메뉴 건너뛰기




Volumn 20, Issue 7, 2006, Pages

Transmissibility of mouse AApoAII amyloid fibrils: Inactivation by physical and chemical methods

Author keywords

Amyloidosis; Disruption; Organic compounds

Indexed keywords

AMYLOID; CEFALEXIN; CHLORAMPHENICOL; ERYTHROMYCIN; FORMALDEHYDE; FORMIC ACID; GUANIDINE; LINCOMYCIN; NORDIHYDROGUAIARETIC ACID; ORGANIC COMPOUND; PENICILLIN G; POLYMYXIN B; PROTEIN AAPOA2; PROTEINASE K; QUERCETIN; RESVERATROL; RIFAMPICIN; STREPTOMYCIN; TETRACYCLINE; THIOFLAVINE; UREA; APOLIPOPROTEIN A2; FORMIC ACID DERIVATIVE;

EID: 33845648426     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.05-4890fje     Document Type: Article
Times cited : (26)

References (55)
  • 1
    • 0032064203 scopus 로고    scopus 로고
    • The pathogenesis of amyloidosis: Understanding general principles
    • Westermark, P. (1998) The pathogenesis of amyloidosis: understanding general principles. Am. J. Pathol. 152, 1125-1127
    • (1998) Am. J. Pathol. , vol.152 , pp. 1125-1127
    • Westermark, P.1
  • 4
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The beta-fibrilloses
    • Glenner, G. G. (1980) Amyloid deposits and amyloidosis. The beta-fibrilloses. N. Engl. J. Med. 302, 1283-1292
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 5
    • 0023024888 scopus 로고
    • Purification and characterization of a senile amyloid-related antigenic substance (apoSASSAM) from mouse serum. apoSASSAM is an apoA-II apolipoprotein of mouse high density lipoproteins
    • Higuchi, K., Yonezu, T., Kogishi, K., Matsumura, A., Takeshita, S., Higuchi, K., Kohno, A., Matsushita, M., Hosokawa, M., and Takeda, T. (1986) Purification and characterization of a senile amyloid-related antigenic substance (apoSASSAM) from mouse serum. apoSASSAM is an apoA-II apolipoprotein of mouse high density lipoproteins. J. Biol. Chem. 261, 12834-12840
    • (1986) J. Biol. Chem. , vol.261 , pp. 12834-12840
    • Higuchi, K.1    Yonezu, T.2    Kogishi, K.3    Matsumura, A.4    Takeshita, S.5    Higuchi, K.6    Kohno, A.7    Matsushita, M.8    Hosokawa, M.9    Takeda, T.10
  • 7
    • 0022456655 scopus 로고
    • High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II
    • Yonezu, T., Higuchi, K., Tsunasawa, S., Takagi, S., Sakiyama, F., and Takeda, T. (1986) High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II. FEBS Lett. 203, 149-152
    • (1986) FEBS Lett. , vol.203 , pp. 149-152
    • Yonezu, T.1    Higuchi, K.2    Tsunasawa, S.3    Takagi, S.4    Sakiyama, F.5    Takeda, T.6
  • 8
    • 0027528408 scopus 로고
    • Development of congenic strains of mice carrying amyloidogenic apolipoprotein A-II (Apoa2c). Apoa2c reduces the plasma level and the size of high density lipoprotein
    • Higuchi, K., Kitado, H., Kitagawa, K., Kogishi, K., Naiki, H., and Takeda, T. (1993) Development of congenic strains of mice carrying amyloidogenic apolipoprotein A-II (Apoa2c). Apoa2c reduces the plasma level and the size of high density lipoprotein. FEBS Lett. 317, 207-210
    • (1993) FEBS Lett. , vol.317 , pp. 207-210
    • Higuchi, K.1    Kitado, H.2    Kitagawa, K.3    Kogishi, K.4    Naiki, H.5    Takeda, T.6
  • 9
    • 0028836331 scopus 로고
    • Apolipoprotein A-II gene and development of amyloidosis and senescence in a congenic strain of mice carrying amyloidogenic ApoA-II
    • Higuchi, K., Naiki, H., Kitagawa, K., Kitado, H., Kogishi, K., Matsushita, T., and Takeda, T. (1995) Apolipoprotein A-II gene and development of amyloidosis and senescence in a congenic strain of mice carrying amyloidogenic ApoA-II. Lab. Invest. 72, 75-82
    • (1995) Lab. Invest. , vol.72 , pp. 75-82
    • Higuchi, K.1    Naiki, H.2    Kitagawa, K.3    Kitado, H.4    Kogishi, K.5    Matsushita, T.6    Takeda, T.7
  • 10
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T., and Lansbury, P. T. Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 11
