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Volumn 7, Issue 1, 2012, Pages

Remarkable reduction of MAP2 in the brains of scrapie-infected rodents and human prion disease possibly correlated with the increase of calpain

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; MICROTUBULE ASSOCIATED PROTEIN 2; PRION PROTEIN; TUBULIN; MICROTUBULE ASSOCIATED PROTEIN;

EID: 84855822399     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0030163     Document Type: Article
Times cited : (26)

References (43)
  • 2
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge J, (2001) Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci 24: 519-550.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 5
    • 80053096617 scopus 로고    scopus 로고
    • SIRT1, a histone deacetylase, regulates prion protein-induced neuronal cell death
    • Seo JS, Moon MH, Jeong JK, Seol JW, Lee YJ, et al. (2010) SIRT1, a histone deacetylase, regulates prion protein-induced neuronal cell death. Neurobiol Aging.
    • (2010) Neurobiol Aging
    • Seo, J.S.1    Moon, M.H.2    Jeong, J.K.3    Seol, J.W.4    Lee, Y.J.5
  • 6
    • 0034711254 scopus 로고    scopus 로고
    • In vivo cytotoxicity of the prion protein fragment 106-126
    • Ettaiche M, Pichot R, Vincent JP, Chabry J, (2000) In vivo cytotoxicity of the prion protein fragment 106-126. J Biol Chem 275: 36487-36490.
    • (2000) J Biol Chem , vol.275 , pp. 36487-36490
    • Ettaiche, M.1    Pichot, R.2    Vincent, J.P.3    Chabry, J.4
  • 7
    • 0027259274 scopus 로고
    • Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein
    • Selvaggini C, De Gioia L, Cantu L, Ghibaudi E, Diomede L, et al. (1993) Molecular characteristics of a protease-resistant, amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein. Biochem Biophys Res Commun 194: 1380-1386.
    • (1993) Biochem Biophys Res Commun , vol.194 , pp. 1380-1386
    • Selvaggini, C.1    De Gioia, L.2    Cantu, L.3    Ghibaudi, E.4    Diomede, L.5
  • 8
    • 0141996464 scopus 로고    scopus 로고
    • Microtubules, microtubule-interfering agents and apoptosis
    • Mollinedo F, Gajate C, (2003) Microtubules, microtubule-interfering agents and apoptosis. Apoptosis 8: 413-450.
    • (2003) Apoptosis , vol.8 , pp. 413-450
    • Mollinedo, F.1    Gajate, C.2
  • 9
    • 43549104900 scopus 로고    scopus 로고
    • Up-regulation of microtubule-associated protein 2 accompanying the filial imprinting of domestic chicks (Gallus gallus domesticus)
    • Yamaguchi S, Fujii-Taira I, Murakami A, Hirose N, Aoki N, et al. (2008) Up-regulation of microtubule-associated protein 2 accompanying the filial imprinting of domestic chicks (Gallus gallus domesticus). Brain Res Bull 76: 282-288.
    • (2008) Brain Res Bull , vol.76 , pp. 282-288
    • Yamaguchi, S.1    Fujii-Taira, I.2    Murakami, A.3    Hirose, N.4    Aoki, N.5
  • 10
    • 19744382953 scopus 로고    scopus 로고
    • The MAP2/Tau family of microtubule-associated proteins
    • Dehmelt L, Halpain S, (2005) The MAP2/Tau family of microtubule-associated proteins. Genome Biol 6: 204.
    • (2005) Genome Biol , vol.6 , pp. 204
    • Dehmelt, L.1    Halpain, S.2
  • 11
    • 0036946621 scopus 로고    scopus 로고
    • Morphologically distinct plaque types differentially affect dendritic structure and organisation in the early and late stages of Alzheimer's disease
    • Adlard PA, Vickers JC, (2002) Morphologically distinct plaque types differentially affect dendritic structure and organisation in the early and late stages of Alzheimer's disease. Acta Neuropathol 103: 377-383.
