Pharmacological chaperones: Potential treatment for conformational diseases

Trends in Endocrinology and Metabolism

Volumn 15, Issue 5, 2004, Pages 222-228

  Bernier, Virginie ^a   Lagacé, Monique ^a   Bichet, Daniel G ^a   Bouvier, Michel ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

1 [2 (6 METHYL 2 PYRIDYL)ETHYL] 4 (4 METHYLSULFONYLAMINOBENZOYL)PIPERIDINE; ASTEMIZOLE; CAPSAICIN; CHAPERONE; CHLORPROMAZINE; CISAPRIDE; CYCLOPAMINE; CYCLOSPORIN; DIAZOXIDE; GONADORELIN ANTAGONIST; LIXIVAPTAN; MEPACRINE; N (NONYL)DEOXYNOJIRIMYCIN; N TERT BUTYL 4 [5' ETHOXY 4 (2 MORPHOLINOETHOXY) 2' OXOSPIRO[CYCLOHEXANE 1,3' INDOLE] 1' SULFONYL] 3 METHOXYBENZAMIDE; NALTREXONE; NOJIRIMYCIN; UNCLASSIFIED DRUG; VERAPAMIL; VINBLASTINE;

CONFORMATION; GENE MUTATION; HUMAN; HYPERINSULINEMIA; HYPOGLYCEMIA; HYPOGONADOTROPIC HYPOGONADISM; METABOLIC DISORDER; MOLECULAR RECOGNITION; NEPHROGENIC DIABETES INSIPIDUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; QUALITY CONTROL; REVIEW;

ENDOCRINE SYSTEM DISEASES; HUMANS; METABOLIC DISEASES; MOLECULAR CHAPERONES; PROTEIN FOLDING;

EID: 3042540232     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tem.2004.05.003     Document Type: Review

References (57)