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen, R. A., Kocisko, D. A., Raymond, G. J., Nandan, S., Lansbury, P. T., and Caughey, B. (1995) Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375, 698-700
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3    Nandan, S.4    Lansbury, P.T.5    Caughey, B.6
  • 13
    • 0033913783 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathies, amyloidoses and yeast prions: Common threads?
    • Caughey, B. (2000) Transmissible spongiform encephalopathies, amyloidoses and yeast prions: common threads? Nat. Med. 6, 751-754
    • (2000) Nat. Med. , vol.6 , pp. 751-754
    • Caughey, B.1
  • 15
    • 0032472239 scopus 로고    scopus 로고
    • BSE and prions: Uncertainties about the agent
    • Chesebro, B. (1998) BSE and prions: uncertainties about the agent. Science 279, 42-43
    • (1998) Science , vol.279 , pp. 42-43
    • Chesebro, B.1
  • 18
    • 0036222206 scopus 로고    scopus 로고
    • Acceleration of murine AA amyloidosis by oral administration of amyloid fibrils extracted from different species
    • Cui, D., Kawano, H., Takahashi, M., Hoshii, Y., Setoguchi, M., Gondo, T., and Ishihara, T. (2002) Acceleration of murine AA amyloidosis by oral administration of amyloid fibrils extracted from different species. Pathol. Int. 52, 40-45
    • (2002) Pathol. Int. , vol.52 , pp. 40-45
    • Cui, D.1    Kawano, H.2    Takahashi, M.3    Hoshii, Y.4    Setoguchi, M.5    Gondo, T.6    Ishihara, T.7
  • 20
    • 0028376473 scopus 로고
    • Induction of beta (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy
    • Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J., and Bruton, C. J. (1994) Induction of beta (A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate. Comparison with transmission of spongiform encephalopathy. Mol. Neurobiol. 8, 25-39
    • (1994) Mol. Neurobiol. , vol.8 , pp. 25-39
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 23
    • 0038218169 scopus 로고    scopus 로고
    • The challenge of prion decontamination
    • McDonnell, G., and Burke, P. (2003) The challenge of prion decontamination. Clin. Infect. Dis. 36, 1152-1154
    • (2003) Clin. Infect. Dis. , vol.36 , pp. 1152-1154
    • McDonnell, G.1    Burke, P.2
  • 28
    • 0029863551 scopus 로고    scopus 로고
    • Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger
    • Tomiyama, T., Shoji, A., Kataoka, K., Suwa, Y., Asano, S., Kaneko, H., and Endo, N. (1996) Inhibition of amyloid beta protein aggregation and neurotoxicity by rifampicin. Its possible function as a hydroxyl radical scavenger. J. Biol. Chem. 271, 6839-6844
    • (1996) J. Biol. Chem. , vol.271 , pp. 6839-6844
    • Tomiyama, T.1    Shoji, A.2    Kataoka, K.3    Suwa, Y.4    Asano, S.5    Kaneko, H.6    Endo, N.7
  • 29
    • 0036313066 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's beta-amyloid fibrils in vitro
    • Ono, K., Hasegawa, K., Yoshiike, Y., Takashima, A., Yamada, M., and Naiki, H. (2002) Nordihydroguaiaretic acid potently breaks down pre-formed Alzheimer's beta-amyloid fibrils in vitro. J. Neurochem. 81, 434-440
    • (2002) J. Neurochem. , vol.81 , pp. 434-440
    • Ono, K.1    Hasegawa, K.2    Yoshiike, Y.3    Takashima, A.4    Yamada, M.5    Naiki, H.6
  • 30
    • 0014591878 scopus 로고
    • Physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations
    • Pras, M., Zucker-Franklin, D., Rimon, A., and Franklin, E. C. (1969) physical, chemical, and ultrastructural studies of water-soluble human amyloid fibrils. Comparative analyses of nine amyloid preparations. J. Exp. Med. 130, 777-796
    • (1969) J. Exp. Med. , vol.130 , pp. 777-796
    • Pras, M.1    Zucker-Franklin, D.2    Rimon, A.3    Franklin, E.C.4
  • 32
    • 0032878280 scopus 로고    scopus 로고
