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Volumn 74, Issue 2, 2000, Pages 754-762

Effect of amphotericin B on wild-type and mutated prion proteins in cultured cells: Putative mechanism of action in transmissible spongiform encephalopathies

Author keywords

Amphotericin B; Prion protein; Transmissible spongiform encephalopathies

Indexed keywords

AMPHOTERICIN B; GLYCOSYLPHOSPHATIDYLINOSITOL; MUTANT PROTEIN; PRION PROTEIN;

EID: 0033964470     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.740754.x     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0032934347 scopus 로고    scopus 로고
    • MS-8209, a water-soluble amphotericin B derivative, affects both scrapie agent replication and PrPres accumulation in Syrian ham-ster scrapie
    • Adjou K. T., Demaimay R., Deslys J. P., Lasmezas C. I., Beringue V., Demart S., Lamimry F., Seman M., and Dormont D. (1999) MS-8209, a water-soluble amphotericin B derivative, affects both scrapie agent replication and PrPres accumulation in Syrian ham-ster scrapie. J. Gen. Virol. 80, 1079-1085.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1079-1085
    • Adjou, K.T.1    Demaimay, R.2    Deslys, J.P.3    Lasmezas, C.I.4    Beringue, V.5    Demart, S.6    Lamimry, F.7    Seman, M.8    Dormont, D.9
  • 2
    • 0031472117 scopus 로고    scopus 로고
    • Cell membrane lipid composition and distribution: Implications for cell function and lessons learned from photoreceptors and platelets
    • Boesze-Battaglia K. and Schimmel R. (1997) Cell membrane lipid composition and distribution: implications for cell function and lessons learned from photoreceptors and platelets. J. Exp. Biol. 200, 2927-2936.
    • (1997) J. Exp. Biol. , vol.200 , pp. 2927-2936
    • Boesze-Battaglia, K.1    Schimmel, R.2
  • 3
    • 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
  • 4
    • 0027291065 scopus 로고
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor
    • Borchelt D. R., Rogers M., Stahl N., Telling G., and Prusiner S. B. (1993) Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Glycobilogy 3, 319-329.
    • (1993) Glycobilogy , vol.3 , pp. 319-329
    • Borchelt, D.R.1    Rogers, M.2    Stahl, N.3    Telling, G.4    Prusiner, S.B.5
  • 5
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D. A. and Rose J. K. (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.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
    • 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
  • 11
    • 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
  • 12
    • 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
  • 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
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson T. and Kurzchalia T. V. (1998) Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394, 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 18
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergenl-resistant complexes without caveolin
    • Gorodinsky A. and Harris D. A. (1995) Glycolipid-anchored proteins in neuroblastoma cells form detergenl-resistant complexes without caveolin. J. Cell Biol. 129, 619-627.
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 19
    • 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
    • 0030449320 scopus 로고    scopus 로고
    • Amphotericin B: New life for an old drug
    • Hartsel S. and Bolard J. (1996) Amphotericin B: new life for an old drug. Trends Pharmacol. Sci. 17, 445-449.
    • (1996) Trends Pharmacol. Sci. , vol.17 , pp. 445-449
    • Hartsel, S.1    Bolard, J.2
  • 22
    • 0030964917 scopus 로고    scopus 로고
    • COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform
    • Kaneko K., Vey M., Scott M., Pilkuhn S., Cohen F. E., and Prusiner S. B. (1997) COOH-terminal sequence of the cellular prion protein directs subcellular trafficking and controls conversion into the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 2333-2338.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2333-2338
    • Kaneko, K.1    Vey, M.2    Scott, M.3    Pilkuhn, S.4    Cohen, F.E.5    Prusiner, S.B.6
  • 23
    • 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
  • 24
    • 0030050733 scopus 로고    scopus 로고
    • Mutant and infectious prion proteins display common biochemical properties in cultured cells
    • Lehmann S. and Harris D. A. (1996a) 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
  • 25
