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Volumn 103, Issue 6, 2007, Pages 2291-2300

Different structural stability and toxicity of PrPARR and PrPARQ sheep prion protein variants

Author keywords

Cell death; Prion protein genetic polymorphism; Sheep prion protein

Indexed keywords

PRION PROTEIN; PRION PROTEIN ALANYLARGINYLARGININE; PRION PROTEIN ALANYLARGINYLGLUTAMINE; UNCLASSIFIED DRUG;

EID: 36448986023     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04934.x     Document Type: Article
Times cited : (16)

References (41)
  • 1
    • 0028925025 scopus 로고
    • Structural and functional properties of the 34-kDa fragment produced by the N-terminal chymotryptic cleavage of glutathione transferase P1-1
    • Aceto A., Sacchetta P., Bucciarelli T., Dragani B., Angelucci S., Radatti G. L. Di Ilio C. (1995) Structural and functional properties of the 34-kDa fragment produced by the N-terminal chymotryptic cleavage of glutathione transferase P1-1. Arch. Biochem. Biophys. 316, 873 878.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 873-878
    • Aceto, A.1    Sacchetta, P.2    Bucciarelli, T.3    Dragani, B.4    Angelucci, S.5    Radatti, G.L.6    Di Ilio, C.7
  • 2
    • 33645543013 scopus 로고    scopus 로고
    • Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep
    • Andreoletti O., Morel N., Lacroux C. et al. (2006) Bovine spongiform encephalopathy agent in spleen from an ARR/ARR orally exposed sheep. J. Gen. Virol. 87, 1043 1046.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1043-1046
    • Andreoletti, O.1    Morel, N.2    Lacroux, C.3
  • 3
    • 2942748485 scopus 로고    scopus 로고
    • The genetics of scrapie in sheep and goats
    • Baylis M. Goldmann W. (2004) The genetics of scrapie in sheep and goats. Curr. Mol. Med. 4, 385 396.
    • (2004) Curr. Mol. Med. , vol.4 , pp. 385-396
    • Baylis, M.1    Goldmann, W.2
  • 4
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown D. R., Herms J. Kretzschmar H. A. (1994) Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5, 2057 2060.
    • (1994) Neuroreport , vol.5 , pp. 2057-2060
    • Brown, D.R.1    Herms, J.2    Kretzschmar, H.A.3
  • 5
    • 28644432876 scopus 로고    scopus 로고
    • Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations
    • Bujdoso R., Burke D. F. Thackray A. M. (2005) Structural differences between allelic variants of the ovine prion protein revealed by molecular dynamics simulations. Proteins 61, 840 849.
    • (2005) Proteins , vol.61 , pp. 840-849
    • Bujdoso, R.1    Burke, D.F.2    Thackray, A.M.3
  • 6
    • 4544375025 scopus 로고    scopus 로고
    • Neuronal accumulation of abnormal prion protein in sheep carrying a scrapie-resistant genotype (PrPARR/ARR)
    • Buschmann A., Luhken G., Schultz J., Erhardt G. Groschup M. H. (2004) Neuronal accumulation of abnormal prion protein in sheep carrying a scrapie-resistant genotype (PrPARR/ARR). J. Gen. Virol. 85, 2727 2733.
    • (2004) J. Gen. Virol. , vol.85 , pp. 2727-2733
    • Buschmann, A.1    Luhken, G.2    Schultz, J.3    Erhardt, G.4    Groschup, M.H.5
  • 8
    • 2642582407 scopus 로고    scopus 로고
    • Resistance to scrapie in PrP ARR/ARQ heterozygous sheep is not caused by preferential allelic use
    • Caplazi P. A., O'Rourke K. I. Baszler T. V. (2004) Resistance to scrapie in PrP ARR/ARQ heterozygous sheep is not caused by preferential allelic use. J. Clin. Pathol. 57, 647 650.
    • (2004) J. Clin. Pathol. , vol.57 , pp. 647-650
    • Caplazi, P.A.1    O'Rourke, K.I.2    Baszler, T.V.3
  • 10
    • 0037439629 scopus 로고    scopus 로고
    • In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. a nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons
    • Chabry J., Ratsimanohatra C., Sponne I. et al. (2003) In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression. A nonfibrillar form of the fusogenic prion protein fragment [118-135] induces apoptotic cell death in rat cortical neurons. J. Neurosci. 23, 462 469.
    • (2003) J. Neurosci. , vol.23 , pp. 462-469
    • Chabry, J.1    Ratsimanohatra, C.2    Sponne, I.3
  • 11
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa R. Harris D. A. (2001) Prion diseases: what is the neurotoxic molecule? Neurobiol. Dis. 8, 743 763.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 13
