    • 0023774654 scopus 로고
    • Mechanisms of ischemic brain damage
    • Siesjoe, B. K. (1988) Mechanisms of ischemic brain damage. Crit. Care Med. 16, 954-963
    • (1988) Crit. Care Med. , vol.16 , pp. 954-963
    • Siesjoe, B.K.1
  • 6
    • 0028012599 scopus 로고
    • Influence of pH on calcium influx during hypoxia in rat cortical brain slices
    • O'Donnell, B., and Bickler, P. E. (1994) Influence of pH on calcium influx during hypoxia in rat cortical brain slices. Stroke 25, 171-177
    • (1994) Stroke , vol.25 , pp. 171-177
    • O'Donnell, B.1    Bickler, P.E.2
  • 7
    • 0028906351 scopus 로고
    • Acidosis causes failure of astrocyte glutamate uptake during hypoxia
    • Swanson, R. A., Farrell, K., and Simon, R. (1995) Acidosis causes failure of astrocyte glutamate uptake during hypoxia. J. Cereb. Blood Flow Metab. 15, 417-424
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , pp. 417-424
    • Swanson, R.A.1    Farrell, K.2    Simon, R.3
  • 8
    • 18244424540 scopus 로고
    • Acid base changes during complete brain ischemia
    • Siesjoe, B. K., Ekholm, A., Katsura, K., and Theander, S. (1990) Acid base changes during complete brain ischemia. Stroke 21, 194-199
    • (1990) Stroke , vol.21 , pp. 194-199
    • Siesjoe, B.K.1    Ekholm, A.2    Katsura, K.3    Theander, S.4
  • 10
    • 0026884353 scopus 로고
    • Excitatory amino acids contribute to the pathogenesis of perinatal hypoxic-ischemic brain injury
    • Barks, J. D. E., and Silverstein, F. S. (1992) Excitatory amino acids contribute to the pathogenesis of perinatal hypoxic-ischemic brain injury. Brain Pathol. 2, 235-243
    • (1992) Brain Pathol. , vol.2 , pp. 235-243
    • Barks, J.D.E.1    Silverstein, F.S.2
  • 11
    • 0027359376 scopus 로고
    • Ischemia: From acidosis to oxidation
    • Levine, R. L. (1993) Ischemia: from acidosis to oxidation. FASEB J. 7, 1242-1246
    • (1993) FASEB J. , vol.7 , pp. 1242-1246
    • Levine, R.L.1
  • 12
    • 0024993805 scopus 로고
    • Protein kinase C is translocated to cell membranes during cerebral ischemia
    • Cardell, M., Bingren, H., Wieloch, T., Zivin, J., and Saitoh, T. (1990) Protein kinase C is translocated to cell membranes during cerebral ischemia. Neurosci Lett. 119, 228-232
    • (1990) Neurosci Lett. , vol.119 , pp. 228-232
    • Cardell, M.1    Bingren, H.2    Wieloch, T.3    Zivin, J.4    Saitoh, T.5
  • 13
    • 0025604592 scopus 로고
    • Protein kinase C activity in the gerbil hippocampus after transient forebrain ischemia: Morphological and autoradiographic analysis using [3H] phorbol 12,13 dibutyrate
    • Hara, H., Onodera, H., and Kogure, K. (1990) Protein kinase C activity in the gerbil hippocampus after transient forebrain ischemia: morphological and autoradiographic analysis using [3H] phorbol 12,13 dibutyrate. Neurosci. Lett. 120, 120-123
    • (1990) Neurosci. Lett. , vol.120 , pp. 120-123
    • Hara, H.1    Onodera, H.2    Kogure, K.3
  • 14
    • 0024245397 scopus 로고
    • Protein kinase C alterations in the fetal rat brain after global ischemia
    • Louis, J.-C., Magal, E., and Yavin, E. (1988) Protein kinase C alterations in the fetal rat brain after global ischemia. J. Biol. Chem. 263, 19282-19285
    • (1988) J. Biol. Chem. , vol.263 , pp. 19282-19285
    • Louis, J.-C.1    Magal, E.2    Yavin, E.3
  • 15
    • 0026529437 scopus 로고