    • (2002) Acta Neuropathol , vol.103 , pp. 377-383
    • Adlard, P.A.1    Vickers, J.C.2
  • 12
    • 13044287361 scopus 로고    scopus 로고
    • Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models
    • Hsia AY, Masliah E, McConlogue L, Yu GQ, Tatsuno G, et al. (1999) Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc Natl Acad Sci U S A 96: 3228-3233.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3228-3233
    • Hsia, A.Y.1    Masliah, E.2    McConlogue, L.3    Yu, G.Q.4    Tatsuno, G.5
  • 13
    • 33644853371 scopus 로고    scopus 로고
    • Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3
    • Fifre A, Sponne I, Koziel V, Kriem B, Yen Potin FT, et al. (2006) Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3. J Biol Chem 281: 229-240.
    • (2006) J Biol Chem , vol.281 , pp. 229-240
    • Fifre, A.1    Sponne, I.2    Koziel, V.3    Kriem, B.4    Yen Potin, F.T.5
  • 14
    • 78049254440 scopus 로고    scopus 로고
    • Potential therapeutic effects of curcumin: relationship to microtubule-associated proteins 2 in Abeta1-42 insult
    • Xiao Z, Lin L, Liu Z, Ji F, Shao W, et al. (2010) Potential therapeutic effects of curcumin: relationship to microtubule-associated proteins 2 in Abeta1-42 insult. Brain Res 1361: 115-123.
    • (2010) Brain Res , vol.1361 , pp. 115-123
    • Xiao, Z.1    Lin, L.2    Liu, Z.3    Ji, F.4    Shao, W.5
  • 15
    • 80051605287 scopus 로고    scopus 로고
    • Molecular interaction of TPPP with PrP antagonized the CytoPrP-induced disruption of microtubule structures and cytotoxicity
    • Zhou RM, Jing YY, Guo Y, Gao C, Zhang BY, et al. (2011) Molecular interaction of TPPP with PrP antagonized the CytoPrP-induced disruption of microtubule structures and cytotoxicity. PLoS ONE 6: e23079.
    • (2011) PLoS ONE , vol.6
    • Zhou, R.M.1    Jing, Y.Y.2    Guo, Y.3    Gao, C.4    Zhang, B.Y.5
  • 16
    • 79955809111 scopus 로고    scopus 로고
    • Cytosolic PrP induces apoptosis of cell by disrupting microtubule assembly
    • Li XL, Wang GR, Jing YY, Pan MM, Dong CF, et al. (2011) Cytosolic PrP induces apoptosis of cell by disrupting microtubule assembly. J Mol Neurosci 43: 316-325.
    • (2011) J Mol Neurosci , vol.43 , pp. 316-325
    • Li, X.L.1    Wang, G.R.2    Jing, Y.Y.3    Pan, M.M.4    Dong, C.F.5
  • 17
    • 70349448466 scopus 로고    scopus 로고
    • Prion protein region 23-32 interacts with tubulin and inhibits microtubule assembly
    • Osiecka KM, Nieznanska H, Skowronek KJ, Karolczak J, Schneider G, et al. (2009) Prion protein region 23-32 interacts with tubulin and inhibits microtubule assembly. Proteins 77: 279-296.
    • (2009) Proteins , vol.77 , pp. 279-296
    • Osiecka, K.M.1    Nieznanska, H.2    Skowronek, K.J.3    Karolczak, J.4    Schneider, G.5
  • 18
    • 38349061552 scopus 로고    scopus 로고
    • The N-terminus of PrP is responsible for interacting with tubulin and fCJD related PrP mutants possess stronger inhibitive effect on microtubule assembly in vitro
    • Dong CF, Shi S, Wang XF, An R, Li P, et al. (2008) The N-terminus of PrP is responsible for interacting with tubulin and fCJD related PrP mutants possess stronger inhibitive effect on microtubule assembly in vitro. Arch Biochem Biophys 470: 83-92.
