메뉴 건너뛰기




Volumn 233, Issue 1, 2012, Pages 391-399

Signaling mechanisms downstream of quinolinic acid targeting the cytoskeleton of rat striatal neurons and astrocytes

Author keywords

Calcium; Cell signaling; Cyclin dependent kinase 5; Glutamate receptors; Hyperphosphorylation; Intermediate filaments; Quinolinic acid

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM CHANNEL L TYPE; CALCIUM ION; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE 5; GLIAL FIBRILLARY ACIDIC PROTEIN; GLUTAMIC ACID; INTERMEDIATE FILAMENT PROTEIN; METABOTROPIC RECEPTOR 5; N METHYL DEXTRO ASPARTIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NEUROFILAMENT M PROTEIN; NEUROFILAMENT PROTEIN; PROTEIN KINASE C; QUINOLINIC ACID;

EID: 84856208813     PISSN: 00144886     EISSN: 10902430     Source Type: Journal    
DOI: 10.1016/j.expneurol.2011.11.005     Document Type: Article
Times cited : (33)

References (93)
  • 2
    • 79953712286 scopus 로고    scopus 로고
    • Ethanol-induced modulation of synaptic output from the dorsolateral striatum in rat is regulated by cholinergic interneurons
    • Adermark L., Clarke R.B., Soderpalm B., Ericson M. Ethanol-induced modulation of synaptic output from the dorsolateral striatum in rat is regulated by cholinergic interneurons. Neurochem. Int. 2010, 58(6):693-699.
    • (2010) Neurochem. Int. , vol.58 , Issue.6 , pp. 693-699
    • Adermark, L.1    Clarke, R.B.2    Soderpalm, B.3    Ericson, M.4
  • 4
    • 0022446150 scopus 로고
    • Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid
    • Beal M.F., Kowall N.W., Ellison D.W., Mazurek M.F., Swartz K.J., Martin J.B. Replication of the neurochemical characteristics of Huntington's disease by quinolinic acid. Nature 1986, 321(6066):168-171.
    • (1986) Nature , vol.321 , Issue.6066 , pp. 168-171
    • Beal, M.F.1    Kowall, N.W.2    Ellison, D.W.3    Mazurek, M.F.4    Swartz, K.J.5    Martin, J.B.6
  • 5
    • 0033406026 scopus 로고    scopus 로고
    • Oxidative stress as a mechanism for quinolinic acid-induced hippocampal damage: protection by melatonin and deprenyl
    • Behan W.M., McDonald M., Darlington L.G., Stone T.W. Oxidative stress as a mechanism for quinolinic acid-induced hippocampal damage: protection by melatonin and deprenyl. Br. J. Pharmacol. 1999, 128(8):1754-1760.
    • (1999) Br. J. Pharmacol. , vol.128 , Issue.8 , pp. 1754-1760
    • Behan, W.M.1    McDonald, M.2    Darlington, L.G.3    Stone, T.W.4
  • 8
    • 0036703779 scopus 로고    scopus 로고
    • Deregulation of cdk5, hyperphosphorylation, and cytoskeletal pathology in the Niemann-Pick type C murine model
    • Bu B., Li J., Davies P., Vincent I. Deregulation of cdk5, hyperphosphorylation, and cytoskeletal pathology in the Niemann-Pick type C murine model. J. Neurosci. 2002, 22(15):6515-6525.
    • (2002) J. Neurosci. , vol.22 , Issue.15 , pp. 6515-6525
    • Bu, B.1    Li, J.2    Davies, P.3    Vincent, I.4
  • 9
    • 73249121300 scopus 로고    scopus 로고
    • Kynurenine Pathway Metabolites in Humans: Disease and Healthy States
    • Chen Y., Guillemin G.J. Kynurenine Pathway Metabolites in Humans: Disease and Healthy States. Int J of Trypt Res 2009, 2(1):1-19.
    • (2009) Int J of Trypt Res , vol.2 , Issue.1 , pp. 1-19
    • Chen, Y.1    Guillemin, G.J.2
  • 10
    • 0032866536 scopus 로고    scopus 로고
    • Analysis of the roles of the head domains of type IV rat neuronal intermediate filament proteins in filament assembly using domain-swapped chimeric proteins
    • Ching G.Y., Liem R.K. Analysis of the roles of the head domains of type IV rat neuronal intermediate filament proteins in filament assembly using domain-swapped chimeric proteins. J. Cell Sci. 1999, 112(Pt 13):2233-2240.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 13 , pp. 2233-2240
    • Ching, G.Y.1    Liem, R.K.2
  • 11
    • 0023876882 scopus 로고
    • Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo
    • Connick J.H., Stone T.W. Quinolinic acid effects on amino acid release from the rat cerebral cortex in vitro and in vivo. Br. J. Pharmacol. 1988, 93(4):868-876.