    • Effect of brain ischemia on protein kinase C
    • Domanska-Janik, K., and Zalewska, T. (1992) Effect of brain ischemia on protein kinase C. J. Neurochem. 58, 1432-1439
    • (1992) J. Neurochem. , vol.58 , pp. 1432-1439
    • Domanska-Janik, K.1    Zalewska, T.2
  • 16
    • 0027932931 scopus 로고
    • Regional alterations of protein kinase C activity following transient cerebral ischemia: Effects of intraischemic brain temperature modulation
    • Busto, R., Globus, Y. T., Neary, J. T., and Ginsberg, M. D. (1994) Regional alterations of protein kinase C activity following transient cerebral ischemia: effects of intraischemic brain temperature modulation. J. Neurochem. 63, 1095-1103
    • (1994) J. Neurochem. , vol.63 , pp. 1095-1103
    • Busto, R.1    Globus, Y.T.2    Neary, J.T.3    Ginsberg, M.D.4
  • 17
    • 0026073294 scopus 로고
    • Changes in the activity of protein kinase C and the differential subcellular redistribution of its isoenzymes in the rat striatum during and following transient forebrain ischemia
    • Wieloch, T., Cardell, M., Bingren, H., Zivin, J., and Saitoh, T. (1991) Changes in the activity of protein kinase C and the differential subcellular redistribution of its isoenzymes in the rat striatum during and following transient forebrain ischemia. J. Neurochem. 56, 1227-1235
    • (1991) J. Neurochem. , vol.56 , pp. 1227-1235
    • Wieloch, T.1    Cardell, M.2    Bingren, H.3    Zivin, J.4    Saitoh, T.5
  • 18
    • 0026668149 scopus 로고
    • 2+/calmodulin-dependent protein kinase II: Potential role in neuronal damage
    • 2+/calmodulin-dependent protein kinase II: potential role in neuronal damage. J. Neurochem. 58, 1743-1753
    • (1992) J. Neurochem. , vol.58 , pp. 1743-1753
    • Aronowski, J.1    Grotta, J.2    Waxham, M.N.3
  • 19
    • 0029897947 scopus 로고    scopus 로고
    • Signalling by protein kinase C isoforms in the heart
    • Puceat, M., and Vassort, G. (1996) Signalling by protein kinase C isoforms in the heart. Mol. Cell Biochem. 157, 65-72
    • (1996) Mol. Cell Biochem. , vol.157 , pp. 65-72
    • Puceat, M.1    Vassort, G.2
  • 20
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y. (1986) Studies and perspectives of protein kinase C. Science 233, 305-312
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 21
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuoka, Y. (1988) The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature (London) 334, 661-665
    • (1988) Nature (London) , vol.334 , pp. 661-665
    • Nishizuoka, Y.1
  • 22
    • 0029996065 scopus 로고    scopus 로고
    • Myocardial preconditioning promises to be a novel approach to the treatment of ischemic heart disease
    • Cohen, M. V., and Downey, J. M. (1996) Myocardial preconditioning promises to be a novel approach to the treatment of ischemic heart disease. Annu. Rev. Med. 47, 21-29
    • (1996) Annu. Rev. Med. , vol.47 , pp. 21-29
    • Cohen, M.V.1    Downey, J.M.2
  • 24
    • 0028908855 scopus 로고
    • Preconditioning of isolated rat heart is mediated by protein kinase C
    • Mitchell, M. B., Meng, X., Ao, L., Brown, J. M., Harken, A. H., and Banerjee, A. (1995) Preconditioning of isolated rat heart is mediated by protein kinase C. Circ. Res. 76, 73-81
    • (1995) Circ. Res. , vol.76 , pp. 73-81
    • Mitchell, M.B.1    Meng, X.2    Ao, L.3    Brown, J.M.4    Harken, A.H.5    Banerjee, A.6
