Chemical and Biological Approaches Synergize to Ameliorate Protein-Folding Diseases

Cell

Volumn 134, Issue 5, 2008, Pages 769-781

  Mu, Ting Wei ^a   Ong, Derrick Sek Tong ^a   Wang, Ya Juan ^a   Balch, William E ^a   Yates III, John R ^a   Segatori, Laura ^a   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

HUMDISEASE; PROTEINS

Indexed keywords

2 ACETAMIDO 2 DEOXYNOJIRIMYCIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BETA N ACETYLHEXOSAMINIDASE; CELASTROL; CELL PROTEIN; CHAPERONE; GLUCOSYLCERAMIDASE; INDOMETACIN; LACTACYSTIN; MUTANT PROTEIN; PHARMACOLOGIC CHAPERONE; PROTEASOME INHIBITOR; PROTEOSTASIS REGULATOR; REGULATOR PROTEIN; SALICYLATE SODIUM; SALUBRINAL; TYROPEPTIN A; UNCLASSIFIED DRUG;

ARTICLE; CELL LEVEL; CONTROLLED STUDY; DRUG POTENTIATION; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; ENZYME ACTIVITY; GAUCHER DISEASE; HOMEOSTASIS; HUMAN; HUMAN CELL; LYSOSOME STORAGE DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN TRANSPORT; PROTEOSTASIS; SIGNAL TRANSDUCTION; TAY SACHS DISEASE;

EID: 50249175120     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.06.037     Document Type: Article

References (54)