    • (1988) Br. J. Pharmacol. , vol.93 , Issue.4 , pp. 868-876
    • Connick, J.H.1    Stone, T.W.2
  • 12
    • 78049266301 scopus 로고    scopus 로고
    • GABA(B) receptors modulate depolarization-stimulated [(3)H]glutamate release in slices of the pars reticulata of the rat substantia nigra
    • Cortes H., Paz F., Erlij D., Aceves J., Floran B. GABA(B) receptors modulate depolarization-stimulated [(3)H]glutamate release in slices of the pars reticulata of the rat substantia nigra. Eur. J. Pharmacol. 2010, 649(1-3):161-167.
    • (2010) Eur. J. Pharmacol. , vol.649 , Issue.1-3 , pp. 161-167
    • Cortes, H.1    Paz, F.2    Erlij, D.3    Aceves, J.4    Floran, B.5
  • 13
    • 0016804523 scopus 로고
    • Synthetic substrate for cyclic AMP-dependent protein kinase
    • Daile P., Carnegie P.R., Young J.D. Synthetic substrate for cyclic AMP-dependent protein kinase. Nature 1975, 257(5525):416-418.
    • (1975) Nature , vol.257 , Issue.5525 , pp. 416-418
    • Daile, P.1    Carnegie, P.R.2    Young, J.D.3
  • 14
    • 0036316279 scopus 로고    scopus 로고
    • Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases
    • Dashiell S.M., Tanner S.L., Pant H.C., Quarles R.H. Myelin-associated glycoprotein modulates expression and phosphorylation of neuronal cytoskeletal elements and their associated kinases. J. Neurochem. 2002, 81(6):1263-1272.
    • (2002) J. Neurochem. , vol.81 , Issue.6 , pp. 1263-1272
    • Dashiell, S.M.1    Tanner, S.L.2    Pant, H.C.3    Quarles, R.H.4
  • 15
    • 0342468278 scopus 로고    scopus 로고
    • The endogenous agonist quinolinic acid and the non endogenous homoquinolinic acid discriminate between NMDAR2 receptor subunits
    • de Carvalho L.P., Bochet P., Rossier J. The endogenous agonist quinolinic acid and the non endogenous homoquinolinic acid discriminate between NMDAR2 receptor subunits. Neurochem. Int. 1996, 28(4):445-452.
    • (1996) Neurochem. Int. , vol.28 , Issue.4 , pp. 445-452
    • de Carvalho, L.P.1    Bochet, P.2    Rossier, J.3
  • 16
    • 35748946053 scopus 로고    scopus 로고
    • Arsenic inhibits neurofilament transport and induces perikaryal accumulation of phosphorylated neurofilaments: roles of JNK and GSK-3beta
    • DeFuria J., Shea T.B. Arsenic inhibits neurofilament transport and induces perikaryal accumulation of phosphorylated neurofilaments: roles of JNK and GSK-3beta. Brain Res. 2007, 1181:74-82.
    • (2007) Brain Res. , vol.1181 , pp. 74-82
    • DeFuria, J.1    Shea, T.B.2
  • 17
    • 4444382866 scopus 로고    scopus 로고
    • Permissive role of adenosine A2A receptors on metabotropic glutamate receptor 5 (mGluR5)-mediated effects in the striatum
    • Domenici M.R., Pepponi R., Martire A., Tebano M.T., Potenza R.L., Popoli P. Permissive role of adenosine A2A receptors on metabotropic glutamate receptor 5 (mGluR5)-mediated effects in the striatum. J. Neurochem. 2004, 90(5):1276-1279.
    • (2004) J. Neurochem. , vol.90 , Issue.5 , pp. 1276-1279
    • Domenici, M.R.1    Pepponi, R.2    Martire, A.3    Tebano, M.T.4    Potenza, R.L.5    Popoli, P.6
  • 18
    • 0034305621 scopus 로고    scopus 로고
    • Glial fibrillary acidic protein: GFAP-thirty-one years (1969-2000)
    • Eng L.F., Ghirnikar R.S., Lee Y.L. Glial fibrillary acidic protein: GFAP-thirty-one years (1969-2000). Neurochem. Res. 2000, 25(9-10):1439-1451.
    • (2000) Neurochem. Res. , vol.25 , Issue.9-10 , pp. 1439-1451
    • Eng, L.F.1    Ghirnikar, R.S.2    Lee, Y.L.3
  • 19
    • 38949103036 scopus 로고    scopus 로고
    • Excitotoxic neuronal death and the pathogenesis of Huntington's disease
    • Estrada Sanchez A.M., Mejia-Toiber J., Massieu L. Excitotoxic neuronal death and the pathogenesis of Huntington's disease. Arch. Med. Res. 2008, 39(3):265-276.
    • (2008) Arch. Med. Res. , vol.39 , Issue.3 , pp. 265-276
    • Estrada Sanchez, A.M.1    Mejia-Toiber, J.2    Massieu, L.3
  • 20
    • 0028283501 scopus 로고
    • Intermediate filaments: structure, dynamics, function, and disease
    • Fuchs E., Weber K. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 1994, 63:345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 21
    • 0036460139 scopus 로고    scopus 로고
    • Synaptic localization of GABA(A) receptor subunits in the substantia nigra of the rat: effects of quinolinic acid lesions of the striatum
    • Fujiyama F., Stephenson F.A., Bolam J.P. Synaptic localization of GABA(A) receptor subunits in the substantia nigra of the rat: effects of quinolinic acid lesions of the striatum. Eur J Neurosci 2002, 15(12):1961-1975.