  • 25
    • 0028490689 scopus 로고
    • Neurocircuitry of the basal ganglia studied by monitoring neurotransmitter release. Effects of intracerebral and perinatal asphyctic lesions
    • Herrera Marschitz, M., Loidl, F., You, Z. B., Andersson, K., Silveira, R., O'Connor, W. T., and Goiny, M. (1994) Neurocircuitry of the basal ganglia studied by monitoring neurotransmitter release. Effects of intracerebral and perinatal asphyctic lesions. Mol. Neurobiol. 9, 171-182
    • (1994) Mol. Neurobiol. , vol.9 , pp. 171-182
    • Herrera Marschitz, M.1    Loidl, F.2    You, Z.B.3    Andersson, K.4    Silveira, R.5    O'Connor, W.T.6    Goiny, M.7
  • 29
    • 0000890081 scopus 로고
    • Analysis by single and double stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange
    • McMaster, G. K., and Carmichael, G. C. (1977) Analysis by single and double stranded nucleic acids on polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc. Natl. Acad. Sci. USA 74, 4835-4841
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4835-4841
    • McMaster, G.K.1    Carmichael, G.C.2
  • 30
    • 0016700864 scopus 로고
    • Detection of specific sequences among DNA fragments separated by gel electrophoresis
    • Southern, E. M. (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98, 503-511
    • (1975) J. Mol. Biol. , vol.98 , pp. 503-511
    • Southern, E.M.1
  • 31
    • 0020479426 scopus 로고
    • Cytoplasmic dot hybridization. Simple analysis of mRNA levels in multiple small cell or tissue samples
    • White, B. A., and Bancroft, F. C. (1982) Cytoplasmic dot hybridization. Simple analysis of mRNA levels in multiple small cell or tissue samples. J. Biol. Chem. 257, 8569-8575.
    • (1982) J. Biol. Chem. , vol.257 , pp. 8569-8575
    • White, B.A.1    Bancroft, F.C.2
  • 32
    • 0343763022 scopus 로고
    • Immunochemical Methods
    • Academic Press, N.Y.
    • Mayer, R. J., and Walker, J. H. (1987) Immunochemical Methods In Cell and Molecular Biology, pp. 259-276, Academic Press, N.Y.
    • (1987) Cell and Molecular Biology , pp. 259-276
    • Mayer, R.J.1    Walker, J.H.2
  • 35
    • 0029946164 scopus 로고    scopus 로고
    • Increased kynurenic acid levels and decreased kynurenine aminotransferases in patients with Down syndrome
    • Baran, H., Cairns, N., Lubec, B., and Lubec, G. (1996) Increased kynurenic acid levels and decreased kynurenine aminotransferases in patients with Down syndrome. Life Sci. 58, 1891-1899
    • (1996) Life Sci. , vol.58 , pp. 1891-1899
    • Baran, H.1    Cairns, N.2    Lubec, B.3    Lubec, G.4
  • 36
    • 0024451119 scopus 로고
    • Response to ischemia-reperfusion injury in hypertrophic heart. Role of free radical metabolic pathways
    • Batist, G., Mersereau, W., Malashenko, B. A., and Chiuc, R. C. (1989) Response to ischemia-reperfusion injury in hypertrophic heart. Role of free radical metabolic pathways. Circulation 80, 10-13
    • (1989) Circulation , vol.80 , pp. 10-13
    • Batist, G.1    Mersereau, W.2    Malashenko, B.A.3    Chiuc, R.C.4
  • 37
    • 0030210778 scopus 로고    scopus 로고
    • The hydroxyl radical: From chemistry to disease
    • Lubec, G. (1996) The hydroxyl radical: from chemistry to disease. J. Invest. Med. 44, 324-346
    • (1996) J. Invest. Med. , vol.44 , pp. 324-346
    • Lubec, G.1
  • 38
