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Volumn 27, Issue 3-4, 2004, Pages 373-379

Excitotoxic and post-ischemic neurodegeneration: Involvement of transglutaminases

Author keywords

Astroglial cells; Cerebellar granule neurons; Excitotoxicity; Ischemia; Neurodegenerative diseases; Transglutaminases

Indexed keywords

1 (4 AMINOPHENYL) 4 METHYL 7,8 METHYLENEDIOXY 5H 2,3 BENZODIAZEPINE; AMPA RECEPTOR ANTAGONIST; CALCIUM ION; DIZOCILPINE; GLUTAMATE RECEPTOR ANTAGONIST; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 12144255196     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-004-0117-1     Document Type: Review
Times cited : (42)

References (52)
  • 1
    • 0036323292 scopus 로고    scopus 로고
    • Increase in glutamate-induced neurotoxicity by activated astrocytes involves stimulation of protein kinase C
    • Ahlemeyer B, Kölker S, Zhu Y, Hoffmann GF, Krieglstein J (2002) Increase in glutamate-induced neurotoxicity by activated astrocytes involves stimulation of protein kinase C. J Neurochem 82: 504-515
    • (2002) J Neurochem , vol.82 , pp. 504-515
    • Ahlemeyer, B.1    Kölker, S.2    Zhu, Y.3    Hoffmann, G.F.4    Krieglstein, J.5
  • 2
    • 0036453620 scopus 로고    scopus 로고
    • Cerebrospinal fluid tissue transglutaminase as a biochemical marker for Alzheimer's disease
    • Bonelli RM, Aschoff A, Niederwieser G, Heuberger C, Jirikowski G (2002) Cerebrospinal fluid tissue transglutaminase as a biochemical marker for Alzheimer's disease. Neurobiol Dis 11: 106-110
    • (2002) Neurobiol Dis , vol.11 , pp. 106-110
    • Bonelli, R.M.1    Aschoff, A.2    Niederwieser, G.3    Heuberger, C.4    Jirikowski, G.5
  • 3
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield DA, Kanski J (2001) Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech Aging Dev 122: 945-962
    • (2001) Mech Aging Dev , vol.122 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 5
    • 0027255942 scopus 로고
    • Apoptosis and disease
    • Carson DA, Ribeiro JM (1993) Apoptosis and disease. Lancet 341: 1251-1254
    • (1993) Lancet , vol.341 , pp. 1251-1254
    • Carson, D.A.1    Ribeiro, J.M.2
  • 6
    • 0032904412 scopus 로고    scopus 로고
    • An evaluation of the role of mitochondria in neurodegenerative diseases: Mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration
    • Cassarino DS, Bennett JP Jr (1999) An evaluation of the role of mitochondria in neurodegenerative diseases: mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration. Brain Res Rev 29: 1-25
    • (1999) Brain Res Rev , vol.29 , pp. 1-25
    • Cassarino, D.S.1    Bennett Jr., J.P.2
  • 7
    • 0025823978 scopus 로고
    • Intercellular signalling in glial cells: Calcium waves and oscillations in response to mechanical stimulation and glutamate
    • Charles AC, Merrill JE, Dirksen ER, Sanderson MJ (1991) Intercellular signalling in glial cells: calcium waves and oscillations in response to mechanical stimulation and glutamate. J Neurosci 6: 983-992
    • (1991) J Neurosci , vol.6 , pp. 983-992
    • Charles, A.C.1    Merrill, J.E.2    Dirksen, E.R.3    Sanderson, M.J.4
  • 8
    • 0035794002 scopus 로고    scopus 로고
    • Oxidative stress and c-Jun-amino-terminal kinase activation involved in apoptosis of primary astrocytes induced by disulfiram-Cu(2+) complex
    • Chen SH, Liu SH, Liang YC, Lin JK, Lin-Shiau SY (2001) Oxidative stress and c-Jun-amino-terminal kinase activation involved in apoptosis of primary astrocytes induced by disulfiram-Cu(2+) complex. Eur J Pharmacol 414: 177-188