1. Albanese V., Yam A.Y., Baughman J., Parnot C., and Frydman J. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124 (2006) 75-88
2. Awasthi N., and Wagner B.J. Upregulation of heat shock protein expression by proteasome inhibition: An antiapoptotic mechanism in the lens. Invest. Ophthalmol. Vis. Sci. 46 (2005) 2082-2091
3. Balch W.E., Morimoto R.I., Dillin A., and Kelly J.W. Adapting proteostasis for disease intervention. Science 319 (2008) 916-919
4. Beutler E. Lysosomal storage diseases: Natural history and ethical and economic aspects. Mol. Genet. Metab. 88 (2006) 208-215
5. Beutler E., Dale G.L., Guinto E., and Kuhl W. Enzyme replacement therapy in Gaucher's disease: Preliminary clinical trial of a new enzyme preparation. Proc. Natl. Acad. Sci. USA 74 (1977) 4620-4623
6. Beutler E., Gelbart T., and Scott C.R. Hematologically important mutations: Gaucher disease. Blood Cells Mol. Dis. 35 (2005) 355-364
7. Bouvier M. When an inhibitor promotes activity. Chem. Biol. 14 (2007) 241-242
8. Boyce M., Bryant K.F., Jousse C., Long K., Harding H.P., Scheuner D., Kaufman R.J., Ma D., Coen D.M., Ron D., et al. A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307 (2005) 935-939
9. Brady R.O. Enzyme replacement for lysosomal diseases. Annu. Rev. Med. 57 (2006) 283-296
10. Brodsky J.L. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation). Biochem. J. 404 (2007) 353-363
11. Brown C.R., Hong-Brown L.Q., and Welch W.J. Correcting temperature-sensitive protein folding defects. J. Clin. Invest. 99 (1997) 1432-1444
12. Bush K.T., Goldberg A.L., and Nigam S.K. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J. Biol. Chem. 272 (1997) 9086-9092
13. Chillaron J., and Haas I.G. Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol. Biol. Cell 11 (2000) 217-226
14. Cohen F.E., and Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature 426 (2003) 905-909
15. Conzelmann E., and Sandhoff K. Partial enzyme deficiencies: Residual activities and the development of neurological disorders. Dev. Neurosci. 6 (1984) 58-71
16. Deuerling E., and Bukau B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 261-277
17. Fan J.Q., Ishii S., Asano N., and Suzuki Y. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat. Med. 5 (1999) 112-115
18. Futerman A.H., and van Meer G. The cell biology of lysosomal storage disorders. Nat. Rev. Mol. Cell Biol. 5 (2004) 554-565
19. Horwich A.L., Fenton W.A., and Farr G.W. Chaperonins. In: Lennarz W., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry Volume 1 (2004), Elsevier, Oxford, UK 393-398
20. Imai J., Yashiroda H., Maruya M., Yahara I., and Tanaka K. Proteasomes and molecular chaperones. Cellular machinery responsible for folding and destruction of unfolded proteins. Cell Cycle 2 (2003) 585-589
21. Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., and Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83 (1995) 129-135
22. Jeyakumar M., Butters T.D., Dwek R.A., and Platt F.M. Glycosphingolipid lysosomal storage diseases: Therapy and pathogenesis. Neuropathol. Appl. Neurobiol. 28 (2002) 343-357
23. Kaufman R.J. Orchestrating the unfolded protein response in health and disease. J. Clin. Invest. 110 (2002) 1389-1398
24. Leclerc D., and Rozen R. Endoplasmic reticulum stress increases the expression of methylenetetrahydrofolate reductase through the IRE1 transducer. J. Biol. Chem. 283 (2008) 3151-3160
25. Liao W., Li X., Mancini M., and Chan L. Proteasome inhibition induces differential heat shock protein response but not unfolded protein response in HepG2 cells. J. Cell. Biochem. 99 (2006) 1085-1095
26. Liao L., Pilotte J., Xu T., Wong C.C.L., Edelman G.M., Vanderklish P., and Yates J.R. BDNF induces widespread changes in synaptic protein content and up-regulates components of the translation machinery: An analysis using high-throughput proteomics. J. Proteome Res. 6 (2007) 1059-1071
27. Lindquist S. The heat-shock response. Annu. Rev. Biochem. 55 (1986) 1151-1191
28. Liu Y., and Chang A. Heat shock response relieves ER stress. EMBO J. 27 (2008) 1049-1059
29. Liu H., Sadygov R.G., and Yates III J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76 (2004) 4193-4201
30. Maegawa G.H.B., Tropak M., Buttner J., Stockley T., Kok F., Clarke J.T.R., and Mahuran D.J. Pyrimethamine as a potential pharmacological chaperone for late-onset forms of GM2 gangliosidosis. J. Biol. Chem. 282 (2007) 9150-9161