    • 0027983930 scopus 로고
    • Racemization and oxidation studies of hair protein in the homotirolensis
    • Lubec, G., Weninger, M., and Anderson, S. R. (1994) Racemization and oxidation studies of hair protein in the homotirolensis. FASEB J. 8, 1166-1169
    • (1994) FASEB J. , vol.8 , pp. 1166-1169
    • Lubec, G.1    Weninger, M.2    Anderson, S.R.3
  • 39
    • 0345104375 scopus 로고    scopus 로고
    • Evidence against the involvement of reactive oxygen species in the pathogenesis of neuronal death in Down syndrome and Alzheimer's disease
    • Hayn, M., Kremser, K., Singewald, N., Cairns, N., Nemethova, M., Lubec, B., and Lubec, G. (1996) Evidence against the involvement of reactive oxygen species in the pathogenesis of neuronal death in Down syndrome and Alzheimer's disease. Life Sci. 59, 537-544
    • (1996) Life Sci. , vol.59 , pp. 537-544
    • Hayn, M.1    Kremser, K.2    Singewald, N.3    Cairns, N.4    Nemethova, M.5    Lubec, B.6    Lubec, G.7
  • 40
    • 0029996871 scopus 로고    scopus 로고
    • Brain lipid peroxidation and hydroxyl radical attack following the intravenous infusion of hydrogen peroxide in an infant
    • Lubec, B., Hayn, M., Denk, W., and Bauer, G. (1996) Brain lipid peroxidation and hydroxyl radical attack following the intravenous infusion of hydrogen peroxide in an infant. Free Rad. Biol. Med. 21, 219-223
    • (1996) Free Rad. Biol. Med. , vol.21 , pp. 219-223
    • Lubec, B.1    Hayn, M.2    Denk, W.3    Bauer, G.4
  • 41
    • 0023201142 scopus 로고
    • Lipoperoxides in plasma as measured by liquid chromatographical separation of malondialdehyde-thiobarbituric acid adduct
    • Wong, H. Y., Knight, J. A., Hopfer, S. M., Zaharia, O., Leach, C. N., Jr., and Sunderman, F. W., Jr. (1987) Lipoperoxides in plasma as measured by liquid chromatographical separation of malondialdehyde-thiobarbituric acid adduct. Clin. Chem. 33, 214-220
    • (1987) Clin. Chem. , vol.33 , pp. 214-220
    • Wong, H.Y.1    Knight, J.A.2    Hopfer, S.M.3    Zaharia, O.4    Leach Jr., C.N.5    Sunderman Jr., F.W.6
  • 43
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quanti tation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quanti tation 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
  • 44
    • 0023505008 scopus 로고
    • Spin trapping ESR parameters of spin adducts
    • Buettner, G. R. (1987) Spin trapping ESR parameters of spin adducts. Free Rad. Biol. Med. 3, 259-303
    • (1987) Free Rad. Biol. Med. , vol.3 , pp. 259-303
    • Buettner, G.R.1
  • 45
    • 0007439615 scopus 로고
    • Subcellular distributiion of two spin trapping agents in rat heart: Possible explanation for their different protective effects against doxorubicin-induced cardiotoxicity
    • Cova, D., De Angelis, L., Monti, E., and Piccinini, F. (1992) Subcellular distributiion of two spin trapping agents in rat heart: possible explanation for their different protective effects against doxorubicin-induced cardiotoxicity. Free Rad. Res. Commun. 15, 353-360
    • (1992) Free Rad. Res. Commun. , vol.15 , pp. 353-360
    • Cova, D.1    De Angelis, L.2    Monti, E.3    Piccinini, F.4
  • 46
    • 0027998359 scopus 로고
    • Murine hepatocyte apoptosis induced in vitro and in vivo by TNF-alpha requires transcriptional arrest