    • Mouse senile amyloid deposition is suppressed by adenovirus-mediated overexpression of amyloid-resistant apolipoprotein A-II
    • Chiba, T., Kogishi, K., Wang, J., Xia, C., Matsushita, T., Miyazaki, J., Saito, I., Hosokawa, M., and Higuchi, K. (1999) Mouse senile amyloid deposition is suppressed by adenovirus-mediated overexpression of amyloid-resistant apolipoprotein A-II. Am. J. Pathol. 155, 1319-1326
    • (1999) Am. J. Pathol. , vol.155 , pp. 1319-1326
    • Chiba, T.1    Kogishi, K.2    Wang, J.3    Xia, C.4    Matsushita, T.5    Miyazaki, J.6    Saito, I.7    Hosokawa, M.8    Higuchi, K.9
  • 33
    • 0025371975 scopus 로고
    • Alzheimer's beta-amyloid protein is covalently modified when dissolved in formic acid
    • Klunk, W. E., and Pettegrew, J. W. (1990) Alzheimer's beta-amyloid protein is covalently modified when dissolved in formic acid. J. Neurochem. 54, 2050-2056
    • (1990) J. Neurochem. , vol.54 , pp. 2050-2056
    • Klunk, W.E.1    Pettegrew, J.W.2
  • 34
    • 0027363495 scopus 로고
    • Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
    • Safar, J., Roller, P. P., Gajdusek, D. C., and Gibbs, C. J. Jr. (1993) Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein. Sci. 2, 2206-2216
    • (1993) Protein. Sci. , vol.2 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 35
    • 0021363548 scopus 로고
    • Sodium hydroxide decontamination of Creutzfeldt-Jakob disease virus
    • Brown, P., Rohwer, R. G., and Gajdusek, D. C. (1984) Sodium hydroxide decontamination of Creutzfeldt-Jakob disease virus. N. Engl. J. Med. 310, 727
    • (1984) N. Engl. J. Med. , vol.310 , pp. 727
    • Brown, P.1    Rohwer, R.G.2    Gajdusek, D.C.3
  • 36
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation and unfolding of scrapie amyloid (prion) protein
    • Safar, J., Roller, P. P., Gajdusek, D. C., and Gibbs, C. J. Jr. (1993) Conformational transitions, dissociation and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268, 20276-20284
    • (1993) J. Biol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 37
    • 0034707048 scopus 로고    scopus 로고
    • Binding of disease-associated prion protein to plasminogen
    • Fischer, M. B., Roeckl, C., Parizek, P., Schwarz, H. P., and Aguzzi, A. (2000) Binding of disease-associated prion protein to plasminogen. Nature 408, 479-483
    • (2000) Nature , vol.408 , pp. 479-483
    • Fischer, M.B.1    Roeckl, C.2    Parizek, P.3    Schwarz, H.P.4    Aguzzi, A.5
  • 38
    • 0141668941 scopus 로고    scopus 로고
    • Folding and stability of the extracellular domain of the human amyloid precursor protein
    • Botelho, M. G., Gralle, M., Oliveira, C. L., Torriani, I., and Ferreira, S. T. (2003) Folding and stability of the extracellular domain of the human amyloid precursor protein. J. Biol. Chem. 278, 34,259-34,267
    • (2003) J. Biol. Chem. , vol.278
    • Botelho, M.G.1    Gralle, M.2    Oliveira, C.L.3    Torriani, I.4    Ferreira, S.T.5
  • 39
    • 0020032352 scopus 로고
    • Effect of chemicals, heat, and histopathologic processing on high-infectivity hamster-adapted scrapie virus
    • Brown, P., Rohwer, R. G., Green, E. M., and Gajdusek, D. C. (1982) Effect of chemicals, heat, and histopathologic processing on high-infectivity hamster-adapted scrapie virus. J. Infect. Dis. 145, 683-687
    • (1982) J. Infect. Dis. , vol.145 , pp. 683-687
    • Brown, P.1    Rohwer, R.G.2    Green, E.M.3    Gajdusek, D.C.4
  • 42
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault, N. R., Lucassen, R. W., and Supattapone, S. (2003) RNA molecules stimulate prion protein conversion. Nature 425, 717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3
  • 43
    • 0033066555 scopus 로고    scopus 로고
    • Infectivity of scrapie prions bound to a stainless steel surface
