Doxycycline and protein folding agents rescue the abnormal phenotype of familial CJD H187R in a cell model

Molecular Brain Research

Volumn 123, Issue 1-2, 2004, Pages 37-44

  Gu, Yaping ^a   Singh, Neena ^a  

^a CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

Chemical chaperones; CJD; Degenerative disease: other; Disorders of the Nervous system; Doxycycline; Familial prion disorders; GFP; Normal cellular prion protein; Prion protein; Protein folding; Protein transport; PrP187R; PrPC

Indexed keywords

DIMETHYL SULFOXIDE; DOXYCYCLINE; GLYCEROL; GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; PRION PROTEIN;

ARTICLE; CONTROLLED STUDY; CREUTZFELDT JAKOB DISEASE; FAMILIAL DISEASE; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; INHIBITION KINETICS; LOW TEMPERATURE; PHENOTYPE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING;

CELL LINE, TUMOR; CREUTZFELDT-JAKOB SYNDROME; DIMETHYL SULFOXIDE; DOSE-RESPONSE RELATIONSHIP, DRUG; DOXYCYCLINE; GLYCEROL; HUMANS; LYSOSOMES; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; MUTATION; PHENOTYPE; PRIONS; PROTEIN FOLDING; TEMPERATURE;

STAPHYLOCOCCUS PHAGE 187;

EID: 1642409785     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbrainres.2004.01.006     Document Type: Article

References (31)

1. Brown P. Drug therapy in human and experimental transmissible spongiform encephalopathy. Neurology. 58:2002;1720-1725.
2. Brown C.R., Hong-Brown L.Q., Biwersi J., Verkman A.S., Welch W.J. Chemical Chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones. 1996;117-125.
3. Butefisch C.M., Gambetti P., Cervenakova L., Park K.Y., Hallett M., Goldfarb L.G. Inherited prion encephalopathy associated with the novel PRNP H187R mutation: a clinical study. Neurology. 55:2000;517-522.
4. Capellari S., Parchi P., Russo C.M., Sanford J., Sy M.-S., Gambetti P., Petersen R.B. Effect of the E200 K Mutation on Prion Protein Metabolism: Comparative Study of a Cell Model and Human Brain. Am. J. Pathol. 157:2002;613-622.
5. Caughey B., Raymond G.J., Ernst D., Race R.E. 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. 65:1991;6597-6603.
6. Chen S.G., Teplow D.B., Parchi P., Teller J.K., Gambetti P., Autilio-Gambetti L. Truncated forms of the human prion protein in normal brain and in prion diseases. J. Biol. Chem. 270:1995;19173-19180.
7. Daude N., Lehmann S., Harris D.A. Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272:1997;11604-11612.
8. Denning G.M., Anderson M.P., Amara J.F., Marshall J., Smith A.E., Welsh M.J. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature (Lond.). 358:1992;761-764.
9. Doh-Ura K., Iwaki T., Caughey B. Lysosomotropic agents and cysteine Protease inhibitors inhibit scrapie-associated prion protein accumulation. J. Virol. 74:2000;4894-4897.
10. Ellgaard L., Molinari M., Helenius A. Setting the standards: quality control in the secretory pathway. Science. 286:1999;1882-1888.
11. Forloni G., Lussich S., Awan T., Colombo L., Angeretti N., Girola L., Bertani L., Poli G., Caramelli M., Bruzzone M.G., Farina L., Limido L., Rossi G., Giaccone G., Ironside J.W., Bugiani O., Salmona M., Tagliavini F. Tetracyclines affect prion infectivity. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10849-10854.
12. Gu Y., Jing Y., Kumar A., Sharma Y., Fujioka H., Singh N. Isolation of human neuronal cells resistant to toxicity by the prion protein peptide 106-126. J. Alzheimer's Dis. 3:2001;169-180.
13. Gu Y., Fujioka H., Mishra R.S., Li R., Singh N. Prion peptide 106-126 modulates the aggregation of cellular prion protein and induces the synthesis of potentially neurotoxic transmembrane PrP. J. Biol. Chem. 277:2002;2275-2286.
14. Gu Y., Verghese S., Mishra R.S., Xu X., Shi Y., Singh N. Intracellular aggregates of mutant prion protein upregulate the synthesis of potentially neurotoxic transmembrane PrP. J. Neurochem. 84:2003;10-22.
15. Hegde R.S., Mastrianni J.A., Scott M.R., DeFea K.A., Tremblay P., Torchia M., DeArmond S.J., Prusiner S.B., Lingappa V.R. A transmembrane form of the prion protein in neurodegenerative disease. Science. 279:1998;827-834.
16. Hegde R.S., Tremblay P., Groth D., DeArmond S.J., Prusiner S.B., Lingappa V.R. Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature. 402:1999;822-826.
17. Ivanova L., Barmada S., Kummer T., Harris D.A. Mutant prion proteins are partially retained in the endoplasmic reticulum. J. Biol. Chem. 276:2001;42409-42421.
18. Jin T., Gu Y., Zanusso G., Sy M.-S., Kumar A., Cohen M., Gambetti P., Singh N. The chaperone protein BiP binds to a mutant prion protein and mediates its degradation by the proteasome. J. Biol. Chem. 275:2000;38699-38704.
19. Kapusnik-Uner J.E., Sande M.A., Chambers F. ANTIMICROBIAL AGENTS Tetracyclines, Chloramphenicol, Erythromycin, and Miscellaneous Antibacterial Agents. Harman J.G., Limbird L.E., Molinof P.B., Ruddon R.W. The pharmacological Basis of Therapeutics. 9th ed. 1996;1123-1130 McGraw-Hill, New York.
20. Korth C., May B.C., Cohen F.E., Prusiner S.B. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci., U. S. A. 98:2001;9836-9841.
21. Lorenz H., Windl O., Kretzschmar H.A. Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases. J. Biol. Chem. 277:2002;8508-8516.
22. Love R. Old drugs to treat new variant Creutzfeldt-Jakob disease. Lancet. 358:2001;563.
23. Sc-like conformation in living cells. Nat. Cell Biol. 1:1999;358-361.
24. Ma J., Lindquist S. Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation. Proc. Natl. Acad. Sci. U. S. A. 98:2001;14955-14960.
25. Mishra R.S., Gu Y., Bose S., Verghese S., Kalepu S., Singh N. Cell surface accumulation of a truncated transmembrane prion protein in GSS P102L. J. Biol. Chem. 277:2002;24554-24561.
26. Singh N., Zanusso G., Chen S.G., Fujioka H., Richardson S., Gambetti P., Petersen R.B. Prion protein aggregation reverted by low temperature in transfected cells carrying a prion protein gene mutation. J. Biol. Chem. 272:1997;28461-28470.
27. Sc in vitro (2000).
28. Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S.B. Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform. J. Cell Biol. 129:1995;121-132.
29. Tatzelt J., Prusiner S.B., Welch W.J. Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15:1996;6363-6373.
30. Yoshida H., Yoshizawa T., Shibasaki F., Shoji S., Kanazawa I. Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Neurobiol. dis. 10:2002;88-99.
31. Zanusso G., Petersen R.B., Jin T., Jing Y., Kanoush R., Ferrari S., Gambetti P., Singh N. Proteasomal degradation and N-terminal protease resistance of the codon 145 mutant prion protein. J. Biol. Chem. 274:1999;23396-23404.