    • (2002) Eur J Neurosci , vol.15 , Issue.12 , pp. 1961-1975
    • Fujiyama, F.1    Stephenson, F.A.2    Bolam, J.P.3
  • 22
    • 0346219384 scopus 로고    scopus 로고
    • Alpha-keto-beta-methylvaleric acid increases the in vitro phosphorylation of intermediate filaments in cerebral cortex of young rats through the gabaergic system
    • Funchal C., Dall Bello Pessutto F., de Almeida L.M., de Lima Pelaez P., Loureiro S.O., Vivian L., Wajner M., Pessoa-Pureur R. Alpha-keto-beta-methylvaleric acid increases the in vitro phosphorylation of intermediate filaments in cerebral cortex of young rats through the gabaergic system. J. Neurol. Sci. 2004, 217(1):17-24.
    • (2004) J. Neurol. Sci. , vol.217 , Issue.1 , pp. 17-24
    • Funchal, C.1    Dall Bello Pessutto, F.2    de Almeida, L.M.3    de Lima, P.P.4    Loureiro, S.O.5    Vivian, L.6    Wajner, M.7    Pessoa-Pureur, R.8
  • 26
    • 0023653418 scopus 로고
    • Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H
    • Geisler N., Vandekerckhove J., Weber K. Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H. FEBS Lett. 1987, 221(2):403-407.
    • (1987) FEBS Lett. , vol.221 , Issue.2 , pp. 403-407
    • Geisler, N.1    Vandekerckhove, J.2    Weber, K.3
  • 27
    • 0025107358 scopus 로고
    • Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit
    • Gill S.R., Wong P.C., Monteiro M.J., Cleveland D.W. Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit. J. Cell Biol. 1990, 111(5 Pt 1):2005-2019.
    • (1990) J. Cell Biol. , vol.111 , Issue.5 PART 1 , pp. 2005-2019
    • Gill, S.R.1    Wong, P.C.2    Monteiro, M.J.3    Cleveland, D.W.4
  • 28
    • 0034433275 scopus 로고    scopus 로고
    • Neurofilament protein synthesis and phosphorylation
    • Grant P., Pant H.C. Neurofilament protein synthesis and phosphorylation. J. Neurocytol. 2000, 29(11-12):843-872.
    • (2000) J. Neurocytol. , vol.29 , Issue.11-12 , pp. 843-872
    • Grant, P.1    Pant, H.C.2
  • 30
    • 0027763184 scopus 로고
    • The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation
    • Heins S., Wong P.C., Muller S., Goldie K., Cleveland D.W., Aebi U. The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation. J. Cell Biol. 1993, 123(6 Pt 1):1517-1533.
    • (1993) J. Cell Biol. , vol.123 , Issue.6 PART 1 , pp. 1517-1533
    • Heins, S.1    Wong, P.C.2    Muller, S.3    Goldie, K.4    Cleveland, D.W.5    Aebi, U.6
  • 31
    • 0025220189 scopus 로고
    • Effects of phosphorylation of the neurofilament L protein on filamentous structures
    • Hisanaga S., Gonda Y., Inagaki M., Ikai A., Hirokawa N. Effects of phosphorylation of the neurofilament L protein on filamentous structures. Cell Regul. 1990, 1(2):237-248.
    • (1990) Cell Regul. , vol.1 , Issue.2 , pp. 237-248
    • Hisanaga, S.1    Gonda, Y.2    Inagaki, M.3    Ikai, A.4    Hirokawa, N.5
  • 32
    • 0348010572 scopus 로고    scopus 로고
    • The regulation of cyclin-dependent kinase 5 activity through the metabolism of p35 or p39 Cdk5 activator
    • Hisanaga S., Saito T. The regulation of cyclin-dependent kinase 5 activity through the metabolism of p35 or p39 Cdk5 activator. Neurosignals 2003, 12(4-5):221-229.
    • (2003) Neurosignals , vol.12 , Issue.4-5 , pp. 221-229
    • Hisanaga, S.1    Saito, T.2
  • 33
    • 0344625369 scopus 로고    scopus 로고
    • Characterization of the phosphorylation sites of human high molecular weight neurofilament protein by electrospray ionization tandem mass spectrometry and database searching
    • Jaffe H., Veeranna Shetty K.T., Pant H.C. Characterization of the phosphorylation sites of human high molecular weight neurofilament protein by electrospray ionization tandem mass spectrometry and database searching. Biochemistry 1998, 37(11):3931-3940.
    • (1998) Biochemistry , vol.37 , Issue.11 , pp. 3931-3940
    • Jaffe, H.1    Veeranna, S.K.T.2    Pant, H.C.3
  • 34
    • 78149408231 scopus 로고    scopus 로고
    • Comparative neuroprotective profile of statins in quinolinic acid induced neurotoxicity in rats
    • Kalonia H., Kumar P., Kumar A. Comparative neuroprotective profile of statins in quinolinic acid induced neurotoxicity in rats. Behav. Brain Res. 2011, 216(1):220-228.