    • (2001) Eur J Pharmacol , vol.414 , pp. 177-188
    • Chen, S.H.1    Liu, S.H.2    Liang, Y.C.3    Lin, J.K.4    Lin-Shiau, S.Y.5
  • 9
    • 0026497926 scopus 로고
    • Excitotoxic cell death
    • Choi DW (1992) Excitotoxic cell death. J Neurobiol 23: 1261-1276
    • (1992) J Neurobiol , vol.23 , pp. 1261-1276
    • Choi, D.W.1
  • 10
    • 0031585857 scopus 로고    scopus 로고
    • Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells
    • Chowdhury ZA, Barsigian C, Chalupowicz GD, Bach TL, Garcia-Manero G, Martinez J ( 1997) Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells. Exp Cell Res 231: 38-49
    • (1997) Exp Cell Res , vol.231 , pp. 38-49
    • Chowdhury, Z.A.1    Barsigian, C.2    Chalupowicz, G.D.3    Bach, T.L.4    Garcia-Manero, G.5    Martinez, J.6
  • 11
    • 0036135523 scopus 로고    scopus 로고
    • Protein cross-linking, tissue transglutaminase, alternative splicing and neurodegeneration
    • Citron BA, Suo Z, SantaCruz K, Davies PJA, Qin F, Festoff BW (2002) Protein cross-linking, tissue transglutaminase, alternative splicing and neurodegeneration. Neurochem Int 40: 69-78
    • (2002) Neurochem Int , vol.40 , pp. 69-78
    • Citron, B.A.1    Suo, Z.2    SantaCruz, K.3    Davies, P.J.A.4    Qin, F.5    Festoff, B.W.6
  • 16
    • 0025277521 scopus 로고
    • Differential expression of excitatory amino acid receptor subtypes in cultured cerebellar neurons
    • Cox JA, Felder CC, Henneberry RC (1990) Differential expression of excitatory amino acid receptor subtypes in cultured cerebellar neurons. Neuron 4: 941-947
    • (1990) Neuron , vol.4 , pp. 941-947
    • Cox, J.A.1    Felder, C.C.2    Henneberry, R.C.3
  • 17
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi V, Melino G (2001) Gene disruption of tissue transglutaminase. Mol Cell Biol 21: 148-155
    • (2001) Mol Cell Biol , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 18
    • 0032967382 scopus 로고    scopus 로고
    • The role of excitotoxicity in neurodegenerative disease: Implications for therapy
    • Doble A (1999) The role of excitotoxicity in neurodegenerative disease: implications for therapy. Pharmacol Ther 81: 163-221
    • (1999) Pharmacol Ther , vol.81 , pp. 163-221
    • Doble, A.1
  • 19
    • 0032425260 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes
    • Fesus L (1998) Transglutaminase-catalyzed protein cross-linking in the molecular program of apoptosis and its relationship to neuronal processes. Cell Mol Neurobiol 18: 683-694
    • (1998) Cell Mol Neurobiol , vol.18 , pp. 683-694
    • Fesus, L.1
  • 20
    • 0032522165 scopus 로고    scopus 로고
    • Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favoured with long polyglutamine domains: A possible mechanism contributing to CAG-triplet diseases
    • Gentile V, Sepe C, Calvani M, Melone MA, Cotrufo R, Cooper AJ, Blass JP, Peluso G (1998) Tissue transglutaminase-catalyzed formation of high-molecular-weight aggregates in vitro is favoured with long polyglutamine domains: a possible mechanism contributing to CAG-triplet diseases. Arch Biochem Biophys 352: 314-321
    • (1998) Arch Biochem Biophys , vol.352 , pp. 314-321
    • Gentile, V.1    Sepe, C.2    Calvani, M.3    Melone, M.A.4    Cotrufo, R.5    Cooper, A.J.6    Blass, J.P.7    Peluso, G.8
  • 21
    • 0035980007 scopus 로고    scopus 로고
    • Evolution of transglutaminase genes: Identification of a transglutaminase gene cluster on human chromosome 15q15
    • Grènard P, Bates MK, Aeschlimann D (2001) Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. J Biol Chem 276: 33066-33078