    • Zobeley, E., Flechsig, E., Cozzio, A., Enari, M., and Weissmann, C. (1999) Infectivity of scrapie prions bound to a stainless steel surface. Mol. Med. 5, 240-243
    • (1999) Mol. Med. , vol.5 , pp. 240-243
    • Zobeley, E.1    Flechsig, E.2    Cozzio, A.3    Enari, M.4    Weissmann, C.5
  • 45
    • 22144462135 scopus 로고    scopus 로고
    • Neurotoxic protein oligomers-what you see is not always what you get
    • Bitan, G., Fradinger, E. A., Spring, S. M., and Teplow, D. B. (2005) Neurotoxic protein oligomers-what you see is not always what you get. Amyloid 12, 88-95
    • (2005) Amyloid , vol.12 , pp. 88-95
    • Bitan, G.1    Fradinger, E.A.2    Spring, S.M.3    Teplow, D.B.4
  • 46
    • 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
  • 47
    • 0036377156 scopus 로고    scopus 로고
    • Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease
    • Zerovnik, E. (2002) Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease. Eur. J. Biochem. 269, 3362-3371
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3362-3371
    • Zerovnik, E.1
  • 49
    • 0037592927 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence
    • Ban, T., Hamada, D., Hasegawa, K., Naiki, H., and Goto, Y. (2003) Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. J. Biol. Chem. 278, 16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 51
    • 0035808264 scopus 로고    scopus 로고
    • Anti-amyloidogenic activity of tetracyclines: Studies in vitro
    • Forloni, G., Colombo, L., Girola, L., Tagliavini, F., and Salmona, M. (2001) Anti-amyloidogenic activity of tetracyclines: studies in vitro. FEBS Lett. 487, 404-407
    • (2001) FEBS Lett. , vol.487 , pp. 404-407
    • Forloni, G.1    Colombo, L.2    Girola, L.3    Tagliavini, F.4    Salmona, M.5
  • 52
    • 0038375018 scopus 로고    scopus 로고
    • 4′-iodo-4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: Screening for TTR fibril disrupters
    • Cardoso, I., Merlini, G., and Saraiva, M. J. (2003) 4′-iodo- 4′-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters. FASEB J. 17, 803-809
    • (2003) FASEB J. , vol.17 , pp. 803-809
    • Cardoso, I.1    Merlini, G.2    Saraiva, M.J.3
  • 53
    • 0032559003 scopus 로고    scopus 로고
    • Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer'sedimentary coeffcient beta-amyloid fibril formation in vitro
    • Naiki, H., Hasegawa, K., Yamaguchi, I., Nakamura, H., Geiyo, F., and Nakakuki, K. (1998) Apolipoprotein E and antioxidants have different mechanisms of inhibiting Alzheimer'sedimentary coeffcient beta-amyloid fibril formation in vitro. Biochemistry 37, 17,882-17,889
    • (1998) Biochemistry , vol.37
    • Naiki, H.1    Hasegawa, K.2    Yamaguchi, I.3    Nakamura, H.4    Geiyo, F.5    Nakakuki, K.6
  • 54
    • 4944236514 scopus 로고    scopus 로고
    • Nordihydroguaiaretic acid does not disaggregate beta-amyloid (1-40) protofibrils but does inhibit growth arising from direct protofibril association
    • Moss, M. A., Varvel, N. H., Nichols, M. R., Reed, D. K., and Rosenberry, T. L. (2004) Nordihydroguaiaretic acid does not disaggregate beta-amyloid (1-40) protofibrils but does inhibit growth arising from direct protofibril association. Mol. Pharmacol. 66, 592-600
    • (2004) Mol. Pharmacol. , vol.66 , pp. 592-600
    • Moss, M.A.1    Varvel, N.H.2    Nichols, M.R.3    Reed, D.K.4    Rosenberry, T.L.5
  • 55
    • 0141642253 scopus 로고    scopus 로고
    • Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: Implications for the prevention and therapeutics of Alzheimer's disease
    • Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., and Yamada, M. (2003) Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease. J. Neurochem. 87, 172-181
    • (2003) J. Neurochem. , vol.87 , pp. 172-181
    • Ono, K.1    Yoshiike, Y.2    Takashima, A.3    Hasegawa, K.4    Naiki, H.5    Yamada, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.