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Volumn 25, Issue 8, 2005, Pages 1171-1183

Altered expression of the prion gene in rat astrocyte and neuron cultures treated with prion peptide 106-126

Author keywords

Cultured astrocytes and neurons; mRNA expression; Prio npeptide 106 126; Real time RT PCR

Indexed keywords

MESSENGER RNA; NITROBLUE TETRAZOLIUM; PEPTIDE; PRION PEPTIDE [106-126]; UNCLASSIFIED DRUG;

EID: 29844439160     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10571-005-8357-5     Document Type: Article
Times cited : (12)

References (32)
  • 2
    • 0032817255 scopus 로고    scopus 로고
    • Prion protein peptide neurotoxicity can be mediated by astrocytes
    • Brown, D. R. (1999a). Prion protein peptide neurotoxicity can be mediated by astrocytes. J. Neurochem. 73(3):1105-1113.
    • (1999) J. Neurochem. , vol.73 , Issue.3 , pp. 1105-1113
    • Brown, D.R.1
  • 3
    • 0033032141 scopus 로고    scopus 로고
    • Neurons depend on astrocytes in a coculture system for protection from glutamate toxicity
    • Brown, D. R. (1999b). Neurons depend on astrocytes in a coculture system for protection from glutamate toxicity. Mol Cell. Neurosci. 13(5):379-389.
    • (1999) Mol Cell. Neurosci. , vol.13 , Issue.5 , pp. 379-389
    • Brown, D.R.1
  • 4
    • 0034533064 scopus 로고    scopus 로고
    • PrPSc-like prion protein peptide inhibits the function of cellular prion protein
    • Brown, D. R. (2000). PrPSc-like prion protein peptide inhibits the function of cellular prion protein. Biochem. J. 352:511-518.
    • (2000) Biochem. J. , vol.352 , pp. 511-518
    • Brown, D.R.1
  • 5
    • 0035254585 scopus 로고    scopus 로고
    • Prion and prejudice: Normal protein and the synapse
    • Brown, D. R. (2001). Prion and prejudice: Normal protein and the synapse. Trends Neurosci. 24(2):85-90.
    • (2001) Trends Neurosci. , vol.24 , Issue.2 , pp. 85-90
    • Brown, D.R.1
  • 6
    • 0033083722 scopus 로고    scopus 로고
    • Astrocytic glutamate uptake and prion protein expression
    • Brown, D. R., and Mohn, C. M. (1999). Astrocytic glutamate uptake and prion protein expression. Glia 25(3):282-292.
    • (1999) Glia , vol.25 , Issue.3 , pp. 282-292
    • Brown, D.R.1    Mohn, C.M.2
  • 7
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1996). Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380:345-347.
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 8
    • 0024366602 scopus 로고
    • Precise targeting of the sialoglyco-protein PrP and vacuolar degeneration in mouse scrapie
    • Bruce, M. E., McBride, P. A., and Farquhar, C. F. (1989). Precise targeting of the sialoglyco-protein PrP and vacuolar degeneration in mouse scrapie. Neurosci. Lett. 102(1):1-6.
    • (1989) Neurosci. Lett. , vol.102 , Issue.1 , pp. 1-6
    • Bruce, M.E.1    McBride, P.A.2    Farquhar, C.F.3
  • 9
    • 0037439629 scopus 로고    scopus 로고
    • In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression
    • Chabry, J., Ratsimanohatra, C., Sponne, I., Elena, P. P., Vincent, J. P., and Pillot, T. (2003). In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. J. Neurosci. 23:462-469.
    • (2003) J. Neurosci. , vol.23 , pp. 462-469
    • Chabry, J.1    Ratsimanohatra, C.2    Sponne, I.3    Elena, P.P.4    Vincent, J.P.5    Pillot, T.6
  • 10
    • 0029027854 scopus 로고
    • Truncated forms of the human prion protein in normal brain and in prion diseases
