메뉴 건너뛰기




Volumn 213, Issue 1, 2008, Pages 145-153

Glutamate alteration of glutamic acid decarboxylase (GAD) in GABAergic neurons: The role of cysteine proteases

Author keywords

Calpain; Cathepsin; Cerebral cortex; Excitotoxicity; GABA; GAD; Glutamate; Neuron

Indexed keywords

4 AMINOBUTYRIC ACID RECEPTOR; CALCIUM ION; CALPAIN; CATHEPSIN PROTEASE; CYSTEINE PROTEINASE; GLUTAMATE DECARBOXYLASE; GLUTAMIC ACID; N ACETYLLEUCYLLEUCYLNORLEUCINAL; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEINASE; VOLTAGE GATED CALCIUM CHANNEL;

EID: 49349116481     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2008.05.013     Document Type: Article
Times cited : (23)

References (56)
  • 1
    • 0031909471 scopus 로고    scopus 로고
    • Calpain I activation in rat hippocampal neurons in culture is NMDA receptor selective and not essential for excitotoxic cell death
    • Adamec E., Beermann M.L., and Nixon R.A. Calpain I activation in rat hippocampal neurons in culture is NMDA receptor selective and not essential for excitotoxic cell death. Mol. Brain Res. 54 (1998) 35-48
    • (1998) Mol. Brain Res. , vol.54 , pp. 35-48
    • Adamec, E.1    Beermann, M.L.2    Nixon, R.A.3
  • 2
    • 33750080428 scopus 로고    scopus 로고
    • Calpain activation is required for glutamate-induced p27 down-regulation in cultured cortical neurons
    • Akashiba H., Matsuki N., and Nishiyama N. Calpain activation is required for glutamate-induced p27 down-regulation in cultured cortical neurons. J. Biol. Chem. 99 (2006) 733-744
    • (2006) J. Biol. Chem. , vol.99 , pp. 733-744
    • Akashiba, H.1    Matsuki, N.2    Nishiyama, N.3
  • 4
    • 0028929820 scopus 로고
    • Brain l-glutamate decarboxylase
    • Bao J., Cheung W.Y., and Wu J.Y. Brain l-glutamate decarboxylase. J. Biol. Chem. 270 (1995) 6464-6467
    • (1995) J. Biol. Chem. , vol.270 , pp. 6464-6467
    • Bao, J.1    Cheung, W.Y.2    Wu, J.Y.3
  • 5
    • 0346850963 scopus 로고    scopus 로고
    • Aβ-mediated activation of the apoptotic cascade in cultured cortical neurones: a role for cathepsin L
    • Boland B., and Campbell V. Aβ-mediated activation of the apoptotic cascade in cultured cortical neurones: a role for cathepsin L. Neurobiol. Aging 25 (2004) 83-91
    • (2004) Neurobiol. Aging , vol.25 , pp. 83-91
    • Boland, B.1    Campbell, V.2
  • 6
    • 0029015969 scopus 로고
    • Delayed antagonism of calpain reduces excitotoxicity in cultured neurons
    • Brorson J.R., Marcuccilli C.J., and Miller R.J. Delayed antagonism of calpain reduces excitotoxicity in cultured neurons. Stroke 26 (1995) 1259-1266
    • (1995) Stroke , vol.26 , pp. 1259-1266
    • Brorson, J.R.1    Marcuccilli, C.J.2    Miller, R.J.3
  • 8
    • 0024508256 scopus 로고
    • Experimental fluid percussion brain injury: vascular disruption and neuronal and glial alterations
    • Cortez S.C., Mcintosh T.K., and Noble L.J. Experimental fluid percussion brain injury: vascular disruption and neuronal and glial alterations. Brain Res. 482 (1989) 271-282
    • (1989) Brain Res. , vol.482 , pp. 271-282
    • Cortez, S.C.1    Mcintosh, T.K.2    Noble, L.J.3
  • 9
    • 0037108019 scopus 로고    scopus 로고
    • Glutamic acid decarboxylase 65 and 67 kDa proteins are reduced in autistic parietal and cerebellar cortices
    • Fatemi S.H., Halt A.R., Stary J.M., Kanodia R., Schultz S.C., and Realmuto G.R. Glutamic acid decarboxylase 65 and 67 kDa proteins are reduced in autistic parietal and cerebellar cortices. Biol. Psych. 52 (2002) 805-810
    • (2002) Biol. Psych. , vol.52 , pp. 805-810
    • Fatemi, S.H.1    Halt, A.R.2    Stary, J.M.3    Kanodia, R.4    Schultz, S.C.5    Realmuto, G.R.6
  • 10