    • (2011) Behav. Brain Res. , vol.216 , Issue.1 , pp. 220-228
    • Kalonia, H.1    Kumar, P.2    Kumar, A.3
  • 35
    • 77953706084 scopus 로고    scopus 로고
    • Pioglitazone ameliorates behavioral, biochemical and cellular alterations in quinolinic acid induced neurotoxicity: possible role of peroxisome proliferator activated receptor-Upsilon (PPARUpsilon) in Huntington's disease
    • Kalonia H., Kumar P., Kumar A. Pioglitazone ameliorates behavioral, biochemical and cellular alterations in quinolinic acid induced neurotoxicity: possible role of peroxisome proliferator activated receptor-Upsilon (PPARUpsilon) in Huntington's disease. Pharmacol. Biochem. Behav. 2011, 96(2):115-124.
    • (2011) Pharmacol. Biochem. Behav. , vol.96 , Issue.2 , pp. 115-124
    • Kalonia, H.1    Kumar, P.2    Kumar, A.3
  • 36
    • 49549088593 scopus 로고    scopus 로고
    • The Notch signaling inhibitor DAPT down-regulates cdk5 activity and modulates the distribution of neuronal cytoskeletal proteins
    • Kanungo J., Zheng Y.L., Amin N.D., Pant H.C. The Notch signaling inhibitor DAPT down-regulates cdk5 activity and modulates the distribution of neuronal cytoskeletal proteins. J. Neurochem. 2008, 106(5):2236-2248.
    • (2008) J. Neurochem. , vol.106 , Issue.5 , pp. 2236-2248
    • Kanungo, J.1    Zheng, Y.L.2    Amin, N.D.3    Pant, H.C.4
  • 37
    • 58649108307 scopus 로고    scopus 로고
    • Neuronal injury induces cytokine-induced neutrophil chemoattractant-1 (CINC-1) production in astrocytes
    • Katayama T., Tanaka H., Yoshida T., Uehara T., Minami M. Neuronal injury induces cytokine-induced neutrophil chemoattractant-1 (CINC-1) production in astrocytes. J. Pharmacol. Sci. 2009, 109(1):88-93.
    • (2009) J. Pharmacol. Sci. , vol.109 , Issue.1 , pp. 88-93
    • Katayama, T.1    Tanaka, H.2    Yoshida, T.3    Uehara, T.4    Minami, M.5
  • 39
    • 34347374872 scopus 로고    scopus 로고
    • Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm
    • Kim S., Coulombe P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 2007, 21(13):1581-1597.
    • (2007) Genes Dev. , vol.21 , Issue.13 , pp. 1581-1597
    • Kim, S.1    Coulombe, P.A.2
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0348011603 scopus 로고    scopus 로고
    • Functions of intermediate filaments in neuronal development and disease
    • Lariviere R.C., Julien J.P. Functions of intermediate filaments in neuronal development and disease. J. Neurobiol. 2004, 58(1):131-148.
    • (2004) J. Neurobiol. , vol.58 , Issue.1 , pp. 131-148
    • Lariviere, R.C.1    Julien, J.P.2
  • 42
    • 0242273897 scopus 로고    scopus 로고
    • Calcium-dependent phosphorylation of glial fibrillary acidic protein (GFAP) in the rat hippocampus: a comparison of the kinase/phosphatase balance in immature and mature slices using tryptic phosphopeptide mapping
    • Leal R.B., Goncalves C.A., Rodnight R. Calcium-dependent phosphorylation of glial fibrillary acidic protein (GFAP) in the rat hippocampus: a comparison of the kinase/phosphatase balance in immature and mature slices using tryptic phosphopeptide mapping. Brain Res. Dev. Brain Res. 1997, 104(1-2):1-10.
    • (1997) Brain Res. Dev. Brain Res. , vol.104 , Issue.1-2 , pp. 1-10
    • Leal, R.B.1    Goncalves, C.A.2    Rodnight, R.3
  • 44
    • 0033000687 scopus 로고    scopus 로고
    • Calcium influx and membrane depolarization induce phosphorylation of neurofilament (NF-M) KSP repeats in PC12 cells
    • Li B.S., Veeranna Grant P., Pant H.C. Calcium influx and membrane depolarization induce phosphorylation of neurofilament (NF-M) KSP repeats in PC12 cells. Brain Res. Mol. Brain Res. 1999, 70(1):84-91.
    • (1999) Brain Res. Mol. Brain Res. , vol.70 , Issue.1 , pp. 84-91
    • Li, B.S.1    Veeranna, G.P.2    Pant, H.C.3
  • 45
    • 0033563176 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases (Erk1 and Erk2) cascade results in phosphorylation of NF-M tail domains in transfected NIH 3T3 cells
    • Li B.S., Veeranna J.G., Grant P., Pant H.C. Activation of mitogen-activated protein kinases (Erk1 and Erk2) cascade results in phosphorylation of NF-M tail domains in transfected NIH 3T3 cells. Eur J Biochem 1999, 262:211-217.