    • (2008) Arch Biochem Biophys , vol.470 , pp. 83-92
    • Dong, C.F.1    Shi, S.2    Wang, X.F.3    An, R.4    Li, P.5
  • 19
    • 84862972248 scopus 로고    scopus 로고
    • The diversities of PrP(Sc) distributions and pathologic changes in various brain regions from a Chinese patient with G114V genetic CJD
    • Shi Q, Zhang BY, Gao C, Han J, Wang GR, et al. (2011) The diversities of PrP(Sc) distributions and pathologic changes in various brain regions from a Chinese patient with G114V genetic CJD. Neuropathology.
    • (2011) Neuropathology
    • Shi, Q.1    Zhang, B.Y.2    Gao, C.3    Han, J.4    Wang, G.R.5
  • 20
    • 76849099629 scopus 로고    scopus 로고
    • Clinical, histopathological and genetic studies in a family with fatal familial insomnia
    • Shi XH, Han J, Zhang J, Shi Q, Chen JM, et al. (2010) Clinical, histopathological and genetic studies in a family with fatal familial insomnia. Infect Genet Evol 10: 292-297.
    • (2010) Infect Genet Evol , vol.10 , pp. 292-297
    • Shi, X.H.1    Han, J.2    Zhang, J.3    Shi, Q.4    Chen, J.M.5
  • 21
    • 33645729661 scopus 로고    scopus 로고
    • Comparative study of the effects of several chemical and physical treatments on the activity of protease resistance and infectivity of scrapie strain 263K
    • Yao HL, Han J, Gao JM, Zhang J, Zhang BY, et al. (2005) Comparative study of the effects of several chemical and physical treatments on the activity of protease resistance and infectivity of scrapie strain 263K. J Vet Med B Infect Dis Vet Public Health 52: 437-443.
    • (2005) J Vet Med B Infect Dis Vet Public Health , vol.52 , pp. 437-443
    • Yao, H.L.1    Han, J.2    Gao, J.M.3    Zhang, J.4    Zhang, B.Y.5
  • 22
    • 0031853417 scopus 로고    scopus 로고
    • Making sense of the multiple MAP-2 transcripts and their role in the neuron
    • Shafit-Zagardo B, Kalcheva N, (1998) Making sense of the multiple MAP-2 transcripts and their role in the neuron. Mol Neurobiol 16: 149-162.
    • (1998) Mol Neurobiol , vol.16 , pp. 149-162
    • Shafit-Zagardo, B.1    Kalcheva, N.2
  • 23
    • 0025201210 scopus 로고
    • The roles of microtubule-associated proteins in brain morphogenesis: a review
    • Tucker RP, (1990) The roles of microtubule-associated proteins in brain morphogenesis: a review. Brain Res Brain Res Rev 15: 101-120.
    • (1990) Brain Res Brain Res Rev , vol.15 , pp. 101-120
    • Tucker, R.P.1
  • 24
    • 0342546002 scopus 로고    scopus 로고
    • Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function
    • Sanchez C, Diaz-Nido J, Avila J, (2000) Phosphorylation of microtubule-associated protein 2 (MAP2) and its relevance for the regulation of the neuronal cytoskeleton function. Prog Neurobiol 61: 133-168.
    • (2000) Prog Neurobiol , vol.61 , pp. 133-168
    • Sanchez, C.1    Diaz-Nido, J.2    Avila, J.3
  • 25
    • 0000146080 scopus 로고
    • Differential expression of distinct microtubule-associated proteins during brain development
    • Riederer B, Matus A, (1985) Differential expression of distinct microtubule-associated proteins during brain development. Proc Natl Acad Sci U S A 82: 6006-6009.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6006-6009
    • Riederer, B.1    Matus, A.2
  • 26
    • 0022723508 scopus 로고
    • One of the antigenic determinants of paired helical filaments is related to tau protein
    • Nukina N, Ihara Y, (1986) One of the antigenic determinants of paired helical filaments is related to tau protein. J Biochem 99: 1541-1544.
