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Volumn 415, Issue 2, 2008, Pages 207-215

Diffusible amyloid oligomers trigger systemic amyloidosis in mice

Author keywords

Amyloid protein A; Diffusible amyloid oligomer; Inflammation; Systemic amyloidosis

Indexed keywords

AGGLOMERATION; BODY FLUIDS; CELL DEATH; MONOMERS; NUCLEATION; OLIGOMERS; POLYMERS; PURIFICATION; TOXIC MATERIALS;

EID: 54049149755     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071696     Document Type: Article
Times cited : (11)

References (37)
  • 1
    • 0029068027 scopus 로고
    • Amyloidasis
    • Hawkins, P. N. (1995) Amyloidasis. Blood Rev. 9, 135-142
    • (1995) Blood Rev , vol.9 , pp. 135-142
    • Hawkins, P.N.1
  • 3
    • 0035961291 scopus 로고    scopus 로고
    • Pathogenesis, diagnosis and treatment of systemic amyloidosis
    • Pepys, M. B. (2001) Pathogenesis, diagnosis and treatment of systemic amyloidosis. Philos. Trans. R. Soc. London B Biol. Sci. 356, 203-210
    • (2001) Philos. Trans. R. Soc. London B Biol. Sci , vol.356 , pp. 203-210
    • Pepys, M.B.1
  • 5
    • 0026555175 scopus 로고
    • The N-terminal segment of protein AA determines its fibrillogenic property
    • Westermark, G. T., Engstrom, U. and Westermark, P. (1992) The N-terminal segment of protein AA determines its fibrillogenic property. Biochem. Biophys. Res. Commun. 182, 27-33
    • (1992) Biochem. Biophys. Res. Commun , vol.182 , pp. 27-33
    • Westermark, G.T.1    Engstrom, U.2    Westermark, P.3
  • 7
    • 0033021099 scopus 로고    scopus 로고
    • A cell culture system for the study of amyloid pathogenesis. Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A
    • Kluve-Beckerman, B., Liepnieks, J. J., Wang, L. and Benson, M. D. (1999) A cell culture system for the study of amyloid pathogenesis. Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A. Am. J. Pathol. 155, 123-133
    • (1999) Am. J. Pathol , vol.155 , pp. 123-133
    • Kluve-Beckerman, B.1    Liepnieks, J.J.2    Wang, L.3    Benson, M.D.4
  • 9
    • 22844437405 scopus 로고    scopus 로고
    • Purification of amyloid protein AA subspecies from amyloid-rich human tissues
    • Westermark, G. T. and Westermark, P. (2005) Purification of amyloid protein AA subspecies from amyloid-rich human tissues. Methods Mol. Biol. 299, 243-254
    • (2005) Methods Mol. Biol , vol.299 , pp. 243-254
    • Westermark, G.T.1    Westermark, P.2
  • 10
    • 0028286663 scopus 로고
    • Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-amyloidosis in mice
    • Ganowiak, K., Hultman, P., Engstrom, U., Gustavsson, A. and Westermark, P. (1994) Fibrils from synthetic amyloid-related peptides enhance development of experimental AA-amyloidosis in mice. Biochem. Biophys. Res. Commun. 199, 306-312
    • (1994) Biochem. Biophys. Res. Commun , vol.199 , pp. 306-312
    • Ganowiak, K.1    Hultman, P.2    Engstrom, U.3    Gustavsson, A.4    Westermark, P.5
  • 12
    • 0028118464 scopus 로고
    • Interaction between circulating amyloid fibril protein precursors and extracellular tissue matrix components in the pathogenesis of systemic amyloidosis
    • Husby, G., Stenstad, T., Magnus, J. H., Sletten, K., Nordvag, B. Y. and Clin, M. G. (1994) Interaction between circulating amyloid fibril protein precursors and extracellular tissue matrix components in the pathogenesis of systemic amyloidosis. Immunol. Immunopathol. 70, 2-9
    • (1994) Immunol. Immunopathol , vol.70 , pp. 2-9
    • Husby, G.1    Stenstad, T.2    Magnus, J.H.3    Sletten, K.4    Nordvag, B.Y.5    Clin, M.G.6
  • 13
    • 0017411543 scopus 로고
    • Murine amyloid protein AA in casein-induced experimental amyloidosis
    • Skinner, M., Shirahama, T., Benson, M. D. and Cohen, A. S. (1977) Murine amyloid protein AA in casein-induced experimental amyloidosis. Lab. Invest. 36, 420-427
    • (1977) Lab. Invest , vol.36 , pp. 420-427
    • Skinner, M.1    Shirahama, T.2    Benson, M.D.3    Cohen, A.S.4
  • 14
    • 0014592387 scopus 로고
    • Experimental murine amyloid. IV. Amyloidosis and immunoglobulins
    • Willerson, J. T., Asofsky, R. and Barth, W. F. (1969) Experimental murine amyloid. IV. Amyloidosis and immunoglobulins. J. Immunol. 103, 741-749
    • (1969) J. Immunol , vol.103 , pp. 741-749
    • Willerson, J.T.1    Asofsky, R.2    Barth, W.F.3
  • 18
    • 0020308923 scopus 로고
    • The association of amyloid P-component (AP) with the amyloid fibril: An updated method for amyloid fibril protein isolation
    • Skinner, M., Shirahama, T., Cohen, A. S. and Deal, C. L. (1982) The association of amyloid P-component (AP) with the amyloid fibril: an updated method for amyloid fibril protein isolation. Prep. Biochem. 12, 461-476
    • (1982) Prep. Biochem , vol.12 , pp. 461-476
    • Skinner, M.1    Shirahama, T.2    Cohen, A.S.3    Deal, C.L.4
  • 20
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chili. F. and Dobson, C. M. (2006) Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chili, F.1    Dobson, C.M.2
  • 22
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N. and Woody. R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 23
