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Volumn 103, Issue 6, 2007, Pages 2597-2609

Intracellular accumulation of a mild-denatured monomer of the human PrP fragment 90-231, as possible mechanism of its neurotoxic effects

Author keywords

Intracellular internalization; Neurotoxicity; Protein aggregation; PrP90 231

Indexed keywords

MONOMER; PRION PROTEIN; PROTEIN PRP 90 231; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ISOPROTEIN; NEUROTOXIN; PEPTIDE FRAGMENT; PRION PROTEIN (90 231); PRION PROTEIN (90-231);

EID: 40549105157     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2007.04965.x     Document Type: Article
Times cited : (29)

References (51)
  • 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. and 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
    • 33745047301 scopus 로고    scopus 로고
    • Prion diseases of humans and farm animals: Epidemiology, genetics, and pathogenesis
    • Aguzzi A. (2006) Prion diseases of humans and farm animals: epidemiology, genetics, and pathogenesis. J. Neurochem. 97, 1726-1739.
    • (2006) J. Neurochem , vol.97 , pp. 1726-1739
    • Aguzzi, A.1
  • 4
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Baskakov I. V., Legname G., Prusiner S. B. and Cohen F. E. (2001) Folding of prion protein to its native alpha-helical conformation is under kinetic control. J. Biol. Chem. 276, 19687-19690.
    • (2001) J. Biol. Chem , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 6
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova O. V., Breydo L., Parfenov A. S., Salnikov V. V. and Baskakov I. V. (2005) In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J. Mol. Biol. 346, 645-659.
    • (2005) J. Mol. Biol , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 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
  • 10
    • 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, 743-763.
    • (2001) Neurobiol. Dis , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 33847166240 scopus 로고    scopus 로고
    • Neurotoxic and gliotrophic activity of a synthetic peptide homologous to Gerstmann-Straussler- Scheinker disease amyloid protein
    • Fioriti L., Angeretti N., Colombo L. et al. (2007) Neurotoxic and gliotrophic activity of a synthetic peptide homologous to Gerstmann-Straussler- Scheinker disease amyloid protein. J. Neurosci. 27, 1576-1583.
    • (2007) J. Neurosci , vol.27 , pp. 1576-1583
    • Fioriti, L.1    Angeretti, N.2    Colombo, L.3
  • 15
    • 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, 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
  • 16
    • 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
  • 18
    • 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
  • 19
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A. L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 20
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C. and Selkoe D. J. (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8, 101-112.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 21
    • 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. and 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
  • 22
    • 0032933448 scopus 로고    scopus 로고
    • Jackson G. S., Hill A. F., Joseph C., Hosszu L., Power A., Waltho J. P., Clarke A. R. and Collinge J. (1999) Multiple folding pathways for heterologously expressed human prion protein. Biochim. Biophys. Acta 1431, 1-
    • Jackson G. S., Hill A. F., Joseph C., Hosszu L., Power A., Waltho J. P., Clarke A. R. and Collinge J. (1999) Multiple folding pathways for heterologously expressed human prion protein. Biochim. Biophys. Acta 1431, 1-
  • 24
    • 0036381074 scopus 로고    scopus 로고
    • Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules
    • Kourie J. I. and Henry C. L. (2002) Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules. Clin. Exp. Pharmacol. Physiol. 29, 741-753.
    • (2002) Clin. Exp. Pharmacol. Physiol , vol.29 , pp. 741-753
    • Kourie, J.I.1    Henry, C.L.2
  • 25
    • 34247185404 scopus 로고    scopus 로고
    • Disease-associated prion protein oligomers inhibit the 26S proteasome
    • Kristiansen M., Deriziotis P., Dimcheff D. E. et al. (2007) Disease-associated prion protein oligomers inhibit the 26S proteasome. Mol. Cell 26, 175-188.
    • (2007) Mol. Cell , vol.26 , pp. 175-188
    • Kristiansen, M.1    Deriziotis, P.2    Dimcheff, D.E.3
  • 26
    • 7944239531 scopus 로고    scopus 로고
    • The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites
    • Leffers K. W., Schell J., Jansen K., Lucassen R., Kaimann T., Nagel-Steger L., Tatzelt J. and Riesner D. (2004) The structural transition of the prion protein into its pathogenic conformation is induced by unmasking hydrophobic sites. J. Mol. Biol. 344, 839-853.
    • (2004) J. Mol. Biol , vol.344 , pp. 839-853
    • Leffers, K.W.1    Schell, J.2    Jansen, K.3    Lucassen, R.4    Kaimann, T.5    Nagel-Steger, L.6    Tatzelt, J.7    Riesner, D.8
  • 28
    • 15844419908 scopus 로고    scopus 로고
    • High-level expression and characterization of a purified 142-residue polypeptide of the prion protein