    • (2001) J Biol Chem , vol.276 , pp. 33066-33078
    • Grènard, P.1    Bates, M.K.2    Aeschlimann, D.3
  • 22
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: Nature's biological glues. Biochem J 368: 377-396
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 23
    • 0032526361 scopus 로고    scopus 로고
    • Calcium influx via L-type voltage-gated channels mediates the delayed, elevated increases in steady-state c-fos mRNA levels in cerebellar granule cells exposed to excitotoxic levels of glutamate
    • Griffiths R, Ritchie L, Lidwell K, Grieve A, Malcolm CS, Frandsen A, Scott M, Meredith C (1998) Calcium influx via L-type voltage-gated channels mediates the delayed, elevated increases in steady-state c-fos mRNA levels in cerebellar granule cells exposed to excitotoxic levels of glutamate. J Neurosci Res 52: 641-652
    • (1998) J Neurosci Res , vol.52 , pp. 641-652
    • Griffiths, R.1    Ritchie, L.2    Lidwell, K.3    Grieve, A.4    Malcolm, C.S.5    Frandsen, A.6    Scott, M.7    Meredith, C.8
  • 24
    • 0037049234 scopus 로고    scopus 로고
    • NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells
    • Ientile R, Caccamo D, Macaione V, Torre V, Macaione S (2002) NMDA-evoked excitotoxicity increases tissue transglutaminase in cerebellar granule cells. Neuroscience 115: 723-729
    • (2002) Neuroscience , vol.115 , pp. 723-729
    • Ientile, R.1    Caccamo, D.2    Macaione, V.3    Torre, V.4    Macaione, S.5
  • 28
    • 1442348416 scopus 로고    scopus 로고
    • Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats
    • Lai TS, Tucker T, Burke JR, Strittmatter WJ, Greenberg CS (2004) Effect of tissue transglutaminase on the solubility of proteins containing expanded polyglutamine repeats. J Neurochem 88: 1253-1260
    • (2004) J Neurochem , vol.88 , pp. 1253-1260
    • Lai, T.S.1    Tucker, T.2    Burke, J.R.3    Strittmatter, W.J.4    Greenberg, C.S.5
  • 29
    • 0033789565 scopus 로고    scopus 로고
    • Free radical pathways in CNS injury
    • Lewen A, Matz P, Chan PH (2000) Free radical pathways in CNS injury. J Neurotrauma 17: 871-890
    • (2000) J Neurotrauma , vol.17 , pp. 871-890
    • Lewen, A.1    Matz, P.2    Chan, P.H.3
  • 30
    • 0032845121 scopus 로고    scopus 로고
    • Ischemic cell death in brain neurons
    • Lipton P (1999) Ischemic cell death in brain neurons. Physiol Rev 79: 1431-1536
    • (1999) Physiol Rev , vol.79 , pp. 1431-1536
    • Lipton, P.1
  • 31
    • 0036069280 scopus 로고    scopus 로고
    • AMPA receptor-mediated toxicity in oligodendrocyte progenitors involves free radical generation and activation of JNK, calpain and caspase 3
    • Liu HN, Giasson BI, Mushynski WE, Almazan G (2002) AMPA receptor-mediated toxicity in oligodendrocyte progenitors involves free radical generation and activation of JNK, calpain and caspase 3. J Neurochem 82: 398-409
    • (2002) J Neurochem , vol.82 , pp. 398-409
    • Liu, H.N.1    Giasson, B.I.2    Mushynski, W.E.3    Almazan, G.4
  • 32
    • 0036320888 scopus 로고    scopus 로고
    • Rapid subcellular redistribution of Bax precedes caspase-3 and endonuclease activation during excitotoxic neuronal apoptosis in rat brain
    • Lok J, Martin LJ (2002) Rapid subcellular redistribution of Bax precedes caspase-3 and endonuclease activation during excitotoxic neuronal apoptosis in rat brain. J Neurotrauma 19: 815-828
    • (2002) J Neurotrauma , vol.19 , pp. 815-828
    • Lok, J.1    Martin, L.J.2
  • 33
    • 0032125488 scopus 로고    scopus 로고
    • Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: A perspective on the contributions of apoptosis and necrosis
    • Martin LJ, Al-Abdulla NA, Brambrink AM, Kirsch JR, Sieber FE, Portera-Cailliau C (1998) Neurodegeneration in excitotoxicity, global cerebral ischemia, and target deprivation: A perspective on the contributions of apoptosis and necrosis. Brain Res Bull 46: 281-309
    • (1998) Brain Res Bull , vol.46 , pp. 281-309
    • Martin, L.J.1    Al-Abdulla, N.A.2    Brambrink, A.M.3    Kirsch, J.R.4    Sieber, F.E.5    Portera-Cailliau, C.6
  • 35
    • 0027049779 scopus 로고
    • Regulation of gene expression in astrocytes by excitatory amino acids
    • McNaughton LA, Hunt SP (1992) Regulation of gene expression in astrocytes by excitatory amino acids. Brain Res Mol Brain Res 16: 261-266
    • (1992) Brain Res Mol Brain Res , vol.16 , pp. 261-266
    • McNaughton, L.A.1    Hunt, S.P.2
  • 36
    • 0034065936 scopus 로고    scopus 로고
    • Glutamate as a neurotransmitter in the brain: Review of physiology and pathology
    • Meldrum BS (2000) Glutamate as a neurotransmitter in the brain: review of physiology and pathology. J Nutr 130: 1007-1015
    • (2000) J Nutr , vol.130 , pp. 1007-1015
    • Meldrum, B.S.1
  • 37
    • 0032560573 scopus 로고    scopus 로고
    • Tissue transglutaminase in cell death: A downstream or a multifunctional upstream effector?
    • Melino G, Piacentini M (1998) Tissue transglutaminase in cell death: a downstream or a multifunctional upstream effector? FEBS Lett 430: 59-63
    • (1998) FEBS Lett , vol.430 , pp. 59-63
    • Melino, G.1    Piacentini, M.2
  • 39
    • 0038641718 scopus 로고    scopus 로고
    • Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: A mechanism for maintaining tissue integrity
    • Nicholas B, Smethurst P, Verderio E, Jones R, Griffin M (2003) Cross-linking of cellular proteins by tissue transglutaminase during necrotic cell death: a mechanism for maintaining tissue integrity. Biochem J 371: 413-422
    • (2003) Biochem J , vol.371 , pp. 413-422
    • Nicholas, B.1    Smethurst, P.2    Verderio, E.3    Jones, R.4    Griffin, M.5
  • 40
    • 0022962477 scopus 로고
    • Inciting excitotoxic cytocide among central neurons
    • Olney JW (1986) Inciting excitotoxic cytocide among central neurons. Adv Exp Med Biol 203: 631-645
    • (1986) Adv Exp Med Biol , vol.203 , pp. 631-645
    • Olney, J.W.1
  • 41
    • 0025092129 scopus 로고
    • Transglutaminase activity in reversible cerebral ischemia in the rat
    • Paschen W, Röhn G, Schmidt-Kastner R (1990) Transglutaminase activity in reversible cerebral ischemia in the rat. Neurosci Lett 110: 232-236
    • (1990) Neurosci Lett , vol.110 , pp. 232-236
    • Paschen, W.1    Röhn, G.2    Schmidt-Kastner, R.3
  • 42
    • 0028927182 scopus 로고
    • Transglutaminase C in cerebellar granule neurons: Regulation and localization of substrate cross-linking
    • Perry MJ, Mahoney SA, Haynes LW (1995) Transglutaminase C in cerebellar granule neurons: regulation and localization of substrate cross-linking. Neuroscience 65: 1063-1076
    • (1995) Neuroscience , vol.65 , pp. 1063-1076
    • Perry, M.J.1    Mahoney, S.A.2    Haynes, L.W.3
  • 43
    • 0001911727 scopus 로고
    • Tissue transglutaminase in cells undergoing apoptosis
    • Tomei LD, Cope FO (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Piacentini M, Davies PJA, Fesus L (1994) Tissue transglutaminase in cells undergoing apoptosis. In: Tomei LD, Cope FO (eds) Apoptosis II: The molecular basis of apoptosis in disease. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 143-163