    • 0028293250 scopus 로고
    • Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain
    • Figueiredo-Pereira M.E., Banik N., and Wilk S. Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: the multicatalytic proteinase complex and m-calpain. J. Neurochem. 62 (1994) 1989-1994
    • (1994) J. Neurochem. , vol.62 , pp. 1989-1994
    • Figueiredo-Pereira, M.E.1    Banik, N.2    Wilk, S.3
  • 12
    • 5344224076 scopus 로고    scopus 로고
    • Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines
    • Graber S., Maiti S., and Halpain S. Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines. Neuropharmacology 47 (2004) 706-713
    • (2004) Neuropharmacology , vol.47 , pp. 706-713
    • Graber, S.1    Maiti, S.2    Halpain, S.3
  • 13
    • 0027340070 scopus 로고
    • 2 deprivation in the central nervous system: on the mechanisms of neuronal response, differential sensitivity and injury
    • 2 deprivation in the central nervous system: on the mechanisms of neuronal response, differential sensitivity and injury. Prog. Neurobiol. 40 (1993) 277-318
    • (1993) Prog. Neurobiol. , vol.40 , pp. 277-318
    • Haddad, G.G.1    Jiang, C.2
  • 14
    • 0030756917 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIα undergo neurotoxin-induced proteolysis
    • Hajimohammadreza I., Raser K.J., Nath R., Nadimpalli R., Scott M., and Wang K.K.W. Neuronal nitric oxide synthase and calmodulin-dependent protein kinase IIα undergo neurotoxin-induced proteolysis. J. Neurochem. 69 (1997) 1006-1013
    • (1997) J. Neurochem. , vol.69 , pp. 1006-1013
    • Hajimohammadreza, I.1    Raser, K.J.2    Nath, R.3    Nadimpalli, R.4    Scott, M.5    Wang, K.K.W.6
  • 15
    • 0025021281 scopus 로고
    • Cysteine proteinase inhibitors and ras gene products share the same biological activities including transforming activity toward NIH3T3 mouse fibroblasts and the differentiation-including activity toward PC12 rat pheochromocytoma cells
    • Hiwasa T., Sawada T., and Sakiyama S. Cysteine proteinase inhibitors and ras gene products share the same biological activities including transforming activity toward NIH3T3 mouse fibroblasts and the differentiation-including activity toward PC12 rat pheochromocytoma cells. Carcinogenesis 11 (1990) 75-80
    • (1990) Carcinogenesis , vol.11 , pp. 75-80
    • Hiwasa, T.1    Sawada, T.2    Sakiyama, S.3
  • 17
    • 0025242563 scopus 로고
    • Massive increases in extracellular potassium and indiscriminate release of glutamate following concussive brain injury
    • Katayama Y., Becker D.P., Tamura T., and Hovda D.A. Massive increases in extracellular potassium and indiscriminate release of glutamate following concussive brain injury. J. Neurosurg. 73 (1990) 889-900
    • (1990) J. Neurosurg. , vol.73 , pp. 889-900
    • Katayama, Y.1    Becker, D.P.2    Tamura, T.3    Hovda, D.A.4
  • 21
    • 0026597280 scopus 로고
    • Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain
    • Litersky J.M., and Johnson G.V. Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267 (1992) 1563-1568
    • (1992) J. Biol. Chem. , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.2
  • 22
    • 0026488694 scopus 로고
    • Selective vulnerability of dentate hilar neurons following traumatic brain injury: a potential mechanistic link between head trauma and disorders of the hippocampus
    • Lowenstein D.H., Thomas M.J., Smith D.H., and Mcintosh T.K. Selective vulnerability of dentate hilar neurons following traumatic brain injury: a potential mechanistic link between head trauma and disorders of the hippocampus. J. Neurosci. 12 (1992) 4846-4853
    • (1992) J. Neurosci. , vol.12 , pp. 4846-4853