    • (1999) Eur J Biochem , vol.262 , pp. 211-217
    • Li, B.S.1    Veeranna, J.G.2    Grant, P.3    Pant, H.C.4
  • 46
    • 0034663040 scopus 로고    scopus 로고
    • Integrin alpha(1) beta(1)-mediated activation of cyclin-dependent kinase 5 activity is involved in neurite outgrowth and human neurofilament protein H Lys-Ser-Pro tail domain phosphorylation
    • Li B.S., Zhang L., Gu J., Amin N.D., Pant H.C. Integrin alpha(1) beta(1)-mediated activation of cyclin-dependent kinase 5 activity is involved in neurite outgrowth and human neurofilament protein H Lys-Ser-Pro tail domain phosphorylation. J. Neurosci. 2000, 20:6055-6062.
    • (2000) J. Neurosci. , vol.20 , pp. 6055-6062
    • Li, B.S.1    Zhang, L.2    Gu, J.3    Amin, N.D.4    Pant, H.C.5
  • 47
    • 0036469286 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 prevents neuronal apoptosis by negative regulation of c-Jun N-terminal kinase 3
    • Li B.S., Zhang L., Takahashi S., Ma W., Jaffe H., Kulkarni A.B., Pant H.C. Cyclin-dependent kinase 5 prevents neuronal apoptosis by negative regulation of c-Jun N-terminal kinase 3. EMBO J. 2002, 21(3):324-333.
    • (2002) EMBO J. , vol.21 , Issue.3 , pp. 324-333
    • Li, B.S.1    Zhang, L.2    Takahashi, S.3    Ma, W.4    Jaffe, H.5    Kulkarni, A.B.6    Pant, H.C.7
  • 48
    • 0030852948 scopus 로고    scopus 로고
    • Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction
    • Liu Y., Peterson D.A., Kimura H., Schubert D. Mechanism of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction. J. Neurochem. 1997, 69(2):581-593.
    • (1997) J. Neurochem. , vol.69 , Issue.2 , pp. 581-593
    • Liu, Y.1    Peterson, D.A.2    Kimura, H.3    Schubert, D.4
  • 49
    • 20444461673 scopus 로고    scopus 로고
    • Propionic and methylmalonic acids increase cAMP levels in slices of cerebral cortex of young rats via adrenergic and glutamatergic mechanisms
    • Loureiro S.O., de Lima Pelaez P., Heimfarth L., Souza D.O., Wajner M., Pessoa-Pureur R. Propionic and methylmalonic acids increase cAMP levels in slices of cerebral cortex of young rats via adrenergic and glutamatergic mechanisms. Biochim. Biophys. Acta 2005, 1740(3):460-466.
    • (2005) Biochim. Biophys. Acta , vol.1740 , Issue.3 , pp. 460-466
    • Loureiro, S.O.1    de Lima, P.P.2    Heimfarth, L.3    Souza, D.O.4    Wajner, M.5    Pessoa-Pureur, R.6
  • 53
    • 33646257802 scopus 로고    scopus 로고
    • Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: regulation by multiple phosphorylation events
    • Motil J., Chan W.K., Dubey M., Chaudhury P., Pimenta A., Chylinski T.M., Ortiz D.T., Shea T.B. Dynein mediates retrograde neurofilament transport within axons and anterograde delivery of NFs from perikarya into axons: regulation by multiple phosphorylation events. Cell Motil. Cytoskeleton 2006, 63:266-286.
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 266-286
    • Motil, J.1    Chan, W.K.2    Dubey, M.3    Chaudhury, P.4    Pimenta, A.5    Chylinski, T.M.6    Ortiz, D.T.7    Shea, T.B.8
  • 54
    • 0027531842 scopus 로고
    • The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology
    • Nixon R.A. The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology. Brain Pathol. 1993, 3(1):29-38.
    • (1993) Brain Pathol. , vol.3 , Issue.1 , pp. 29-38
    • Nixon, R.A.1
  • 55
    • 0025943790 scopus 로고
    • Neurofilament phosphorylation: a new look at regulation and function
    • Nixon R.A., Sihag R.K. Neurofilament phosphorylation: a new look at regulation and function. Trends Neurosci. 1991, 14(11):501-506.
    • (1991) Trends Neurosci. , vol.14 , Issue.11 , pp. 501-506
    • Nixon, R.A.1    Sihag, R.K.2
  • 56
    • 33745873555 scopus 로고    scopus 로고
    • "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights
    • Omary M.B., Ku N.O., Tao G.Z., Toivola D.M., Liao J. "Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem. Sci. 2006, 31(7):383-394.
    • (2006) Trends Biochem. Sci. , vol.31 , Issue.7 , pp. 383-394
    • Omary, M.B.1    Ku, N.O.2    Tao, G.Z.3    Toivola, D.M.4    Liao, J.5
  • 57
    • 0035157216 scopus 로고    scopus 로고
    • The role of group I and group II metabotropic glutamate receptors in modulation of striatal NMDA and quinolinic acid toxicity
    • Orlando L.R., Alsdorf S.A., Penney J.B., Young A.B. The role of group I and group II metabotropic glutamate receptors in modulation of striatal NMDA and quinolinic acid toxicity. Exp. Neurol. 2001, 167(1):196-204.