    • Leist, M., Gantner, F., Bohlinger, I., Germann, P. G., Tiegs, G., and Wendel, A. (1994) Murine hepatocyte apoptosis induced in vitro and in vivo by TNF-alpha requires transcriptional arrest. J. Immunol. 153, 1778-1788
    • (1994) J. Immunol. , vol.153 , pp. 1778-1788
    • Leist, M.1    Gantner, F.2    Bohlinger, I.3    Germann, P.G.4    Tiegs, G.5    Wendel, A.6
  • 47
    • 0026022828 scopus 로고
    • Asphyctic lesion: Proliferation of tyrosine hydroxylase immunoreactive nerve cell bodies in the rat substantia nigra and functional changes in dopamine neurotransmission
    • Bjelke, B., Andersson, K., Oegren, S. O., and Bolme, P. (1991) Asphyctic lesion: proliferation of tyrosine hydroxylase immunoreactive nerve cell bodies in the rat substantia nigra and functional changes in dopamine neurotransmission. Brain Res. 543, 1-9
    • (1991) Brain Res. , vol.543 , pp. 1-9
    • Bjelke, B.1    Andersson, K.2    Oegren, S.O.3    Bolme, P.4
  • 48
    • 0030050099 scopus 로고    scopus 로고
    • + current in human and rabbit ventricular myocytes
    • + current in human and rabbit ventricular myocytes. Circ. Res. 78, 492-498
    • (1996) Circ. Res. , vol.78 , pp. 492-498
    • Hu, K.1    Duan, D.2    Li, G.R.3    Nattel, S.4
  • 49
    • 0029871273 scopus 로고    scopus 로고
    • Phorbol ester activation of chloride current in guinea pig ventricular myocytes
    • Shuba, L. M., Asai, T., and Donald, T. F. (1996) Phorbol ester activation of chloride current in guinea pig ventricular myocytes. Br. J. Pharmacol. 117, 1395-1404
    • (1996) Br. J. Pharmacol. , vol.117 , pp. 1395-1404
    • Shuba, L.M.1    Asai, T.2    Donald, T.F.3
  • 51
    • 0029878244 scopus 로고    scopus 로고
    • Regulation of gap junction channel permeability and conductance by several phosphorylating mechanisms
    • Kwak, B. R., and Jongsma, H. J. (1996) Regulation of gap junction channel permeability and conductance by several phosphorylating mechanisms. Mol. Cell Biochem. 157, 93-99
    • (1996) Mol. Cell Biochem. , vol.157 , pp. 93-99
    • Kwak, B.R.1    Jongsma, H.J.2
  • 53
    • 0026619879 scopus 로고
    • Contribution of both alpha- and beta-adrenoreceptors to the inotropic effects of catecholamines in the rabbit heart
    • Jahnel, U., Kaufmann, B., Rombusch, M., and Nawrath, H. (1992) Contribution of both alpha- and beta-adrenoreceptors to the inotropic effects of catecholamines in the rabbit heart. Naunyn Schmiedebergs Arch. Pharmacol. 346, 665-672
    • (1992) Naunyn Schmiedebergs Arch. Pharmacol. , vol.346 , pp. 665-672
    • Jahnel, U.1    Kaufmann, B.2    Rombusch, M.3    Nawrath, H.4
  • 54
    • 0026730334 scopus 로고
    • Functional effects of protein kinase C-mediated phosphorylation of chick heart muscarinic cholinergic receptors
    • Richardson, R. M., Ptasienski, J., and Hosey, N. M. (1992) Functional effects of protein kinase C-mediated phosphorylation of chick heart muscarinic cholinergic receptors. J. Biol. Chem. 267, 10127-10132
    • (1992) J. Biol. Chem. , vol.267 , pp. 10127-10132
    • Richardson, R.M.1    Ptasienski, J.2    Hosey, N.M.3
  • 55
    • 0029671256 scopus 로고    scopus 로고
    • Adenosinc A1 stimulation activates delta-protein kinase C in rat ventricular myocytes
    • Henry, P., Demolombe, S., Puceat, M., and Escande, D. (1996) Adenosinc A1 stimulation activates delta-protein kinase C in rat ventricular myocytes. Circ. Res. 78, 161-165