    • Chen, S. G., Teplow, D. B., Parchi, P., Teller, J. K., Gambetti, P., and Autilio-Gambetti, L. (1995). Truncated forms of the human prion protein in normal brain and in prion diseases. J. Biol. Chem. 270(32):19173-19180.
    • (1995) J. Biol. Chem. , vol.270 , Issue.32 , pp. 19173-19180
    • Chen, S.G.1    Teplow, D.B.2    Parchi, P.3    Teller, J.K.4    Gambetti, P.5    Autilio-Gambetti, L.6
  • 11
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa, R., and Harris, D. A. (2001). Prion diseases: What is the neurotoxic molecule? Neurobiol. Dis. 8(5):743-763.
    • (2001) Neurobiol. Dis. , vol.8 , Issue.5 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 12
    • 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
  • 13
  • 14
    • 0025967257 scopus 로고
    • Scrapie-associated prion protein accumulates in astrocytes during scrapie infection
    • Diedrich, J. F., Bendheim, P. E., Kim, Y. S., Carp, R. I., and Haase, A. T. (1991). Scrapie-associated prion protein accumulates in astrocytes during scrapie infection. Proc. Natl Acad. Sci. U.S.A. 88(2):375-379.
    • (1991) Proc. Natl Acad. Sci. U.S.A. , vol.88 , Issue.2 , pp. 375-379
    • Diedrich, J.F.1    Bendheim, P.E.2    Kim, Y.S.3    Carp, R.I.4    Haase, A.T.5
  • 15
    • 0034711254 scopus 로고    scopus 로고
    • In vivo cytotoxicity of the prion protein fragment 106-126
    • Ettaiche, M., Pichot, R., Vincent, J. P., and Chabry, J. (2000). In vivo cytotoxicity of the prion protein fragment 106-126. J. Biol Chem. 275(47):36487-36490.
    • (2000) J. Biol Chem. , vol.275 , Issue.47 , pp. 36487-36490
    • Ettaiche, M.1    Pichot, R.2    Vincent, J.P.3    Chabry, J.4
  • 16
    • 10644226077 scopus 로고    scopus 로고
    • The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species
    • Fioriti, L., Quagliom, E., Massignan, T., Colombo, L., Stewart, R. S., Salmona, M., Harris, D. A., Forloni, G., and Chiesa, R. (2005). The neurotoxicity of prion protein (PrP) peptide 106-126 is independent of the expression level of PrP and is not mediated by abnormal PrP species. Mol. Cell. Neurosci. 28(1):165-176.
    • (2005) Mol. Cell. Neurosci. , vol.28 , Issue.1 , pp. 165-176
    • Fioriti, L.1    Quagliom, E.2    Massignan, T.3    Colombo, L.4    Stewart, R.S.5    Salmona, M.6    Harris, D.A.7    Forloni, G.8    Chiesa, R.9
  • 17
    • 0032213349 scopus 로고    scopus 로고
    • Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line
    • Florio, T., Thellung, S., Amico, C., Robello, M., Salmona, M., Bugiani, O., Tagliavini, F., Forloni, G., and Schettini, G. (1998). Prion protein fragment 106-126 induces apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in the GH3 cell line. J. Neurosci. Res. 54(3):341-352.
    • (1998) J. Neurosci. Res. , vol.54 , Issue.3 , pp. 341-352
    • Florio, T.1    Thellung, S.2    Amico, C.3    Robello, M.4    Salmona, M.5    Bugiani, O.6    Tagliavini, F.7    Forloni, G.8    Schettini, G.9
  • 20
    • 0001847208 scopus 로고
    • Culture of specific cell types
    • Freshney, R. I. (ed.). AR Liss, New York
    • Freshney, R. I. (1987). Culture of specific cell types. In Freshney, R. I. (ed.). Culture of Animal Cells: A Manual of Basic Technique, AR Liss, New York, pp. 257-288.
    • (1987) Culture of Animal Cells: A Manual of Basic Technique , pp. 257-288
    • Freshney, R.I.1
  • 21
    • 0033763178 scopus 로고    scopus 로고
    • PrP(C) expression in the peripheral nervous system is a determinant of prion neuroinvasion