    • Mehlhorn I., Groth D., Stockel J. et al. (1996) High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35, 5528-5537.
    • (1996) Biochemistry , vol.35 , pp. 5528-5537
    • Mehlhorn, I.1    Groth, D.2    Stockel, J.3
  • 29
    • 0027233992 scopus 로고
    • Cytoprotective effect of NMDA receptor antagonists on prion protein (PrionSc)-induced toxicity in rat cortical cell cultures
    • Muller W. E., Ushijima H., Schroder H. C., Forrest J. M., Schatton W. F., Rytik P. G. and Heffner-Lauc M. (1993) Cytoprotective effect of NMDA receptor antagonists on prion protein (PrionSc)-induced toxicity in rat cortical cell cultures. Eur. J. Pharmacol. 246, 261-267.
    • (1993) Eur. J. Pharmacol , vol.246 , pp. 261-267
    • Muller, W.E.1    Ushijima, H.2    Schroder, H.C.3    Forrest, J.M.4    Schatton, W.F.5    Rytik, P.G.6    Heffner-Lauc, M.7
  • 30
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Epub 12006 Mar 13822
    • Novitskaya V., Bocharova O. V., Bronstein I. and Baskakov I. V. (2006) Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J. Biol. Chem. 281, 13828-13836. Epub 12006 Mar 13822.
    • (2006) J. Biol. Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 31
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 32
    • 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
  • 35
    • 14744284214 scopus 로고    scopus 로고
    • Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities
    • Rezaei H., Eghiaian F., Perez J., Doublet B., Choiset Y., Haertle T. and Grosclaude J. (2005) Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J. Mol. Biol. 347, 665-679.
    • (2005) J. Mol. Biol , vol.347 , pp. 665-679
    • Rezaei, H.1    Eghiaian, F.2    Perez, J.3    Doublet, B.4    Choiset, Y.5    Haertle, T.6    Grosclaude, J.7
  • 36
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout H. J., Lang-Rollin I. and Stefanis L. (2004) Involvement of macroautophagy in the dissolution of neuronal inclusions. Int. J. Biochem. Cell Biol. 36, 2551-2562.
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 37
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C. A. and Poirier M. A. (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10(Suppl.), S10-S17.
    • (2004) Nat. Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 38
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein D. C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780-786.
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 39
    • 0033567401 scopus 로고    scopus 로고
    • Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126
    • Salmona M., Malesani P., De Gioia L. et al. (1999) Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106-126. Biochem. J. 342, 207-214.
    • (1999) Biochem. J , vol.342 , pp. 207-214
    • Salmona, M.1    Malesani, P.2    De Gioia, L.3
  • 40
    • 0141841804 scopus 로고    scopus 로고
    • Association of an 11-12 kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt-Jakob disease and other prion diseases
    • Satoh K., Muramoto T., Tanaka T., Kitamoto N., Ironside J. W., Nagashima K., Yamada M., Sato T., Mohri S. and Kitamoto T. (2003) Association of an 11-12 kDa protease-resistant prion protein fragment with subtypes of dura graft-associated Creutzfeldt-Jakob disease and other prion diseases. J. Gen. Virol. 84, 2885-2893.
    • (2003) J. Gen. Virol , vol.84 , pp. 2885-2893
    • Satoh, K.1    Muramoto, T.2    Tanaka, T.3    Kitamoto, N.4    Ironside, J.W.5    Nagashima, K.6    Yamada, M.7    Sato, T.8    Mohri, S.9    Kitamoto, T.10
  • 42
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein
    • Sokolowski F., Modler A. J., Masuch R., Zirwer D., Baier M., Lutsch G., Moss D. A., Gast K. and Naumann D. (2003) Formation of critical oligomers is a key event during conformational transition of recombinant syrian hamster prion protein. J. Biol. Chem. 278, 40481-40492.
    • (2003) J. Biol. Chem , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Masuch, R.3    Zirwer, D.4    Baier, M.5    Lutsch, G.6    Moss, D.A.7    Gast, K.8    Naumann, D.9
  • 43
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki W., Morillas M., Chen S. G., Gambetti P. and Surewicz W. K. (2000) Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry 39, 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 44
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor J. P., Hardy J. and Fischbeck K. H. (2002) Toxic proteins in neurodegenerative disease. Science 296, 1991-1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 46
    • 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. (2000b) 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
  • 49
    • 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
  • 51
    • 0141577720 scopus 로고    scopus 로고
    • Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease
    • Zou W. Q., Capellari S., Parchi P., Sy M. S., Gambetti P. and Chen S. G. (2003) Identification of novel proteinase K-resistant C-terminal fragments of PrP in Creutzfeldt-Jakob disease. J. Biol. Chem. 278, 40429-40436.
    • (2003) J. Biol. Chem , vol.278 , pp. 40429-40436
    • Zou, W.Q.1    Capellari, S.2    Parchi, P.3    Sy, M.S.4    Gambetti, P.5    Chen, S.G.6


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