    • 18344385828 scopus 로고    scopus 로고
    • Expression in E. coli and purification of recombinant fragments of wild type and mutant human prion protein
    • Corsaro A., Thellung S., Russo C. et al. (2002) Expression in E. coli and purification of recombinant fragments of wild type and mutant human prion protein. Neurochem. Int. 41, 55 63.
    • (2002) Neurochem. Int. , vol.41 , pp. 55-63
    • Corsaro, A.1    Thellung, S.2    Russo, C.3
  • 14
    • 10744228678 scopus 로고    scopus 로고
    • Prion protein fragment 106-126 induces a p38 MAP kinase-dependent apoptosis in SH-SY5Y neuroblastoma cells independently from the amyloid fibril formation
    • Corsaro A., Thellung S., Villa V. et al. (2003) Prion protein fragment 106-126 induces a p38 MAP kinase-dependent apoptosis in SH-SY5Y neuroblastoma cells independently from the amyloid fibril formation. Ann. N. Y. Acad. Sci. 1010, 610 622.
    • (2003) Ann. N. Y. Acad. Sci. , vol.1010 , pp. 610-622
    • Corsaro, A.1    Thellung, S.2    Villa, V.3
  • 15
    • 33746831567 scopus 로고    scopus 로고
    • Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231
    • Corsaro A., Paludi D., Villa V. et al. (2006) Conformation dependent pro-apoptotic activity of the recombinant human prion protein fragment 90-231. Int. J. Immunopathol. Pharmacol. 19, 339 356.
    • (2006) Int. J. Immunopathol. Pharmacol. , vol.19 , pp. 339-356
    • Corsaro, A.1    Paludi, D.2    Villa, V.3
  • 16
    • 0035213414 scopus 로고    scopus 로고
    • Toxicity of novel C-terminal prion protein fragments and peptides harbouring disease-related C-terminal mutations
    • Daniels M., Cereghetti G. M. Brown D. R. (2001) Toxicity of novel C-terminal prion protein fragments and peptides harbouring disease-related C-terminal mutations. Eur. J. Biochem. 268, 6155 6164.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6155-6164
    • Daniels, M.1    Cereghetti, G.M.2    Brown, D.R.3
  • 19
    • 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. 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, 341 352.
    • (1998) J. Neurosci. Res. , vol.54 , 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
    • 0037380980 scopus 로고    scopus 로고
    • Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic
    • Florio T., Paludi D., Villa V. et al. (2003) Contribution of two conserved glycine residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J. Neurochem. 85, 62 72.
    • (2003) J. Neurochem. , vol.85 , pp. 62-72
    • Florio, T.1    Paludi, D.2    Villa, V.3
  • 21
    • 20044381672 scopus 로고    scopus 로고
    • Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: The disease associated D202N mutation destabilizes the helical conformation
    • Gallo M., Paludi D., Cicero D. O. et al. (2005) Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation. Int. J. Immunopathol. Pharmacol. 18, 95 112.
    • (2005) Int. J. Immunopathol. Pharmacol. , vol.18 , pp. 95-112
    • Gallo, M.1    Paludi, D.2    Cicero, D.O.3
  • 24
    • 33751099559 scopus 로고    scopus 로고
    • Transmission of chronic wasting disease of mule deer to Suffolk sheep following intracerebral inoculation
    • Hamir A. N., Kunkle R. A., Cutlip R. C., Miller J. M., Williams E. S. Richt J. A. (2006) Transmission of chronic wasting disease of mule deer to Suffolk sheep following intracerebral inoculation. J. Vet. Diagn. Invest. 18, 558 565.
    • (2006) J. Vet. Diagn. Invest. , vol.18 , pp. 558-565
    • Hamir, A.N.1    Kunkle, R.A.2    Cutlip, R.C.3    Miller, J.M.4    Williams, E.S.5    Richt, J.A.6
  • 26
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C., Russelakis-Carneiro M., Maundrell K., Castilla J. Soto C. (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J. 22, 5435 5445.
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 27
    • 0345621492 scopus 로고    scopus 로고
    • Pathology of variant Creutzfeldt-Jakob disease
    • Ironside J. W. (2000) Pathology of variant Creutzfeldt-Jakob disease. Arch. Virol. Suppl. 16, 143 151
    • (2000) Arch. Virol. Suppl. , vol.16 , pp. 143-151
    • Ironside, J.W.1
  • 28
    • 0033485260 scopus 로고    scopus 로고