    • Lowenstein, D.H.1    Thomas, M.J.2    Smith, D.H.3    Mcintosh, T.K.4
  • 23
    • 0029827457 scopus 로고    scopus 로고
    • The rate of turnover of cortical GABA from [1-C-13]glucose is reduced in rats treated with the GABA-transaminase inhibitor vigabatrin (gamma-vinyl GABA)
    • Manor D., Rothman D.L., Mason G.F., Hyder F., Petroff O.A.C., and Behar K.L. The rate of turnover of cortical GABA from [1-C-13]glucose is reduced in rats treated with the GABA-transaminase inhibitor vigabatrin (gamma-vinyl GABA). Neurochem. Res. 21 (1996) 1031-1041
    • (1996) Neurochem. Res. , vol.21 , pp. 1031-1041
    • Manor, D.1    Rothman, D.L.2    Mason, G.F.3    Hyder, F.4    Petroff, O.A.C.5    Behar, K.L.6
  • 24
    • 34248562936 scopus 로고    scopus 로고
    • Reduced dendrite growth and altered glutamic acid decarboxylase (GAD) 65- and 67-kDa isoform protein expression from mouse cortical GABAergic neurons following excitotoxic injury in vitro
    • Monnerie H., and Le Roux P. Reduced dendrite growth and altered glutamic acid decarboxylase (GAD) 65- and 67-kDa isoform protein expression from mouse cortical GABAergic neurons following excitotoxic injury in vitro. Exp. Neurol. 205 (2007) 367-382
    • (2007) Exp. Neurol. , vol.205 , pp. 367-382
    • Monnerie, H.1    Le Roux, P.2
  • 25
    • 0027048272 scopus 로고
    • Changes in glutamic acid decarboxylase mRNA in the pallidum of the rat following unilateral damage of the striatum and overlying cortex
    • Najlerahim A., and Pearson R.C.A. Changes in glutamic acid decarboxylase mRNA in the pallidum of the rat following unilateral damage of the striatum and overlying cortex. Exp. Neurol. 118 (1992) 352-356
    • (1992) Exp. Neurol. , vol.118 , pp. 352-356
    • Najlerahim, A.1    Pearson, R.C.A.2
  • 26
    • 0026726565 scopus 로고
    • Increased expression of GAD mRNA during the chronic epileptic syndrome due to intrahippocampal tetanus toxin
    • Najlerahim A., Williams S.F., Pearson R.C.A., and Jefferys J.G.R. Increased expression of GAD mRNA during the chronic epileptic syndrome due to intrahippocampal tetanus toxin. Exp. Brain Res. 90 (1992) 332-342
    • (1992) Exp. Brain Res. , vol.90 , pp. 332-342
    • Najlerahim, A.1    Williams, S.F.2    Pearson, R.C.A.3    Jefferys, J.G.R.4
  • 28
    • 0031038166 scopus 로고    scopus 로고
    • Phosphorylation of serine residues 3, 6, 10 and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65a
    • Namchuk M., Lindsay L., Turck C.W., Kanaani J., and Baekkeskov S. Phosphorylation of serine residues 3, 6, 10 and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65a. J. Biol. Chem. 272 (1997) 1548-1557
    • (1997) J. Biol. Chem. , vol.272 , pp. 1548-1557
    • Namchuk, M.1    Lindsay, L.2    Turck, C.W.3    Kanaani, J.4    Baekkeskov, S.5
  • 29
    • 0036978932 scopus 로고    scopus 로고
    • Glutamate NMDA receptor subunit R1 and GAD mRNA expression in human temporal lobe epilepsy
    • Neder L., Valente V., and Carlotti C.G. Glutamate NMDA receptor subunit R1 and GAD mRNA expression in human temporal lobe epilepsy. Cell Mol. Neurobiol. 22 (2002) 689-698
    • (2002) Cell Mol. Neurobiol. , vol.22 , pp. 689-698
    • Neder, L.1    Valente, V.2    Carlotti, C.G.3
  • 30
    • 0035078189 scopus 로고    scopus 로고
    • The neuronal endosomal-lysosomal system in Alzheimer's disease
    • Nixon R.A., Mathews P.M., and Cataldo A.M. The neuronal endosomal-lysosomal system in Alzheimer's disease. J. Alzheimer's Dis. 3 (2001) 97-107
    • (2001) J. Alzheimer's Dis. , vol.3 , pp. 97-107
    • Nixon, R.A.1    Mathews, P.M.2    Cataldo, A.M.3
  • 31
    • 0027378804 scopus 로고
