메뉴 건너뛰기




Volumn 74, Issue 1, 2000, Pages 222-230

Effect of Congo red on wild-type and mutated prion proteins in cultured cells

Author keywords

Congo red; Prion protein; Transmissible spongiform encephalopathies

Indexed keywords

CONGO RED; GLYCOSAMINOGLYCAN; PRION PROTEIN;

EID: 0033961817     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0740222.x     Document Type: Article
Times cited : (36)

References (48)
  • 1
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen R. A. and Marsh R. F. (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859-7868.
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 2
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt D. R., Taraboulos A., and Prusiner S. B. (1992) Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem. 267, 16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 3
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in triton X-114 solution
    • Bordier C. (1981) Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256, 1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 6
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo red
    • Caughey B. and Race R. E. (1992) Potent inhibition of scrapie-associated PrP accumulation by Congo red. J. Neurochem. 59, 768-771.
    • (1992) J. Neurochem. , vol.59 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 7
    • 0027535855 scopus 로고
    • Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells
    • Caughey B. and Raymond G. J. (1993) Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J. Virol. 67, 643-650.
    • (1993) J. Virol. , vol.67 , pp. 643-650
    • Caughey, B.1    Raymond, G.J.2
  • 8
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): Implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B., Raymond G. J., Ernst D., and Race R. E. (1991a) N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65, 6597-6603.
    • (1991) J. Virol. , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 9
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey B. W., Dong A., Bhat K. S., Ernst D., Hayes S. F., and Caughey W. S. (1991b) Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30, 7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 10
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and Congo red
    • Caughey B., Brown K., Raymond G. J., Katzenstein G. E., and Thresher W. (1994) Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and Congo red. J. Virol. 68, 2135-2141.
    • (1994) J. Virol. , vol.68 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3    Katzenstein, G.E.4    Thresher, W.5
  • 11
    • 0029583794 scopus 로고
    • Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state
    • Caughey B., Kocisko D. A., Raymond G. J., and Lansbury P. T. Jr. (1995) Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2, 807-817.
    • (1995) Chem. Biol. , vol.2 , pp. 807-817
    • Caughey, B.1    Kocisko, D.A.2    Raymond, G.J.3    Lansbury P.T., Jr.4
  • 12
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • Chiesa R., Piccardo P., Ghetti B., and Harris D. A. (1998) Neurological illness in transgenic mice expressing a prion protein with an insertional mutation. Neuron 21, 1339-1351.
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 13
    • 0030896803 scopus 로고    scopus 로고
    • Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells
    • Daude N., Lehmann S., and Harris D. A. (1997) Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604-11612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11604-11612
    • Daude, N.1    Lehmann, S.2    Harris, D.A.3
  • 14
    • 0031797266 scopus 로고    scopus 로고
    • Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation
    • Demaimay R., Harper J., Gordon H., Weaver D., Chesebro B., and Caughey B. (1998) Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation. J. Neurochem. 71, 2534-2541.
    • (1998) J. Neurochem. , vol.71 , pp. 2534-2541
    • Demaimay, R.1    Harper, J.2    Gordon, H.3    Weaver, D.4    Chesebro, B.5    Caughey, B.6
  • 15
    • 0033050207 scopus 로고    scopus 로고
    • Effectiveness of polyene antibiotics in treatment of transmissible spongiform encephalopathy in transgenic mice expressing Syrian hamster PrP only in neurons
    • Demaimay R., Race R., and Chesebro B. (1999) Effectiveness of polyene antibiotics in treatment of transmissible spongiform encephalopathy in transgenic mice expressing Syrian hamster PrP only in neurons. J. Virol. 73, 3511-3513.
    • (1999) J. Virol. , vol.73 , pp. 3511-3513
    • Demaimay, R.1    Race, R.2    Chesebro, B.3
  • 16
  • 17
    • 0021282464 scopus 로고
    • Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen
    • Ehlers B. and Diringer H. (1984) Dextran sulphate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J. Gen. Virol. 65, 1325-1330.
    • (1984) J. Gen. Virol. , vol.65 , pp. 1325-1330
    • Ehlers, B.1    Diringer, H.2
  • 18
    • 0022609913 scopus 로고
    • Prolongation of scrapie incubation period by an injection of dextran sulphate 500 within the month before or after infection
    • Farquhar C. F. and Dickinson A. G. (1986) Prolongation of scrapie incubation period by an injection of dextran sulphate 500 within the month before or after infection. J. Gen. Virol. 67, 463-473.
    • (1986) J. Gen. Virol. , vol.67 , pp. 463-473
    • Farquhar, C.F.1    Dickinson, A.G.2
  • 20
    • 0023958458 scopus 로고