    • A single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy
    • Manson J. C., Jamieson E., Baybutt H. et al. (1999) A single amino acid alteration (101L) introduced into murine PrP dramatically alters incubation time of transmissible spongiform encephalopathy. EMBO J. 18, 6855 6864.
    • (1999) EMBO J. , vol.18 , pp. 6855-6864
    • Manson, J.C.1    Jamieson, E.2    Baybutt, H.3
  • 30
    • 0035941307 scopus 로고    scopus 로고
    • Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells
    • O'Donovan C. N., Tobin D. Cotter T. G. (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
  • 31
    • 33646931017 scopus 로고    scopus 로고
    • Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo
    • Piening N., Nonno R., Di Bari M., Walter S., Windl O., Agrimi U., Kretzschmar H. A. Bertsch U. (2006) Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo. J. Biol. Chem. 281, 9373 9384.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9373-9384
    • Piening, N.1    Nonno, R.2    Di Bari, M.3    Walter, S.4    Windl, O.5    Agrimi, U.6    Kretzschmar, H.A.7    Bertsch, U.8
  • 33
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture - Neurodegenerative diseases and prions
    • Prusiner S. B. (2001) Shattuck lecture - neurodegenerative diseases and prions. N. Engl. J. Med. 344, 1516 1526.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1516-1526
    • Prusiner, S.B.1
  • 34
    • 0034127890 scopus 로고    scopus 로고
    • High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility
    • Rezaei H., Marc D., Choiset Y., Takahashi M., Hui Bon Hoa G., Haertle T., Grosclaude J. Debey P. (2000) High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 267, 2833 2839.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2833-2839
    • Rezaei, H.1    Marc, D.2    Choiset, Y.3    Takahashi, M.4    Hui Bon Hoa, G.5    Haertle, T.6    Grosclaude, J.7    Debey, P.8
  • 35
    • 23844476256 scopus 로고    scopus 로고
    • Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion
    • Rigter A. Bossers A. (2005) Sheep scrapie susceptibility-linked polymorphisms do not modulate the initial binding of cellular to disease-associated prion protein prior to conversion. J. Gen. Virol. 86, 2627 2634.
    • (2005) J. Gen. Virol. , vol.86 , pp. 2627-2634
    • Rigter, A.1    Bossers, A.2
  • 37
    • 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. et al. (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, 299 309.
    • (2000) Neurobiol. Dis. , vol.7 , pp. 299-309
    • Thellung, S.1    Florio, T.2    Villa, V.3
  • 38
    • 0036176506 scopus 로고    scopus 로고
    • P38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells
    • Thellung S., Villa V., Corsaro A. et al. (2002) p38 MAP kinase mediates the cell death induced by PrP106-126 in the SH-SY5Y neuroblastoma cells. Neurobiol. Dis. 9, 69 81.
    • (2002) Neurobiol. Dis. , vol.9 , pp. 69-81
    • Thellung, S.1    Villa, V.2    Corsaro, A.3
  • 39
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • Vanik D. L., Surewicz K. A. Surewicz W. K. (2004) Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol. Cell 14, 139 145.
    • (2004) Mol. Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 40
    • 34247553753 scopus 로고    scopus 로고
    • Characterization of the proapoptotic intracellular mechanisms induced by a toxic conformer of the recombinant human prion protein fragment 90-231
    • Villa V., Corsaro A., Thellung S. et al. (2006) Characterization of the proapoptotic intracellular mechanisms induced by a toxic conformer of the recombinant human prion protein fragment 90-231. Ann. N. Y. Acad. Sci. 1090, 276 291.
    • (2006) Ann. N. Y. Acad. Sci. , vol.1090 , pp. 276-291
    • Villa, V.1    Corsaro, A.2    Thellung, S.3
  • 41
    • 2642553049 scopus 로고    scopus 로고
    • Copper induces increased beta-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARR
    • Wong E., Thackray A. M. Bujdoso R. (2004) Copper induces increased beta-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARR. Biochem. J. 380, 273 282.
    • (2004) Biochem. J. , vol.380 , pp. 273-282
    • Wong, E.1    Thackray, A.M.2    Bujdoso, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.