    • Loss of glutamate decarboxylase mRNA-containing neurons in the rat dentate gyrus following pilocarpine-induced seizures
    • Obenaus A., Esclapez M., and Hauser C.R. Loss of glutamate decarboxylase mRNA-containing neurons in the rat dentate gyrus following pilocarpine-induced seizures. J. Neurosci. 13 (1993) 4470-4485
    • (1993) J. Neurosci. , vol.13 , pp. 4470-4485
    • Obenaus, A.1    Esclapez, M.2    Hauser, C.R.3
  • 32
    • 0022566936 scopus 로고
    • Excitotoxic mechanisms of epileptic brain damage
    • Olney J.W., Collins R.C., and Sloviter R.S. Excitotoxic mechanisms of epileptic brain damage. Adv. Neurol. 44 (1986) 857-877
    • (1986) Adv. Neurol. , vol.44 , pp. 857-877
    • Olney, J.W.1    Collins, R.C.2    Sloviter, R.S.3
  • 33
    • 0022333159 scopus 로고
    • Selective neuronal vulnerability: morphological and molecular characteristics
    • Pulsinelli W.A. Selective neuronal vulnerability: morphological and molecular characteristics. Prog. Brain Res. 63 (1985) 29-37
    • (1985) Prog. Brain Res. , vol.63 , pp. 29-37
    • Pulsinelli, W.A.1
  • 34
    • 0018366075 scopus 로고
    • Inhibitory, GABAergic nerve terminals decrease at sites of focal epilepsy
    • Ribak C.E., Harris A.B., Vaughn J.E., and Roberts E. Inhibitory, GABAergic nerve terminals decrease at sites of focal epilepsy. Science 205 (1979) 211-214
    • (1979) Science , vol.205 , pp. 211-214
    • Ribak, C.E.1    Harris, A.B.2    Vaughn, J.E.3    Roberts, E.4
  • 35
    • 0343192494 scopus 로고    scopus 로고
    • Growth of the NMDA receptor industrial complex
    • Sheng M., and Lee S.H. Growth of the NMDA receptor industrial complex. Nat. Neurosci. 3 (2000) 633-635
    • (2000) Nat. Neurosci. , vol.3 , pp. 633-635
    • Sheng, M.1    Lee, S.H.2
  • 36
    • 0034555122 scopus 로고    scopus 로고
    • Fetal hippocampal grafts containing CA3 cells restore host hippocampal glutamate decarboxylase-positive interneuron numbers in a rat model of temporal lobe epilepsy
    • Shetty A.K., and Turner D.A. Fetal hippocampal grafts containing CA3 cells restore host hippocampal glutamate decarboxylase-positive interneuron numbers in a rat model of temporal lobe epilepsy. J. Neurosci. 20 (2000) 8788-8801
    • (2000) J. Neurosci. , vol.20 , pp. 8788-8801
    • Shetty, A.K.1    Turner, D.A.2
  • 37
    • 0024020782 scopus 로고
    • Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo
    • Siman R., and Noszek J.C. Excitatory amino acids activate calpain I and induce structural protein breakdown in vivo. Neuron 1 (1988) 279-287
    • (1988) Neuron , vol.1 , pp. 279-287
    • Siman, R.1    Noszek, J.C.2
  • 38
    • 0024363137 scopus 로고
    • Calpain I activation is specifically related to excitatory amino-acid induction of hippocampal damage
    • Siman R., Noszek J.C., and Kegerise C. Calpain I activation is specifically related to excitatory amino-acid induction of hippocampal damage. J. Neurosci. 9 (1989) 1579-1590
    • (1989) J. Neurosci. , vol.9 , pp. 1579-1590
    • Siman, R.1    Noszek, J.C.2    Kegerise, C.3
  • 40
    • 0021125255 scopus 로고
    • Calcium overload in selectively vulnerable neurons in the hippocampus during and after ischemia: and electron microscopy study in the rat
    • Simon R.P., Griffiths T., Evans M.C., Swan J.H., and Meldrum B.S. Calcium overload in selectively vulnerable neurons in the hippocampus during and after ischemia: and electron microscopy study in the rat. J. Cereb. Blood Flow Metab. 4 (1984) 350-361
    • (1984) J. Cereb. Blood Flow Metab. , vol.4 , pp. 350-361
    • Simon, R.P.1    Griffiths, T.2    Evans, M.C.3    Swan, J.H.4    Meldrum, B.S.5
  • 41
    • 0032416442 scopus 로고    scopus 로고
    • Two isoforms of glutamate decarboxylase: why?