    • Glatzel, M., and Aguzzi, A. (2000). PrP(C) expression in the peripheral nervous system is a determinant of prion neuroinvasion. J. Gen. Virol. 81:2813-2821.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2813-2821
    • Glatzel, M.1    Aguzzi, A.2
  • 22
    • 0037127225 scopus 로고    scopus 로고
    • Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP
    • Gu, Y., Fujioka, H., Mishra, R. S., Li, R., and Singh, N. (2002). Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP. J. Biol. Chem. 277:2275-2286.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2275-2286
    • Gu, Y.1    Fujioka, H.2    Mishra, R.S.3    Li, R.4    Singh, N.5
  • 23
    • 0029964280 scopus 로고    scopus 로고
    • Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, a beta 25-35
    • Hope, J., Shearman, M. S., Baxter, H. C., Chong, A., Kelly, S. M., and Price, N. C. (1996). Cytotoxicity of prion protein peptide (PrP106-126) differs in mechanism from the cytotoxic activity of the Alzheimer's disease amyloid peptide, a beta 25-35. Neurodegeneration 5(1):1-11.
    • (1996) Neurodegeneration , vol.5 , Issue.1 , pp. 1-11
    • Hope, J.1    Shearman, M.S.2    Baxter, H.C.3    Chong, A.4    Kelly, S.M.5    Price, N.C.6
  • 24
    • 0021335259 scopus 로고
    • Autoradiographic localization and depolarization-induced release of acidic amino acids in differentiating cerebellar granule cell cultures
    • Levi, G., Aloisi, F., Ciotti, M. T., and Gallo, V. (1984). Autoradiographic localization and depolarization-induced release of acidic amino acids in differentiating cerebellar granule cell cultures. Brain Res. 290(1):77-86.
    • (1984) Brain Res. , vol.290 , Issue.1 , pp. 77-86
    • Levi, G.1    Aloisi, F.2    Ciotti, M.T.3    Gallo, V.4
  • 25
  • 26
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B. (1991). Molecular biology of prion diseases. Science 252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 27
    • 0027001034 scopus 로고
    • Chemistry and biology of prions
    • Prusiner, S. B. (1992). Chemistry and biology of prions. Biochemistry 31(49):12277-12288.
    • (1992) Biochemistry , vol.31 , Issue.49 , pp. 12277-12288
    • Prusiner, S.B.1
  • 30
    • 0033777826 scopus 로고    scopus 로고
    • The role of prion peptide structure and aggregation in toxicity and membrane binding
    • Rymer, D. L., and Good, T. A. (2000). The role of prion peptide structure and aggregation in toxicity and membrane binding. J. Neurochem. 75(6):2536-2545.
    • (2000) J. Neurochem. , vol.75 , Issue.6 , pp. 2536-2545
    • Rymer, D.L.1    Good, T.A.2
  • 32
    • 0033826141 scopus 로고    scopus 로고
    • Apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in rat cerebellar granule cells treated with the prion protein fragment 106-126
    • Thellung, S., Florio, T., Villa, V., Corsaro, A., Arena, S., Amico, C., Robello, M., Salmona, M., Forloni, G., Bugiani, O., Tagliavini, F., and Schettini, G. (2000). Apoptotic cell death and impairment of L-type voltage-sensitive calcium channel activity in rat cerebellar granule cells treated with the prion protein fragment 106-126. Neurobiol. Dis. 7(4):299-309.
    • (2000) Neurobiol. Dis. , vol.7 , Issue.4 , pp. 299-309
    • Thellung, S.1    Florio, T.2    Villa, V.3    Corsaro, A.4    Arena, S.5    Amico, C.6    Robello, M.7    Salmona, M.8    Forloni, G.9    Bugiani, O.10    Tagliavini, F.11    Schettini, G.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.