메뉴 건너뛰기




Volumn 9, Issue 12, 2007, Pages 2870-2879

Activation of classical pathway of complement cascade by soluble oligomers of prion

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C1Q; MONOMER; OLIGOMER; PRION PROTEIN;

EID: 35948932203     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2007.01002.x     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0026027948 scopus 로고
    • Computer-assisted kinetic assay for quantification of total complement activity
    • Abbal, M., Tkaczuk, J., Praud, C., Msayeh, F., and Ohayon, E. (1991) Computer-assisted kinetic assay for quantification of total complement activity. Complement Inflamm 8: 92-103.
    • (1991) Complement Inflamm , vol.8 , pp. 92-103
    • Abbal, M.1    Tkaczuk, J.2    Praud, C.3    Msayeh, F.4    Ohayon, E.5
  • 2
    • 0018755977 scopus 로고
    • Differential elution of Clq, Clr and Cls from human Cl bound to immune aggregates. Use in the rapid purification of Cl subcomponents
    • Arlaud, G.J., Sim, R.B., Duplaa, A.M., and Colomb, M.G. (1979) Differential elution of Clq, Clr and Cls from human Cl bound to immune aggregates. Use in the rapid purification of Cl subcomponents. Mol Immunol 16: 445-450.
    • (1979) Mol Immunol , vol.16 , pp. 445-450
    • Arlaud, G.J.1    Sim, R.B.2    Duplaa, A.M.3    Colomb, M.G.4
  • 3
    • 15544372950 scopus 로고    scopus 로고
    • Complement protein C1q recognizes a conformationally modified form of the prion protein
    • Blanquet-Grossard, F., Thielens, N.M., Vendrely, C., Jamin, M., and Arlaud, G.J. (2005) Complement protein C1q recognizes a conformationally modified form of the prion protein. Biochemistry 44: 4349-4356.
    • (2005) Biochemistry , vol.44 , pp. 4349-4356
    • Blanquet-Grossard, F.1    Thielens, N.M.2    Vendrely, C.3    Jamin, M.4    Arlaud, G.J.5
  • 4
    • 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
  • 6
    • 0032746253 scopus 로고    scopus 로고
    • Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells
    • Brown, K.L., Stewart, K., Ritchie, D.L., Mabbott, N.A., Williams, A., Fraser, H., et al. (1999) Scrapie replication in lymphoid tissues depends on prion protein-expressing follicular dendritic cells. Nat Med 5: 1308-1312.
    • (1999) Nat Med , vol.5 , pp. 1308-1312
    • Brown, K.L.1    Stewart, K.2    Ritchie, D.L.3    Mabbott, N.A.4    Williams, A.5    Fraser, H.6
  • 7
    • 0033231290 scopus 로고    scopus 로고
    • Prion protein and the transmissible spongiform encephalopathy diseases
    • Chesebro, B. (1999) Prion protein and the transmissible spongiform encephalopathy diseases. Neuron 24: 503-506.
    • (1999) Neuron , vol.24 , pp. 503-506
    • Chesebro, B.1
  • 8
    • 25844472720 scopus 로고    scopus 로고
    • The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation
    • Cordeiro, Y., Kraineva, J., Gomes, M.P., Lopes, M.H., Martins, V.R., Lima, L.M., et al. (2005) The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation. Biophys J 89: 2667-2676.
    • (2005) Biophys J , vol.89 , pp. 2667-2676
    • Cordeiro, Y.1    Kraineva, J.2    Gomes, M.P.3    Lopes, M.H.4    Martins, V.R.5    Lima, L.M.6
  • 9
    • 0344012497 scopus 로고    scopus 로고
    • The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
    • Gaboriaud, C., Juanhuix, J., Gruez, A., Lacroix, M., Darnault, C., Pignol, D., et al. (2003) The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem 278: 46974-46982.
    • (2003) J Biol Chem , vol.278 , pp. 46974-46982
    • Gaboriaud, C.1    Juanhuix, J.2    Gruez, A.3    Lacroix, M.4    Darnault, C.5    Pignol, D.6
  • 11
    • 0016248833 scopus 로고
    • A new one-step method for the functional assay of the fourth component (C4) of human and guinea pig complement
    • Gaither, T.A., Alling, D.W., and Frank, M.M. (1974) A new one-step method for the functional assay of the fourth component (C4) of human and guinea pig complement. J Immunol 113: 574-583.