    • (2001) Exp. Neurol. , vol.167 , Issue.1 , pp. 196-204
    • Orlando, L.R.1    Alsdorf, S.A.2    Penney, J.B.3    Young, A.B.4
  • 58
    • 0343036220 scopus 로고    scopus 로고
    • Phosphorylation of human high molecular weight neurofilament protein (hNF-H) by neuronal cyclin-dependent kinase 5 (cdk5)
    • Pant A.C., Veeranna Pant H.C., Amin N. Phosphorylation of human high molecular weight neurofilament protein (hNF-H) by neuronal cyclin-dependent kinase 5 (cdk5). Brain Res. 1997, 765(2):259-266.
    • (1997) Brain Res. , vol.765 , Issue.2 , pp. 259-266
    • Pant, A.C.1    Veeranna, P.H.C.2    Amin, N.3
  • 59
    • 0036712430 scopus 로고    scopus 로고
    • Beyond structure: do intermediate filaments modulate cell signalling?
    • Paramio J.M., Jorcano J.L. Beyond structure: do intermediate filaments modulate cell signalling?. Bioessays 2002, 24(9):836-844.
    • (2002) Bioessays , vol.24 , Issue.9 , pp. 836-844
    • Paramio, J.M.1    Jorcano, J.L.2
  • 61
    • 77953700414 scopus 로고    scopus 로고
    • Acute intrastriatal administration of quinolinic acid provokes hyperphosphorylation of cytoskeletal intermediate filament proteins in astrocytes and neurons of rats
    • Pierozan P., Zamoner A., Soska A.K., Silvestrin R.B., Loureiro S.O., Heimfarth L., Mello e Souza T., Wajner M., Pessoa-Pureur R. Acute intrastriatal administration of quinolinic acid provokes hyperphosphorylation of cytoskeletal intermediate filament proteins in astrocytes and neurons of rats. Exp. Neurol. 2010, 224(1):188-196.
    • (2010) Exp. Neurol. , vol.224 , Issue.1 , pp. 188-196
    • Pierozan, P.1    Zamoner, A.2    Soska, A.K.3    Silvestrin, R.B.4    Loureiro, S.O.5    Heimfarth, L.6    Mello e Souza, T.7    Wajner, M.8    Pessoa-Pureur, R.9
  • 62
    • 79751475463 scopus 로고    scopus 로고
    • Gamma-Aminobutyric acid type B receptor changes in the rat striatum and substantia nigra following intrastriatal quinolinic acid lesions
    • Rekik L., Daguin-Nerriere V., Petit J.Y., Brachet P. gamma-Aminobutyric acid type B receptor changes in the rat striatum and substantia nigra following intrastriatal quinolinic acid lesions. J Neurosci Res 2011, 89(4):524-535.
    • (2011) J Neurosci Res , vol.89 , Issue.4 , pp. 524-535
    • Rekik, L.1    Daguin-Nerriere, V.2    Petit, J.Y.3    Brachet, P.4
  • 63
    • 78649281822 scopus 로고    scopus 로고
    • Group I metabotropic glutamate receptor signalling and its implication in neurological disease
    • Ribeiro F.M., Paquet M., Cregan S.P., Ferguson S.S. Group I metabotropic glutamate receptor signalling and its implication in neurological disease. CNS Neurol. Disord. Drug Targets 2010, 9(5):574-595.
    • (2010) CNS Neurol. Disord. Drug Targets , vol.9 , Issue.5 , pp. 574-595
    • Ribeiro, F.M.1    Paquet, M.2    Cregan, S.P.3    Ferguson, S.S.4
  • 65
    • 0025936872 scopus 로고
    • Quinolinic acid is a potent lipid peroxidant in rat brain homogenates
    • Rios C., Santamaria A. Quinolinic acid is a potent lipid peroxidant in rat brain homogenates. Neurochem. Res. 1991, 16(10):1139-1143.
    • (1991) Neurochem. Res. , vol.16 , Issue.10 , pp. 1139-1143
    • Rios, C.1    Santamaria, A.2
  • 67
    • 0036784518 scopus 로고    scopus 로고
    • Manipulation of brain kynurenines: glial targets, neuronal effects, and clinical opportunities
    • Schwarcz R., Pellicciari R. Manipulation of brain kynurenines: glial targets, neuronal effects, and clinical opportunities. J. Pharmacol. Exp. Ther. 2002, 303(1):1-10.
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , Issue.1 , pp. 1-10
    • Schwarcz, R.1    Pellicciari, R.2
  • 68
    • 0006145378 scopus 로고    scopus 로고
    • Ryanodine binding sites on the sarcoplasmic reticulum Ca2C release channel
    • R. Sitsapesan, A.J. Willaims (Eds.)
    • Serysheva I.I., Hamilton S.L. Ryanodine binding sites on the sarcoplasmic reticulum Ca2C release channel. Structure and Function of Ryanodine Receptors 1998, 95-104. R. Sitsapesan, A.J. Willaims (Eds.).