    • Soghomonian J.-J., and Martin D.L. Two isoforms of glutamate decarboxylase: why?. TIPS 19 (1998) 500-505
    • (1998) TIPS , vol.19 , pp. 500-505
    • Soghomonian, J.-J.1    Martin, D.L.2
  • 42
    • 0024556629 scopus 로고
    • GABAergic neocortical neurons are resistant to NMDA receptor-mediated injury
    • Tecoma E.S., and Choi D.W. GABAergic neocortical neurons are resistant to NMDA receptor-mediated injury. Neurology 39 (1989) 676-682
    • (1989) Neurology , vol.39 , pp. 676-682
    • Tecoma, E.S.1    Choi, D.W.2
  • 45
    • 0025255957 scopus 로고
    • Developing selective inhibitors of calpain
    • Wang K.K.W. Developing selective inhibitors of calpain. Trends Pharmacol. Sci. 11 (1990) 139-142
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 139-142
    • Wang, K.K.W.1
  • 46
    • 33747870115 scopus 로고    scopus 로고
    • Calpain and synaptic function
    • Wu H., and Lynch D.R. Calpain and synaptic function. Mol. Neurobiol. 33 (2006) 215-236
    • (2006) Mol. Neurobiol. , vol.33 , pp. 215-236
    • Wu, H.1    Lynch, D.R.2
  • 49
    • 0034739734 scopus 로고    scopus 로고
    • Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates
    • Yamashima T. Implication of cysteine proteases calpain, cathepsin and caspase in ischemic neuronal death of primates. Prog. Neurobiol. 62 (2000) 273-295
    • (2000) Prog. Neurobiol. , vol.62 , pp. 273-295
    • Yamashima, T.1
  • 50
    • 3342900223 scopus 로고    scopus 로고
    • 2+-dependent proteases in ischemic neuronal death. A conserved 'calpain-cathepsin cascade' from nematodes to primates
    • 2+-dependent proteases in ischemic neuronal death. A conserved 'calpain-cathepsin cascade' from nematodes to primates. Cell Calcium 36 (2004) 285-293
    • (2004) Cell Calcium , vol.36 , pp. 285-293
    • Yamashima, T.1
  • 51
    • 0031817004 scopus 로고    scopus 로고
    • Inhibition of ischemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: a novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'
    • Yamashima T., Kohda Y., Tsuchiya K., Ueno T., Yamashita J., Yoshioka T., and Kominami E. Inhibition of ischemic hippocampal neuronal death in primates with cathepsin B inhibitor CA-074: a novel strategy for neuroprotection based on 'calpain-cathepsin hypothesis'. Eur. J. Neurosci. 10 (1998) 1723-1733
    • (1998) Eur. J. Neurosci. , vol.10 , pp. 1723-1733
    • Yamashima, T.1    Kohda, Y.2    Tsuchiya, K.3    Ueno, T.4    Yamashita, J.5    Yoshioka, T.6    Kominami, E.7
  • 52
    • 0242539781 scopus 로고    scopus 로고
    • Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates
    • Yamashima T., Tonchev A.B., Tsukada T., Saido T.C., Imajoh-Ohmi S., Momoi T., and Kominami E. Sustained calpain activation associated with lysosomal rupture executes necrosis of the postischemic CA1 neurons in primates. Hippocampus 13 (2003) 791-800
    • (2003) Hippocampus , vol.13 , pp. 791-800
    • Yamashima, T.1    Tonchev, A.B.2    Tsukada, T.3    Saido, T.C.4    Imajoh-Ohmi, S.5    Momoi, T.6    Kominami, E.7
  • 54
    • 0034714585 scopus 로고    scopus 로고
    • Expression of invariant chain and pro-cathepsin L in Alzheimer's brain
    • Yoshiyama Y., Arai K., Oki T., and Hattori T. Expression of invariant chain and pro-cathepsin L in Alzheimer's brain. Neurosci. Lett. 290 (2000) 125-128
    • (2000) Neurosci. Lett. , vol.290 , pp. 125-128
    • Yoshiyama, Y.1    Arai, K.2    Oki, T.3    Hattori, T.4
  • 55
    • 34249777520 scopus 로고    scopus 로고
    • M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43-3
    • Zakharov V., and Mosevitsky M.I. M-calpain-mediated cleavage of GAP-43 near Ser41 is negatively regulated by protein kinase C, calmodulin and calpain-inhibiting fragment GAP-43-3. J. Neurochem. 101 (2007) 1539-1551
    • (2007) J. Neurochem. , vol.101 , pp. 1539-1551
    • Zakharov, V.1    Mosevitsky, M.I.2
  • 56
    • 34247119196 scopus 로고    scopus 로고
    • Calpain-mediated collapsin response mediator protein-1, -2, and -4 proteolysis after neurotoxic and traumatic brain injury
    • Zhang Z., Ottens A.K., Sadasivan S., Kobeissy F.H., Fang T., Hayes R.L., and Wang K.K.W. Calpain-mediated collapsin response mediator protein-1, -2, and -4 proteolysis after neurotoxic and traumatic brain injury. J. Neurotrauma 24 (2007) 460-472
    • (2007) J. Neurotrauma , vol.24 , pp. 460-472
    • Zhang, Z.1    Ottens, A.K.2    Sadasivan, S.3    Kobeissy, F.H.4    Fang, T.5    Hayes, R.L.6    Wang, K.K.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.