    • (1974) J Immunol , vol.113 , pp. 574-583
    • Gaither, T.A.1    Alling, D.W.2    Frank, M.M.3
  • 12
    • 0034943638 scopus 로고    scopus 로고
    • Folding dynamics and energetics of recombinant prion proteins
    • Glockshuber, R. (2001) Folding dynamics and energetics of recombinant prion proteins. Adv Protein Chem 57: 83-105.
    • (2001) Adv Protein Chem , vol.57 , pp. 83-105
    • Glockshuber, R.1
  • 13
    • 25444512040 scopus 로고    scopus 로고
    • Interactions of the extracellular matrix proteoglycans decorin and biglycan with C1q and collectins
    • Groeneveld, T.W., Oroszlan, M., Owens, R.T., Faber-Krol, M.C., Bakker, A.C., Arlaud, G.J., et al. (2005) Interactions of the extracellular matrix proteoglycans decorin and biglycan with C1q and collectins. J Immunol 175: 4715-4723.
    • (2005) J Immunol , vol.175 , pp. 4715-4723
    • Groeneveld, T.W.1    Oroszlan, M.2    Owens, R.T.3    Faber-Krol, M.C.4    Bakker, A.C.5    Arlaud, G.J.6
  • 14
    • 13844259181 scopus 로고    scopus 로고
    • Chronic lymphocytic inflammation specifies the organ tropism of prions
    • Heikenwalder, M., Zeller, N., Seeger, H., Prinz, M., Klohn, P.C., Schwarz, P., et al. (2005) Chronic lymphocytic inflammation specifies the organ tropism of prions. Science 307: 1107-1110.
    • (2005) Science , vol.307 , pp. 1107-1110
    • Heikenwalder, M.1    Zeller, N.2    Seeger, H.3    Prinz, M.4    Klohn, P.C.5    Schwarz, P.6
  • 15
    • 0033947551 scopus 로고    scopus 로고
    • C1q: Structure, function, and receptors
    • Kishore, U., and Reid, K.B. (2000) C1q: Structure, function, and receptors. Immunopharmacology 49: 159-170.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 17
    • 1842791529 scopus 로고    scopus 로고
    • Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro
    • Lawson, V.A., Priola, S.A., Meade-White, K., Lawson, M., and Chesebro, B. (2004) Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro. J Biol Chem 279: 13689-13695.
    • (2004) J Biol Chem , vol.279 , pp. 13689-13695
    • Lawson, V.A.1    Priola, S.A.2    Meade-White, K.3    Lawson, M.4    Chesebro, B.5
  • 18
    • 0035794531 scopus 로고    scopus 로고
    • Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form
    • Leclerc, E., Peretz, D., Ball, H., Sakurai, H., Legname, G., Serban, A., et al. (2001) Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J 20: 1547-1554.
    • (2001) EMBO J , vol.20 , pp. 1547-1554
    • Leclerc, E.1    Peretz, D.2    Ball, H.3    Sakurai, H.4    Legname, G.5    Serban, A.6
  • 20
    • 0034796073 scopus 로고    scopus 로고
    • The immunobiology of TSE diseases
    • Mabbott, N.A., and Bruce, M.E. (2001) The immunobiology of TSE diseases. J Gen Virol 82: 2307-2318.
    • (2001) J Gen Virol , vol.82 , pp. 2307-2318
    • Mabbott, N.A.1    Bruce, M.E.2
  • 21
    • 0034099095 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-deficient, but not interleukin-6-deficient, mice resist peripheral infection with scrapie
    • Mabbott, N.A., Williams, A., Farquhar, C.F., Pasparakis, M., Kollias, G., and Bruce, M.E. (2000) Tumor necrosis factor alpha-deficient, but not interleukin-6-deficient, mice resist peripheral infection with scrapie. J Virol 74: 3338-3344.
    • (2000) J Virol , vol.74 , pp. 3338-3344
    • Mabbott, N.A.1    Williams, A.2    Farquhar, C.F.3    Pasparakis, M.4    Kollias, G.5    Bruce, M.E.6
  • 22
    • 0035053039 scopus 로고    scopus 로고
    • Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie
    • Mabbott, N.A., Bruce, M.E., Botto, M., Walport, M.J., and Pepys, M.B. (2001) Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie. Nat Med 7: 485-487.