    • (1998) Structure and Function of Ryanodine Receptors , pp. 95-104
    • Serysheva, I.I.1    Hamilton, S.L.2
  • 69
    • 0037146705 scopus 로고    scopus 로고
    • Insulin-like growth factor-I inhibits endogenous acetylcholine release from the rat hippocampal formation: possible involvement of GABA in mediating the effects
    • Seto D., Zheng W.H., McNicoll A., Collier B., Quirion R., Kar S. Insulin-like growth factor-I inhibits endogenous acetylcholine release from the rat hippocampal formation: possible involvement of GABA in mediating the effects. Neuroscience 2002, 115(2):603-612.
    • (2002) Neuroscience , vol.115 , Issue.2 , pp. 603-612
    • Seto, D.1    Zheng, W.H.2    McNicoll, A.3    Collier, B.4    Quirion, R.5    Kar, S.6
  • 71
    • 42049107093 scopus 로고    scopus 로고
    • Regulation of neurofilament dynamics by phosphorylation
    • Shea T.B., Chan W.K. Regulation of neurofilament dynamics by phosphorylation. Eur. J. Neurosci. 2008, 27(8):1893-1901.
    • (2008) Eur. J. Neurosci. , vol.27 , Issue.8 , pp. 1893-1901
    • Shea, T.B.1    Chan, W.K.2
  • 72
    • 2642524580 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 increases perikaryal neurofilament phosphorylation and inhibits neurofilament axonal transport in response to oxidative stress
    • Shea T.B., Zheng Y.L., Ortiz D., Pant H.C. Cyclin-dependent kinase 5 increases perikaryal neurofilament phosphorylation and inhibits neurofilament axonal transport in response to oxidative stress. J. Neurosci. Res. 2004, 76(6):795-800.
    • (2004) J. Neurosci. Res. , vol.76 , Issue.6 , pp. 795-800
    • Shea, T.B.1    Zheng, Y.L.2    Ortiz, D.3    Pant, H.C.4
  • 73
    • 34249714850 scopus 로고    scopus 로고
    • Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments
    • Sihag R.K., Inagaki M., Yamaguchi T., Shea T.B., Pant H.C. Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments. Exp. Cell Res. 2007, 313(10):2098-2109.
    • (2007) Exp. Cell Res. , vol.313 , Issue.10 , pp. 2098-2109
    • Sihag, R.K.1    Inagaki, M.2    Yamaguchi, T.3    Shea, T.B.4    Pant, H.C.5
  • 74
    • 0024531851 scopus 로고
    • In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases
    • Sihag R.K., Nixon R.A. In vivo phosphorylation of distinct domains of the 70-kilodalton neurofilament subunit involves different protein kinases. J. Biol. Chem. 1989, 264(1):457-464.
    • (1989) J. Biol. Chem. , vol.264 , Issue.1 , pp. 457-464
    • Sihag, R.K.1    Nixon, R.A.2
  • 76
    • 26244468293 scopus 로고    scopus 로고
    • Adenylyl cyclase type-VIII activity is regulated by G(betagamma) subunits
    • Steiner D., Saya D., Schallmach E., Simonds W.F., Vogel Z. Adenylyl cyclase type-VIII activity is regulated by G(betagamma) subunits. Cell. Signal. 2006, 18(1):62-68.
    • (2006) Cell. Signal. , vol.18 , Issue.1 , pp. 62-68
    • Steiner, D.1    Saya, D.2    Schallmach, E.3    Simonds, W.F.4    Vogel, Z.5
  • 77
    • 0027486072 scopus 로고
    • Neuropharmacology of quinolinic and kynurenic acids
    • Stone T.W. Neuropharmacology of quinolinic and kynurenic acids. Pharmacol. Rev. 1993, 45(3):309-379.
    • (1993) Pharmacol. Rev. , vol.45 , Issue.3 , pp. 309-379
    • Stone, T.W.1
  • 78
    • 0019440926 scopus 로고
    • Quinolinic acid: a potent endogenous excitant at amino acid receptors in CNS
    • Stone T.W., Perkins M.N. Quinolinic acid: a potent endogenous excitant at amino acid receptors in CNS. Eur. J. Pharmacol. 1981, 72(4):411-412.
    • (1981) Eur. J. Pharmacol. , vol.72 , Issue.4 , pp. 411-412
    • Stone, T.W.1    Perkins, M.N.2
  • 79
    • 0035951789 scopus 로고    scopus 로고
    • 2+-dependent cell signaling through calmodulin-activated protein phosphatase and protein kinases minireview series
    • 2+-dependent cell signaling through calmodulin-activated protein phosphatase and protein kinases minireview series. J. Biol. Chem. 2001, 276(4):2311-2312.
    • (2001) J. Biol. Chem. , vol.276 , Issue.4 , pp. 2311-2312
    • Stull, J.T.1
  • 80
    • 17544370807 scopus 로고    scopus 로고
    • Phosphorylation of the high molecular weight neurofilament protein (NF-H) by Cdk5 and p35
    • Sun D., Leung C.L., Liem R.K. Phosphorylation of the high molecular weight neurofilament protein (NF-H) by Cdk5 and p35. J. Biol. Chem. 1996, 271(24):14245-14251.