    • (1996) Circ. Res. , vol.78 , pp. 161-165
    • Henry, P.1    Demolombe, S.2    Puceat, M.3    Escande, D.4
  • 56
    • 0027328409 scopus 로고
    • Heat shock inhibits protein synthesis and eIF-2 activity in cultured cortical neurons
    • Fang-Ren Hu, Y.-R., Yang, Y.-B. O., and Wieloch T. (1993) Heat shock inhibits protein synthesis and eIF-2 activity in cultured cortical neurons. Neurochem. Res. 18, 1003-1007
    • (1993) Neurochem. Res. , vol.18 , pp. 1003-1007
    • Fang-Ren Hu, Y.-R.1    Yang, Y.-B.O.2    Wieloch, T.3
  • 57
    • 0022510617 scopus 로고
    • Initiation of protein synthesis in mammalian cells
    • Pain, V. M. (1986) Initiation of protein synthesis in mammalian cells. Biochem. J. 235, 625-637
    • (1986) Biochem. J. , vol.235 , pp. 625-637
    • Pain, V.M.1
  • 58
    • 0023665208 scopus 로고
    • Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis
    • Scorsone, K. A., Panniers, R., Rowlands, A. G., and Henshaw, E. C.(1987) Phosphorylation of eukaryotic initiation factor 2 during physiological stresses which affect protein synthesis. J. Biol. Chem. 262, 14538-14543
    • (1987) J. Biol. Chem. , vol.262 , pp. 14538-14543
    • Scorsone, K.A.1    Panniers, R.2    Rowlands, A.G.3    Henshaw, E.C.4
  • 59
    • 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
  • 60
    • 0028986375 scopus 로고
    • Transient changes in fos and GFAP immunoreactivity precede neuronal cell loss in the rat hippocampus following neonatal anoxia
    • Dell'Anna, E., Geloso, M. C., Draisci G., and Luthman J. (1995) Transient changes in fos and GFAP immunoreactivity precede neuronal cell loss in the rat hippocampus following neonatal anoxia. Exp. Neurol. 131, 144-156
    • (1995) Exp. Neurol. , vol.131 , pp. 144-156
    • Dell'Anna, E.1    Geloso, M.C.2    Draisci, G.3    Luthman, J.4
  • 62
    • 0024556434 scopus 로고
    • Calcium fluxes, calcium antagonists, and calcium related pathology in brain ischemia, hypoglycemia, and spreading depression: A unifying hypothesis
    • Siesjoe, B. K., and Bengtsson, F. (1989) Calcium fluxes, calcium antagonists, and calcium related pathology in brain ischemia, hypoglycemia, and spreading depression: a unifying hypothesis. J. Cereb. Blood Flow Metab. 9, 127-140
    • (1989) J. Cereb. Blood Flow Metab. , vol.9 , pp. 127-140
    • Siesjoe, B.K.1    Bengtsson, F.2
  • 63
    • 0023753142 scopus 로고
    • Calcium-mediated neurotoxicity: Relationship to specific channel types and role in ischemic damage
    • Choi, D. W. (1988) Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage. Trends Neurosci. 11, 465-469
    • (1988) Trends Neurosci. , vol.11 , pp. 465-469
    • Choi, D.W.1
  • 64
    • 0029093341 scopus 로고
    • High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP activated protein kinase inhibition of acetyl-Coa carboxylase
    • Kudo, N., Barr, A. J., Barr, R. L., Desai, S., and Lopaschuk, G. D. (1995) High rates of fatty acid oxidation during reperfusion of ischemic hearts are associated with a decrease in malonyl-CoA levels due to an increase in 5′-AMP activated protein kinase inhibition of acetyl-CoA carboxylase. J. Biol. Chem. 270, 17513-17520
    • (1995) J. Biol. Chem. , vol.270 , pp. 17513-17520
    • Kudo, N.1    Barr, A.J.2    Barr, R.L.3    Desai, S.4    Lopaschuk, G.D.5


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