    • (2001) Nat Med , vol.7 , pp. 485-487
    • Mabbott, N.A.1    Bruce, M.E.2    Botto, M.3    Walport, M.J.4    Pepys, M.B.5
  • 23
    • 33947145602 scopus 로고    scopus 로고
    • Prion protein activates and fixes complement directly via the classical pathway: Implications for the mechanism of scrapie agent propagation in lymphoid tissue
    • Mitchell, D.A., Kirby, L., Paulin, S.M., Villiers, C.L., and Sim, R.B. (2007) Prion protein activates and fixes complement directly via the classical pathway: Implications for the mechanism of scrapie agent propagation in lymphoid tissue. Mol Immunol 44: 2997-3004.
    • (2007) Mol Immunol , vol.44 , pp. 2997-3004
    • Mitchell, D.A.1    Kirby, L.2    Paulin, S.M.3    Villiers, C.L.4    Sim, R.B.5
  • 24
    • 0034686002 scopus 로고    scopus 로고
    • Impaired prion replication in spleens of mice lacking functional follicular dendritic cells
    • Montrasio, F., Frigg, R., Glatzel, M., Klein, M.A., Mackay, F., Aguzzi, A., and Weissmann, C. (2000) Impaired prion replication in spleens of mice lacking functional follicular dendritic cells. Science 288: 1257-1259.
    • (2000) Science , vol.288 , pp. 1257-1259
    • Montrasio, F.1    Frigg, R.2    Glatzel, M.3    Klein, M.A.4    Mackay, F.5    Aguzzi, A.6    Weissmann, C.7
  • 25
    • 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
  • 26
    • 0022824266 scopus 로고
    • Prions are novel infectious pathogens causing scrapie and Creutzfeldt-Jakob disease
    • Prusiner, S.B. (1986) Prions are novel infectious pathogens causing scrapie and Creutzfeldt-Jakob disease. Bioessays 5: 281-286.
    • (1986) Bioessays , vol.5 , pp. 281-286
    • Prusiner, S.B.1
  • 29
    • 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., et al. (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
  • 30
    • 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
  • 31
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R., and Wuthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett 413: 282-288.
    • (1997) FEBS Lett , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 33
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M., and Dobson, C.M. (2003) Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81: 678-699.
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 34
    • 0035575742 scopus 로고    scopus 로고
    • Beta-amyloid fibrils activate the C1 complex of complement under physiological conditions: Evidence for a binding site for A beta on the C1q globular regions
    • Tacnet-Delorme, P., Chevallier, S., and Arlaud, G.J. (2001) Beta-amyloid fibrils activate the C1 complex of complement under physiological conditions: Evidence for a binding site for A beta on the C1q globular regions. J Immunol 167: 6374-6381.
    • (2001) J Immunol , vol.167 , pp. 6374-6381
    • Tacnet-Delorme, P.1    Chevallier, S.2    Arlaud, G.J.3
  • 35
    • 23144463784 scopus 로고    scopus 로고
    • Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers
    • Vendrely, C., Valadie, H., Bednarova, L., Cardin, L., Pasdeloup, M., Cappadoro, J., et al. (2005) Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers. Biochim Biophys Acta 1724: 355-366.
    • (2005) Biochim Biophys Acta , vol.1724 , pp. 355-366
    • Vendrely, C.1    Valadie, H.2    Bednarova, L.3    Cardin, L.4    Pasdeloup, M.5    Cappadoro, J.6
  • 36
    • 22744435641 scopus 로고    scopus 로고
    • Birth of a prion: Spontaneousgeneration revisited
    • Weissmann, C. (2005) Birth of a prion: Spontaneous generation revisited. Cell 122: 165-168.
    • (2005) Cell , vol.122 , pp. 165-168
    • Weissmann, C.1
  • 37
    • 0025376223 scopus 로고
    • Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin
    • Zgirski, A., and Frieden, E. (1990) Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin. J Inorg Biochem 39: 137-148.
    • (1990) J Inorg Biochem , vol.39 , pp. 137-148
    • Zgirski, A.1    Frieden, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.