    • (1996) J. Biol. Chem. , vol.271 , Issue.24 , pp. 14245-14251
    • Sun, D.1    Leung, C.L.2    Liem, R.K.3
  • 81
    • 77549083577 scopus 로고    scopus 로고
    • Calcium, ischemia and excitotoxicity
    • Szydlowska K., Tymianski M. Calcium, ischemia and excitotoxicity. Cell Calcium 2010, 47(2):122-129.
    • (2010) Cell Calcium , vol.47 , Issue.2 , pp. 122-129
    • Szydlowska, K.1    Tymianski, M.2
  • 83
    • 0036546687 scopus 로고    scopus 로고
    • Cdk5/p35 regulates neurotransmitter release through phosphorylation and downregulation of P/Q-type voltage-dependent calcium channel activity
    • Tomizawa K., Ohta J., Matsushita M., Moriwaki A., Li S.T., Takei K., Matsui H. Cdk5/p35 regulates neurotransmitter release through phosphorylation and downregulation of P/Q-type voltage-dependent calcium channel activity. J. Neurosci. 2002, 22(7):2590-2597.
    • (2002) J. Neurosci. , vol.22 , Issue.7 , pp. 2590-2597
    • Tomizawa, K.1    Ohta, J.2    Matsushita, M.3    Moriwaki, A.4    Li, S.T.5    Takei, K.6    Matsui, H.7
  • 85
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax J.A., Ferrell J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 2007, 8(7):530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.7 , pp. 530-541
    • Ubersax, J.A.1    Ferrell, J.E.2
  • 86
    • 0032100631 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M
    • Veeranna Amin N.D., Ahn N.G., Jaffe H., Winters C.A., Grant P., Pant H.C. Mitogen-activated protein kinases (Erk1,2) phosphorylate Lys-Ser-Pro (KSP) repeats in neurofilament proteins NF-H and NF-M. J. Neurosci. 1998, 18(11):4008-4021.
    • (1998) J. Neurosci. , vol.18 , Issue.11 , pp. 4008-4021
    • Veeranna, A.N.D.1    Ahn, N.G.2    Jaffe, H.3    Winters, C.A.4    Grant, P.5    Pant, H.C.6
  • 87
    • 1842610852 scopus 로고    scopus 로고
    • Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5
    • Wang Q., Walsh D.M., Rowan M.J., Selkoe D.J., Anwyl R. Block of long-term potentiation by naturally secreted and synthetic amyloid beta-peptide in hippocampal slices is mediated via activation of the kinases c-Jun N-terminal kinase, cyclin-dependent kinase 5, and p38 mitogen-activated protein kinase as well as metabotropic glutamate receptor type 5. J. Neurosci. 2004, 24(13):3370-3378.
    • (2004) J. Neurosci. , vol.24 , Issue.13 , pp. 3370-3378
    • Wang, Q.1    Walsh, D.M.2    Rowan, M.J.3    Selkoe, D.J.4    Anwyl, R.5
  • 89
    • 0026668808 scopus 로고
    • Identification of six phosphorylation sites in the COOH-terminal tail region of the rat neurofilament protein M
    • Xu Z.S., Liu W.S., Willard M.B. Identification of six phosphorylation sites in the COOH-terminal tail region of the rat neurofilament protein M. J. Biol. Chem. 1992, 267(7):4467-4471.
    • (1992) J. Biol. Chem. , vol.267 , Issue.7 , pp. 4467-4471
    • Xu, Z.S.1    Liu, W.S.2    Willard, M.B.3
  • 90
    • 0034030749 scopus 로고    scopus 로고
    • Phospho-dependent association of neurofilament proteins with kinesin in situ
    • Yabe J.T., Jung C., Chan W.K., Shea T.B. Phospho-dependent association of neurofilament proteins with kinesin in situ. Cell Motil. Cytoskeleton 2000, 45(4):249-262.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , Issue.4 , pp. 249-262
    • Yabe, J.T.1    Jung, C.2    Chan, W.K.3    Shea, T.B.4
  • 92
    • 56249113024 scopus 로고    scopus 로고
    • Congenital hypothyroidism is associated with intermediate filament misregulation, glutamate transporters down-regulation and MAPK activation in developing rat brain
    • Zamoner A., Heimfarth L., Pessoa-Pureur R. Congenital hypothyroidism is associated with intermediate filament misregulation, glutamate transporters down-regulation and MAPK activation in developing rat brain. Neurotoxicology 2008, 29:1092-1099.
    • (2008) Neurotoxicology , vol.29 , pp. 1092-1099
    • Zamoner, A.1    Heimfarth, L.2    Pessoa-Pureur, R.3
  • 93
    • 77950555100 scopus 로고    scopus 로고
    • Increased expression of cdk5/p25 in N2a cells leads to hyperphosphorylation and impaired axonal transport of neurofilament proteins
    • Zhou J., Wang H., Feng Y., Chen J. Increased expression of cdk5/p25 in N2a cells leads to hyperphosphorylation and impaired axonal transport of neurofilament proteins. Life Sci. 2010, 86(13-14):532-537.
    • (2010) Life Sci. , vol.86 , Issue.13-14 , pp. 532-537
    • Zhou, J.1    Wang, H.2    Feng, Y.3    Chen, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.