    • (1994) Apoptosis II: the Molecular Basis of Apoptosis in Disease , pp. 143-163
    • Piacentini, M.1    Davies, P.J.A.2    Fesus, L.3
  • 45
    • 0033562768 scopus 로고    scopus 로고
    • Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes
    • Polakowska RR, Graf BA, Falciano V, LaCelle P (1999) Transcription regulatory elements of the first intron control human transglutaminase type I gene expression in epidermal keratinocytes. J Cell Biochem 73: 355-369
    • (1999) J Cell Biochem , vol.73 , pp. 355-369
    • Polakowska, R.R.1    Graf, B.A.2    Falciano, V.3    Lacelle, P.4
  • 46
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ (2002) Alzheimer's disease is a synaptic failure. Science 298: 789-791
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 47
    • 0035798308 scopus 로고    scopus 로고
    • Cycloheximide reduces infarct volume when administered up to 6 h after mild focal ischemia in rats
    • Snider BJ, Du C, Wei L, Choi DW (2001) Cycloheximide reduces infarct volume when administered up to 6 h after mild focal ischemia in rats. Brain Res 917: 147-157
    • (2001) Brain Res , vol.917 , pp. 147-157
    • Snider, B.J.1    Du, C.2    Wei, L.3    Choi, D.W.4
  • 48
    • 0033979539 scopus 로고    scopus 로고
    • Involvement of activated caspase-3-like proteases in N-methyl-D- aspartate-induced apoptosis in cerebrocortical neurons
    • Tenneti L, Lipton SA (2000) Involvement of activated caspase-3-like proteases in N-methyl-D-aspartate-induced apoptosis in cerebrocortical neurons. J Neurochem 74: 134-142
    • (2000) J Neurochem , vol.74 , pp. 134-142
    • Tenneti, L.1    Lipton, S.A.2
  • 49
    • 0036319364 scopus 로고    scopus 로고
    • Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner
    • Tucholski J, Johnson GVW (2002) Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner. J Neurochem 81: 780-791
    • (2002) J Neurochem , vol.81 , pp. 780-791
    • Tucholski, J.1    Johnson, G.V.W.2
  • 50
    • 0034131832 scopus 로고    scopus 로고
    • Protective effect of a caspase inhibitor in models for cerebral ischemia in vitro and in vivo
    • Wiessner C, Sauer D, Alaimo D, Allegrini PR (2000) Protective effect of a caspase inhibitor in models for cerebral ischemia in vitro and in vivo. Cell Mol Biol 46: 53-62
    • (2000) Cell Mol Biol , vol.46 , pp. 53-62
    • Wiessner, C.1    Sauer, D.2    Alaimo, D.3    Allegrini, P.R.4
  • 51
    • 0029008636 scopus 로고
    • Developmental expression of N-methyl-D-aspartate (NMDA)-induced neurotoxicity, NMDA receptor function, and the NMDA-R1 and glutamate-binding protein subunits in cerebellar granule cells in primary cultures
    • Xia Y, Ragan RE, Seah EE, Michaelis ML, Michaelis EK (1995) Developmental expression of N-methyl-D-aspartate (NMDA)-induced neurotoxicity, NMDA receptor function, and the NMDA-R1 and glutamate-binding protein subunits in cerebellar granule cells in primary cultures. Neurochem Res 20: 617-629
    • (1995) Neurochem Res , vol.20 , pp. 617-629
    • Xia, Y.1    Ragan, R.E.2    Seah, E.E.3    Michaelis, M.L.4    Michaelis, E.K.5
  • 52
    • 0034881872 scopus 로고    scopus 로고
    • Ischemia-induced apoptosis in primary cultures of astrocytes
    • Yu AC, Wong HK, Yung HW, Lau LT (2001) Ischemia-induced apoptosis in primary cultures of astrocytes. Glia 35: 121-130
    • (2001) Glia , vol.35 , pp. 121-130
    • Yu, A.C.1    Wong, H.K.2    Yung, H.W.3    Lau, L.T.4


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