31. Morimoto R.I. Regulation of the heat shock transcriptional response: Cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev. 12 (1998) 3788-3796
32. Moyer B.D., and Balch W.E. A new frontier in pharmacology: The endoplasmic reticulum as a regulated export pathway in health and disease. Expert Opin. Ther. Targets 5 (2001) 165-176
33. Mu T.W., Fowler D.M., and Kelly J.W. Partial restoration of mutant enzyme homeostasis in three distinct lysosomal storage disease cell lines by altering calcium homeostasis. PLoS. Biol. 6 (2008) e26
34. Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131 (2007) 1190-1203
35. Ron I., and Horowitz M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum. Mol. Genet. 14 (2005) 2387-2398
36. Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8 (2007) 519-529
37. Sawkar A.R., Cheng W.C., Beutler E., Wong C.H., Balch W.E., and Kelly J.W. Chemical chaperones increase the cellular activity of N370S beta-glucosidase: A therapeutic strategy for Gaucher disease. Proc. Natl. Acad. Sci. USA 99 (2002) 15428-15433
38. Sawkar A.R., Adamski-Werner S.L., Cheng W.C., Wong C.H., Beutler E., Zimmer K.P., and Kelly J.W. Gaucher disease-associated glucocerebrosidases show mutation-dependent chemical chaperoning profiles. Chem. Biol. 12 (2005) 1235-1244
39. Sawkar A.R., D'Haeze W., and Kelly J.W. Therapeutic strategies to ameliorate lysosomal storage disorders-A focus on Gaucher disease. Cell. Mol. Life Sci. 63 (2006) 1179-1192
40. Sawkar A.R., Schmitz M., Zimmer K.-P., Reczek D., Edmunds T., Balch W.E., and Kelly J.W. Chemical chaperones and permissive temperatures alter the cellular localization of Gaucher disease associated glucocerebrosidase variants. ACS Chem. Biol. 1 (2006) 235-251
41. Schmitz M., Alfalah M., Aerts J.M.F.G., Naim H.Y., and Zimmer K.-P. Impaired trafficking of mutants of lysosomal glucocerebrosidase in Gaucher's disease. Int. J. Biochem. Cell Biol. 37 (2005) 2310-2320
42. Schröder M., and Kaufman R.J. The mammalian unfolded protein response. Annu. Rev. Biochem. 74 (2005) 739-789
43. Schueler U.H., Kolter T., Kaneski C.R., Zirzow G.C., Sandhoff K., and Brady R.O. Correlation between enzyme activity and substrate storage in a cell culture model system for Gaucher disease. J. Inherit. Metab. Dis. 27 (2004) 649-658
44. Tropak M.B., Reid S.P., Guiral M., Withers S.G., and Mahuran D. Pharmacological enhancement of beta-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff patients. J. Biol. Chem. 279 (2004) 13478-13487
45. Ulloa-Aguirre A., Janovick J.A., Brothers S.P., and Conn P.M. Pharmacologic rescue of conformationally-defective proteins: Implications for the treatment of human disease. Traffic 5 (2004) 821-837
46. Wang X., Venable J., LaPointe P., Hutt D.M., Koulov A.V., Coppinger J., Gurkan C., Kellner W., Matteson J., Plutner H., et al. Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127 (2006) 803-815
47. Westerheide S.D., and Morimoto R.I. Heat shock response modulators as therapeutic tools for diseases of protein conformation. J. Biol. Chem. 280 (2005) 33097-33100
48. Westerheide S.D., Bosman J.D., Mbadugha B.N., Kawahara T.L., Matsumoto G., Kim S., Gu W., Devlin J.P., Silverman R.B., and Morimoto R.I. Celastrols as inducers of the heat shock response and cytoprotection. J. Biol. Chem. 279 (2004) 56053-56060
49. Wiseman R.L., Powers E.T., Buxbaum J.N., Kelly J.W., and Balch W.E. An adaptable standard for protein export from the endoplasmic reticulum. Cell 131 (2007) 809-821
50. Yam G.H.F., Bosshard N., Zuber C., Steinmann B., and Roth J. Pharmacological chaperone corrects lysosomal storage in Fabry disease caused by trafficking-incompetent variants. Am. J. Physiol. Cell Physiol. 290 (2006) C1076-C1082
51. Yan F.F., Lin C.W., Cartier E.A., and Shyng S.L. Role of ubiquitin-proteasome degradation pathway in biogenesis efficiency of β-cell ATP-sensitive potassium channels. Am. J. Physiol. Cell Physiol. 289 (2005) C1351-C1359
52. Yang H., Chen D., Cui Q.C., Yuan X., and Dou Q.P. Celastrol, a triterpene extracted from the Chinese "Thunder of God Vine," is a potent proteasome inhibitor and suppresses human prostate cancer growth in nude mice. Cancer Res. 66 (2006) 4758-4765
53. Young J.C., Agashe V.R., Siegers K., and Hartl F.U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol. 5 (2004) 781-791
54. Yu Z., Sawkar A.R., Whalen L.J., Wong C.-H., and Kelly J.W. Isofagomine- and 2,5-anhydro-2,5-imino-D-glucitol-based glucocerebrosidase pharmacological chaperones for Gaucher disease intervention. J. Med. Chem. 50 (2007) 94-100