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong. A., Huang, P. and Caughey, W. S. (1990) Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29, 3303-3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 25
    • 0037151046 scopus 로고    scopus 로고
    • Accelerated plaque accumulation, associative learning deficits, and up-regulation of α7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins
    • Dineley, K. T., Xia, X., Bui, D., Sweatt, J. D. and Zheng, H. (2002) Accelerated plaque accumulation, associative learning deficits, and up-regulation of α7 nicotinic receptor protein in transgenic mice co-expressing mutant human presenilin 1 and amyloid precursor proteins. J. Biol. Chem. 277, 22768-22780
    • (2002) J. Biol. Chem , vol.277 , pp. 22768-22780
    • Dineley, K.T.1    Xia, X.2    Bui, D.3    Sweatt, J.D.4    Zheng, H.5
  • 27
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar, C. M. and Whitehead, A. S. (1999) Serum amyloid A, the major vertebrate acute-phase reactant. Eur. J. Biochem. 265, 501-523
    • (1999) Eur. J. Biochem , vol.265 , pp. 501-523
    • Uhlar, C.M.1    Whitehead, A.S.2
  • 28
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali, R. and Wetzel, R. (2007) Polymorphism in the intermediates and products of amyloid assembly. Curr. Opin. Struct. Biol. 17, 48-57
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 29
    • 34547947641 scopus 로고    scopus 로고
    • Conversion of non-fibrillar β-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation
    • Benseny-Cases, N., Cocera, M. and Cladera, J. (2007) Conversion of non-fibrillar β-sheet oligomers into amyloid fibrils in Alzheimer's disease amyloid peptide aggregation. Biochem. Biophys. Res. Commun. 361, 916-921
    • (2007) Biochem. Biophys. Res. Commun , vol.361 , pp. 916-921
    • Benseny-Cases, N.1    Cocera, M.2    Cladera, J.3
  • 30
    • 1542315306 scopus 로고    scopus 로고
    • Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation
    • Gu, Z., Zhu, X., Ni, S., Su, Z. and Zhou, H. M. (2004) Conformational changes of lysozyme refolding intermediates and implications for aggregation and renaturation. Int. J. Biochem. Cell Biol. 36, 795-805
    • (2004) Int. J. Biochem. Cell Biol , vol.36 , pp. 795-805
    • Gu, Z.1    Zhu, X.2    Ni, S.3    Su, Z.4    Zhou, H.M.5
  • 31
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and tibril branching by the Alzheimer's disease amyloid-β protein
    • Harper, J. D., Lieber, C. M. and Lansbury, Jr, P. T. (1997) Atomic force microscopic imaging of seeded fibril formation and tibril branching by the Alzheimer's disease amyloid-β protein. Chem. Biol. 4, 951-959
    • (1997) Chem. Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr, P.T.3
  • 32
    • 0029670277 scopus 로고    scopus 로고
    • Stine, Jr, W. B., Snyder, S. W.. Ladror, U. S., Wade, W. S., Miller, M. F, Perun, T. J., Holzman, T. F. and Krafft, G. A. (1996) The nanometer-scale structure of amyloid-β visualized by atomic force microscopy. J. Protein Chem. 15, 193-203
    • Stine, Jr, W. B., Snyder, S. W.. Ladror, U. S., Wade, W. S., Miller, M. F, Perun, T. J., Holzman, T. F. and Krafft, G. A. (1996) The nanometer-scale structure of amyloid-β visualized by atomic force microscopy. J. Protein Chem. 15, 193-203
  • 33
    • 28244446220 scopus 로고    scopus 로고
    • Aspects on human amyloid forms and their fibril polypeptides
    • Westermark, P. (2005) Aspects on human amyloid forms and their fibril polypeptides. FEBS J. 272, 5942-5949
    • (2005) FEBS J , vol.272 , pp. 5942-5949
    • Westermark, P.1
  • 34
    • 0034806294 scopus 로고    scopus 로고
    • Expression of serum amyloid A genes in mouse brain: Unprecedented response to inflammatory mediators
    • Tucker, P. C. and Sack, Jr. G. H. (2001) Expression of serum amyloid A genes in mouse brain: unprecedented response to inflammatory mediators. FASEB J. 15, 2241-2246
    • (2001) FASEB J , vol.15 , pp. 2241-2246
    • Tucker, P.C.1    Sack Jr., G.H.2
  • 36
    • 0033566744 scopus 로고    scopus 로고
    • Persistent expression of serum amyloid A during experimentally induced chronic inflammatory condition in rabbit involves differential activation of SAF, NF-κB, and C/EBP transcription factors
    • Ray, A. and Ray, B. K. (1999) Persistent expression of serum amyloid A during experimentally induced chronic inflammatory condition in rabbit involves differential activation of SAF, NF-κB, and C/EBP transcription factors. J. Immunol. 163, 2143-2150
    • (1999) J. Immunol , vol.163 , pp. 2143-2150
    • Ray, A.1    Ray, B.K.2
  • 37
    • 0037101616 scopus 로고    scopus 로고
    • Inflammation-dependent cerebral deposition of serum amyloid a protein in a mouse model of amyloidosis
    • Guo, J. T., Yu, J., Grass, D., de Beer, F. C. and Kindy, M. S. (2002) Inflammation-dependent cerebral deposition of serum amyloid a protein in a mouse model of amyloidosis. J. Neurosci. 22, 5900-5909
    • (2002) J. Neurosci , vol.22 , pp. 5900-5909
    • Guo, J.T.1    Yu, J.2    Grass, D.3    de Beer, F.C.4    Kindy, M.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.