    • (1986) J Biochem , vol.99 , pp. 1541-1544
    • Nukina, N.1    Ihara, Y.2
  • 27
    • 2442443113 scopus 로고    scopus 로고
    • Dynamic analyses of PrP and PrP(Sc) in brain tissues of golden hamsters infected with scrapie strain 263K revealed various PrP forms
    • Gao JM, Gao C, Han J, Zhou XB, Xiao XL, et al. (2004) Dynamic analyses of PrP and PrP(Sc) in brain tissues of golden hamsters infected with scrapie strain 263K revealed various PrP forms. Biomed Environ Sci 17: 8-20.
    • (2004) Biomed Environ Sci , vol.17 , pp. 8-20
    • Gao, J.M.1    Gao, C.2    Han, J.3    Zhou, X.B.4    Xiao, X.L.5
  • 28
    • 0030930824 scopus 로고    scopus 로고
    • Rapid calpain I activation and cytoskeletal protein degradation following traumatic spinal cord injury: attenuation with riluzole pretreatment
    • Springer JE, Azbill RD, Kennedy SE, George J, Geddes JW, (1997) Rapid calpain I activation and cytoskeletal protein degradation following traumatic spinal cord injury: attenuation with riluzole pretreatment. J Neurochem 69: 1592-1600.
    • (1997) J Neurochem , vol.69 , pp. 1592-1600
    • Springer, J.E.1    Azbill, R.D.2    Kennedy, S.E.3    George, J.4    Geddes, J.W.5
  • 29
    • 0032080434 scopus 로고    scopus 로고
    • Prion protein fragment interacts with PrP-deficient cells
    • Brown DR, Schmidt B, Kretzschmar HA, (1998) Prion protein fragment interacts with PrP-deficient cells. J Neurosci Res 52: 260-267.
    • (1998) J Neurosci Res , vol.52 , pp. 260-267
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 30
    • 0033370716 scopus 로고    scopus 로고
    • Cellular uptake of the prion protein fragment PrP106-126 in vitro
    • McHattie SJ, Brown DR, Bird MM, (1999) Cellular uptake of the prion protein fragment PrP106-126 in vitro. J Neurocytol 28: 149-159.
    • (1999) J Neurocytol , vol.28 , pp. 149-159
    • McHattie, S.J.1    Brown, D.R.2    Bird, M.M.3
  • 31
    • 0034653970 scopus 로고    scopus 로고
    • Altered toxicity of the prion protein peptide PrP106-126 carrying the Ala(117)-&Val mutation
    • Brown DR, (2000) Altered toxicity of the prion protein peptide PrP106-126 carrying the Ala(117)-&Val mutation. Biochem J 346 Pt 3: 785-791.
    • (2000) Biochem J , vol.346 Pt , pp. 785-791
    • Brown, D.R.1
  • 32
    • 33749826279 scopus 로고    scopus 로고
    • Study on interaction between microtubule associated protein tau and prion protein
    • Han J, Zhang J, Yao H, Wang X, Li F, et al. (2006) Study on interaction between microtubule associated protein tau and prion protein. Sci China C Life Sci 49: 473-479.
    • (2006) Sci China C Life Sci , vol.49 , pp. 473-479
    • Han, J.1    Zhang, J.2    Yao, H.3    Wang, X.4    Li, F.5
  • 33
    • 80051605287 scopus 로고    scopus 로고
    • Molecular interaction of TPPP with PrP antagonized the CytoPrP-induced disruption of microtubule structures and cytotoxicity
    • Zhou R-M, Jing Y-Y, Gao C, Guo Y, (2011) Molecular interaction of TPPP with PrP antagonized the CytoPrP-induced disruption of microtubule structures and cytotoxicity. PLoS ONE 26: 379-386.
    • (2011) PLoS ONE , vol.26 , pp. 379-386
    • Zhou, R.-M.1    Jing, Y.-Y.2    Gao, C.3    Guo, Y.4
  • 34
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease
    • Ebneth A, Godemann R, Stamer K, Illenberger S, Trinczek B, et al. (1998) Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: implications for Alzheimer's disease. J Cell Biol 143: 777-794.