    • Screening of monoclonal antibodies using antigens labeled with acetylcholinesterase: Application to the peripheral proteins of photosystem 1
    • Grassi J., Frobert Y., Lamourette P., and Lagoutte B. (1988) Screening of monoclonal antibodies using antigens labeled with acetylcholinesterase: application to the peripheral proteins of photosystem 1. Anal. Biochem. 168, 436-450.
    • (1988) Anal. Biochem. , vol.168 , pp. 436-450
    • Grassi, J.1    Frobert, Y.2    Lamourette, P.3    Lagoutte, B.4
  • 21
    • 0028970386 scopus 로고
    • Congo red prolongs the incubation period in scrapie-infected hamsters
    • Ingrosso L., Ladogana A., and Pocchiari M. (1995) Congo red prolongs the incubation period in scrapie-infected hamsters. J. Virol. 69, 506-508.
    • (1995) J. Virol. , vol.69 , pp. 506-508
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 24
    • 0022450560 scopus 로고
    • Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions
    • Kimberlin R. H. and Walker C. A. (1986) Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions. Antimicrob. Agents Chemother. 30, 409-413.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 409-413
    • Kimberlin, R.H.1    Walker, C.A.2
  • 27
    • 0028866917 scopus 로고
    • A mutant prion protein displays an aberrant membrane association when expressed in cultured cells
    • Lehmann S. and Harris D. A. (1995) A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J. Biol. Chem. 270, 24589-24597.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24589-24597
    • Lehmann, S.1    Harris, D.A.2
  • 28
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • Lehmann S. and Harris D. A. (1996) Mutant and infectious prion proteins display common biochemical properties in cultured cells. J. Biol. Chem. 271, 1633-1637.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1633-1637
    • Lehmann, S.1    Harris, D.A.2
  • 29
    • 0030799062 scopus 로고    scopus 로고
    • Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells
    • Lehmann S. and Harris D. A. (1997) Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272, 21479-21487.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21479-21487
    • Lehmann, S.1    Harris, D.A.2
  • 33
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P. C. and Harris D. A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 34
    • 0028069116 scopus 로고
    • Prions and related neurological diseases
    • Pocchiari M. (1994) Prions and related neurological diseases. Mol. Aspects Med. 15, 195-291.
    • (1994) Mol. Aspects Med. , vol.15 , pp. 195-291
    • Pocchiari, M.1
  • 36
    • 0028420936 scopus 로고
    • Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis
    • Priola S. A. and Caughey B. (1994) Inhibition of scrapie-associated PrP accumulation. Probing the role of glycosaminoglycans in amyloidogenesis. Mol. Neurobiol. 8, 113-120.
    • (1994) Mol. Neurobiol. , vol.8 , pp. 113-120
    • Priola, S.A.1    Caughey, B.2
  • 37
    • 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
  • 38
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner S. B., Groth D. F., Bolton D. C., Kent S. B., and Hood L. E. (1984) Purification and structural studies of a major scrapie prion protein. Cell 38, 127-134.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 41
    • 0031436335 scopus 로고    scopus 로고
    • The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells
    • Rieger R., Edenhofer F., Lasmezas C. I., and Weiss S. (1997) The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3, 1383-1388.
    • (1997) Nat. Med. , vol.3 , pp. 1383-1388
    • Rieger, R.1    Edenhofer, F.2    Lasmezas, C.I.3    Weiss, S.4
  • 42
    • 0029564913 scopus 로고
    • Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells
    • Shyng S. L., Lehmann S., Moulder K. L., and Harris D. A. (1995a) Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J. Biol. Chem. 270, 30221-30229.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30221-30229
    • Shyng, S.L.1    Lehmann, S.2    Moulder, K.L.3    Harris, D.A.4
  • 43
    • 0029054937 scopus 로고
    • The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits
    • Shyng S. L., Moulder K. L., Lesko A., and Harris D. A. (1995b) The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits. J. Biol. Chem. 270, 14793-14800.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14793-14800
    • Shyng, S.L.1    Moulder, K.L.2    Lesko, A.3    Harris, D.A.4
  • 44
    • 0025243737 scopus 로고
    • Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • Snow A. D., Wight T. N., Nochlin D., Koike Y., Kimata K., DeArmond S. J., and Prusiner S. B. (1990) Immunolocalization of heparan sulfate proteoglycans to the prion protein amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie. Lab. Invest. 63, 601-611.
    • (1990) Lab. Invest. , vol.63 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 47
    • 0028882424 scopus 로고
    • Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein
    • Telling G. C., Scott M., Mastriani J., Gabizon R., Torchia M., Cohen F. E., DeArmond S. J., and Prusiner S. B. (1995) Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79-90.
    • (1995) Cell , vol.83 , pp. 79-90
    • Telling, G.C.1    Scott, M.2    Mastriani, J.3    Gabizon, R.4    Torchia, M.5    Cohen, F.E.6    DeArmond, S.J.7    Prusiner, S.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.