1. Carrell R.W., Lomas D.A. Conformational disease. Lancet. 350:1997;134-138
2. Kopito R.R., Ron D. Conformational disease. Nat. Cell Biol. 2:2000;E207-E209
3. Selkoe D.J. Folding proteins in fatal ways. Nature. 426:2003;900-904
4. Sitia R., Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature. 426:2003;891-894
5. Welch W.J., Brown C.R. Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperones. 1:1996;109-115
6. Morello J.P., et al. Pharmacological chaperones: a new twist on receptor folding. Trends Pharmacol. Sci. 21:2000;466-469
7. Cohen F.E., Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature. 426:2003;905-909
8. Conn P.M., et al. Protein origami: therapeutic rescue of misfolded gene products. Mol. Intervent. 2:2002;308-316
9. Smith D.F., et al. Molecular chaperones: biology and prospects for pharmacological intervention. Pharmacol. Rev. 50:1998;493-514
10. Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4:2003;49-60
11. Kopito R.R. Biosynthesis and degradation of CFTR. Physiol. Rev. 79:1999;S167-S173
12. Denning G.M., et al. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature. 358:1992;761-764
13. Sato S., et al. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271:1996;635-638
14. Brown C.R., et al. Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones. 1:1996;117-125
15. Loo T.W., Clarke D.M. Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J. Biol. Chem. 269:1994;28683-28689
16. Loo T.W., Clarke D.M. P-glycoprotein. Associations between domains and between domains and molecular chaperones. J. Biol. Chem. 270:1995;21839-21844
17. Loo T.W., Clarke D.M. Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol- modification techniques. Biochim. Biophys. Acta. 1461:1999;315-325
18. Morello J.P., et al. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J. Clin. Invest. 105:2000;887-895
19. Kaler S.G. Diagnosis and therapy of Menkes syndrome, a genetic form of copper deficiency. Am. J. Clin. Nutr. 67:1998;1029S-1034S
20. Kim B.E., et al. A conditional mutation affecting localization of the Menkes disease copper ATPase. Suppression by copper supplementation. J. Biol. Chem. 277:2002;44079-44084
21. Thomas P.M., et al. Mutations in the sulfonylurea receptor gene in familial persistent hyperinsulinemic hypoglycemia of infancy. Science. 268:1995;426-429
22. Partridge C.J., et al. Identification and pharmacological correction of a membrane trafficking defect associated with a mutation in the sulfonylurea receptor causing familial hyperinsulinism. J. Biol. Chem. 276:2001;35947-35952
23. Huopio H., et al. K(ATP) channels and insulin secretion disorders. Am. J. Physiol. Endocrinol. Metab. 283:2002;E207-E216
24. Morello J.P., Bichet D.G. Nephrogenic diabetes insipidus. Annu. Rev. Physiol. 63:2001;607-630
25. Ulloa-Aguirre A., et al. Misrouted cell surface receptors as a novel disease aetiology and potential therapeutic target: the case of hypogonadotropic hypogonadism due to gonadotropin-releasing hormone resistance. Expert Opin. Ther. Targets. 7:2003;175-185
26. Janovick J.A., et al. Rescue of hypogonadotropic hypogonadism-causing and manufactured GnRH receptor mutants by a specific protein-folding template: misrouted proteins as a novel disease etiology and therapeutic target. J. Clin. Endocrinol. Metab. 87:2002;3255-3262
27. Desnick, R.J., et al. (2001) α-Galactosidase A deficiency: Fabry disease. In The Metabolic and Molecular Bases of Inherited Disease (Seriver, C.R. et al., eds), pp. 9733-3774, McGraw-Hill.
28. Ishii S., et al. Aggregation of the inactive form of human α-galactosidase in the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 220:1996;812-815
29. Fan J.Q., et al. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat. Med. 5:1999;112-115
30. Frustaci A., et al. Improvement in cardiac function in the cardiac variant of Fabry's disease with galactose-infusion therapy. N. Engl. J. Med. 345:2001;25-32
31. Suzuki Y., et al. β-Galactosidase deficiency (β-galactosidosis) : GM1-gangliosidosis and Morquio B disease. Scriver C.R.,, et al. The Metabolic and Molecular Bases of Inherited Disease. 2001;3775-3809 McGraw-Hill
32. Tominaga L., et al. Galactonojirimycin derivatives restore mutant human β-galactosidase activities expressed in fibroblasts from enzyme-deficient knockout mouse. Brain Dev. 23:2001;284-287
33. Matsuda J., et al. Chemical chaperone therapy for brain pathology in G(M1)-gangliosidosis. Proc. Natl. Acad. Sci. U. S. A. 100:2003;15912-15917
34. de Fost M., et al. Gaucher disease: from fundamental research to effective therapeutic interventions. Neth. J. Med. 61:2003;3-8
35. Sawkar A.R., et al. Chemical chaperones increase the cellular activity of N370S β-glucosidase: a therapeutic strategy for Gaucher disease. Proc. Natl. Acad. Sci. U. S. A. 99:2002;15428-15433
36. Dormer R.L., et al. Correction of delF508-CFTR activity with benzo(c)quinolizinium compounds through facilitation of its processing in cystic fibrosis airway cells. J. Cell Sci. 114:2001;4073-4081
37. Galietta L.J., et al. Novel CFTR chloride channel activators identified by screening of combinatorial libraries based on flavone and benzoquinolizinium lead compounds. J. Biol. Chem. 276:2001;19723-19728
38. Neufeld E.B., et al. The ABCA1 transporter modulates late endocytic trafficking: insights from the correction of the genetic defect in Tangier disease. J Biol. Chem. 279:2004;15571-15578
39. Brosius U., Gartner J. Cellular and molecular aspects of Zellweger syndrome and other peroxisome biogenesis disorders. Cell. Mol. Life Sci. 59:2002;1058-1069
40. Myerowitz R. Tay-Sachs disease-causing mutations and neutral polymorphisms in the Hex A gene. Hum. Mutat. 9:1997;195-208
41. Shaukat S., et al. Syndromic and non-syndromic deafness, molecular aspects of Pendred syndrome and its reported mutations. J. Ayub Med. Coll. Abbottabad. 15:2003;59-64
42. Speiser P.W., White P.C. Congenital adrenal hyperplasia. N. Engl. J. Med. 349:2003;776-788
43. Baskakov I.V., et al. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. J. Biol. Chem. 274:1999;10693-10696
44. Burrows J.A., et al. Chemical chaperones mediate increased secretion of mutant α1-antitrypsin (α1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency. Proc. Natl. Acad. Sci. U. S. A. 97:2000;1796-1801
45. Yoshida H., et al. 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
46. Song J.L., Chuang D.T. Natural osmolyte trimethylamine N-oxide corrects assembly defects of mutant branched-chain α-ketoacid decarboxylase in maple syrup urine disease. J. Biol. Chem. 276:2001;40241-40246
47. Tamarappoo B.K., et al. Misfolding of mutant aquaporin-2 water channels in nephrogenic diabetes insipidus. J. Biol. Chem. 274:1999;34825-34831
48. Tan C.M., et al. Appropriate polarization following pharmacological rescue of v2 vasopressin receptors encoded by X-linked nephrogenic diabetes insipidus alleles involves a conformation of the receptor that also attains mature glycosylation. J. Biol. Chem. 278:2003;35678-35686
49. Curran M.E., et al. A molecular basis for cardiac arrhythmia: HERG mutations cause long QT syndrome. Cell. 80:1995;795-803
50. Soto C., et al. Reversion of prion protein conformational changes by synthetic β-sheet breaker peptides. Lancet. 355:2000;192-197
51. Korth C., et al. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9836-9841
52. Ryou C., et al. Differential inhibition of prion propagation by enantiomers of quinacrine. Lab. Invest. 83:2003;837-843
53. Noorwez S.M., et al. Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J. Biol. Chem. 278:2003;14442-14450
54. Hammarstrom P., et al. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science. 299:2003;713-716
55. Chen J.K., et al. Inhibition of Hedgehog signaling by direct binding of cyclopamine to smoothened. Genes Dev. 16:2002;2743-2748
56. Wiens G.D., et al. Recovering antibody secretion using a hapten ligand as a chemical chaperone. J. Biol. Chem. 276:2001;40933-40939
57. Petaja-Repo U.E., et al. Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation. EMBO J. 21:2002;1628-1637