    • (1998) J Cell Biol , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trinczek, B.5
  • 36
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: roles in synaptic plasticity and cell death
    • Chan SL, Mattson MP, (1999) Caspase and calpain substrates: roles in synaptic plasticity and cell death. J Neurosci Res 58: 167-190.
    • (1999) J Neurosci Res , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 37
    • 0030636607 scopus 로고    scopus 로고
    • Changes of cytoskeletal protein immunostaining in myelinated fibre tracts after focal cerebral ischaemia in the rat
    • Dewar D, Dawson DA, (1997) Changes of cytoskeletal protein immunostaining in myelinated fibre tracts after focal cerebral ischaemia in the rat. Acta Neuropathol 93: 71-77.
    • (1997) Acta Neuropathol , vol.93 , pp. 71-77
    • Dewar, D.1    Dawson, D.A.2
  • 38
    • 0029889986 scopus 로고    scopus 로고
    • Intracortical perfusion of glutamate in vivo induces alterations of tau and microtubule-associated protein 2 immunoreactivity in the rat
    • Irving EA, McCulloch J, Dewar D, (1996) Intracortical perfusion of glutamate in vivo induces alterations of tau and microtubule-associated protein 2 immunoreactivity in the rat. Acta Neuropathol 92: 186-196.
    • (1996) Acta Neuropathol , vol.92 , pp. 186-196
    • Irving, E.A.1    McCulloch, J.2    Dewar, D.3
  • 39
    • 37549015597 scopus 로고    scopus 로고
    • Role of cyclin-dependent kinase 5 in the neurodegenerative process triggered by amyloid-Beta and prion peptides: implications for Alzheimer's disease and prion-related encephalopathies
    • Lopes JP, Oliveira CR, Agostinho P, (2007) Role of cyclin-dependent kinase 5 in the neurodegenerative process triggered by amyloid-Beta and prion peptides: implications for Alzheimer's disease and prion-related encephalopathies. Cell Mol Neurobiol 27: 943-957.
    • (2007) Cell Mol Neurobiol , vol.27 , pp. 943-957
    • Lopes, J.P.1    Oliveira, C.R.2    Agostinho, P.3
  • 40
    • 58149397537 scopus 로고    scopus 로고
    • Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: neuroprotection by CAST overexpression
    • Rao MV, Mohan PS, Peterhoff CM, Yang DS, Schmidt SD, et al. (2008) Marked calpastatin (CAST) depletion in Alzheimer's disease accelerates cytoskeleton disruption and neurodegeneration: neuroprotection by CAST overexpression. J Neurosci 28: 12241-12254.
    • (2008) J Neurosci , vol.28 , pp. 12241-12254
    • Rao, M.V.1    Mohan, P.S.2    Peterhoff, C.M.3    Yang, D.S.4    Schmidt, S.D.5
  • 41
    • 0035941307 scopus 로고    scopus 로고
    • Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells
    • O'Donovan CN, Tobin D, Cotter TG, (2001) Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. J Biol Chem 276: 43516-43523.
    • (2001) J Biol Chem , vol.276 , pp. 43516-43523
    • O'Donovan, C.N.1    Tobin, D.2    Cotter, T.G.3
  • 42
    • 0036830947 scopus 로고    scopus 로고
    • Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease
    • LaFerla FM, (2002) Calcium dyshomeostasis and intracellular signalling in Alzheimer's disease. Nat Rev Neurosci 3: 862-872.
    • (2002) Nat Rev Neurosci , vol.3 , pp. 862-872
    • LaFerla, F.M.1
  • 43
    • 0034524665 scopus 로고    scopus 로고
    • The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states
    • Vanderklish PW, Bahr BA, (2000) The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states. Int J Exp Pathol 81: 323-339.
    • (2000) Int J Exp Pathol , vol.81 , pp. 323-339
    • Vanderklish, P.W.1    Bahr, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.