    • 0030006902 scopus 로고    scopus 로고
    • Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform
    • Lehmann S. and Harris D. A. (1996A) Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl. Acad. Sci. USA 93, 5610-5614.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5610-5614
    • Lehmann, S.1    Harris, D.A.2
  • 26
    • 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
  • 28
    • 0033961817 scopus 로고    scopus 로고
    • Effect of Congo red on wild-type and mutated prion proteins in cultured cells
    • Milhavet O., Mangé A., Casanova D., and Lehmann S. (2000) Effect of Congo red on wild-type and mutated prion proteins in cultured cells. J. Neurochem. 74, 222-230.
    • (2000) J. Neurochem. , vol.74 , pp. 222-230
    • Milhavet, O.1    Mangé, A.2    Casanova, D.3    Lehmann, S.4
  • 29
    • 0033529289 scopus 로고    scopus 로고
    • Prion proteins carrying pathogenic mutations are resistant to phospholipase cleavage of their glyco-lipid anchors
    • Narwa R. and Harris D. A. (1999) Prion proteins carrying pathogenic mutations are resistant to phospholipase cleavage of their glyco-lipid anchors. Biochemistry 38, 8770-8777.
    • (1999) Biochemistry , vol.38 , pp. 8770-8777
    • Narwa, R.1    Harris, D.A.2
  • 30
    • 0030894380 scopus 로고    scopus 로고
    • Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform
    • Naslavsky N., Stein R., Yanai A., Friedlander G., and Taraboulos A. (1997) Characterization of detergent-insoluble complexes containing the cellular prion protein and its scrapie isoform. J. Biol. Chem. 272, 6324-6331.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6324-6331
    • Naslavsky, N.1    Stein, R.2    Yanai, A.3    Friedlander, G.4    Taraboulos, A.5
  • 33
    • 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
  • 34
    • 0023243085 scopus 로고
    • Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters
    • Pocchiari M., Schmittinger S.. and Masullo C. (1987) Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters. J. Gen. Virol. 68, 219-223.
    • (1987) J. Gen. Virol. , vol.68 , pp. 219-223
    • Pocchiari, M.1    Schmittinger, S.2    Masullo, C.3
  • 36
    • 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
  • 37
    • 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. (19956) 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
  • 38
    • 0032476714 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids inhibit T cell signal transduction by modification of detergent-insoluble membrane domains
    • Stulnig T. M., Berger M., Sigmund T., Raederstorff D., Stockinger H., nd Waldhausl W. (1998) Polyunsaturated fatty acids inhibit T cell signal transduction by modification of detergent-insoluble membrane domains. J. Cell Biol. 143, 637-644.
    • (1998) J. Cell Biol. , vol.143 , pp. 637-644
    • Stulnig, T.M.1    Berger, M.2    Sigmund, T.3    Raederstorff, D.4    Stockinger, H.5    Waldhausl, W.6
  • 41
    • 0028966735 scopus 로고
    • Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform
    • Published erratum appears in J. Cell Biol. (1995) 130, 501
    • Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S. B., and Avraham D. (1995) Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell Biol. 129, 121-132. [Published erratum appears in J. Cell Biol. (1995) 130, 501.
    • (1995) J. Cell Biol. , vol.129 , pp. 121-132
    • Taraboulos, A.1    Scott, M.2    Semenov, A.3    Avrahami, D.4    Laszlo, L.5    Prusiner, S.B.6    Avraham, D.7
  • 42
    • 0028133261 scopus 로고
    • The endocytic process in CHO cells, a toxic pathway of the polyene antibiotic amphotericin B
    • Vertut-Doi A., Ohnishi S. I., and Bolard J. (1994) The endocytic process in CHO cells, a toxic pathway of the polyene antibiotic amphotericin B. Antimicrob. Agents Chemother. 38, 2373-2379.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2373-2379
    • Vertut-Doi, A.1    Ohnishi, S.I.2    Bolard, J.3
  • 44
    • 0026600866 scopus 로고
    • Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation
    • Xi Y. G., Ingrosso L., Ladogana A., Masullo C., and Pocchiari M. (1992) Amphotericin B treatment dissociates in vivo replication of the scrapie agent from PrP accumulation. Nature 356, 598-601.
    • (1992) Nature , vol.356 , pp. 598-601
    • Xi, Y.G.1    Ingrosso, L.2    Ladogana, A.3    Masullo, C.4    Pocchiari, M.5


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