A cure for traffic jams: Small molecule chaperones in the endoplasmic reticulum

Traffic

Volumn 5, Issue 11, 2004, Pages 815-820

  Römisch, Karin ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Chemical chaperones; Conformational diseases; Endoplasmic reticulum; Pharmaceutical chaperones; Protein degradation; Protein folding; Protein quality control; Protein secretion

Indexed keywords

1 DEOXYGALACTONOJIRIMYCIN; 4 PHENYLBUTYRIC ACID; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE INHIBITOR; ALPHA 1 ANTITRYPSIN; ALPHA GALACTOSIDASE; ANTINEOPLASTIC AGENT; BLOOD CLOTTING FACTOR; CARRIER PROTEIN; CHAPERONE; CURCUMIN; ENZYME INHIBITOR; GALACTOSE; GLYCEROL; HEAT SHOCK COGNATE PROTEIN 70; PROTEASOME INHIBITOR; SECRETORY PROTEIN; THAPSIGARGIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; TREHALOSE; UNCLASSIFIED DRUG;

BINDING AFFINITY; CARBOHYDRATE SYNTHESIS; CELL COMMUNICATION; CYSTIC FIBROSIS; DRUG PROTEIN BINDING; EMPHYSEMA; ENDOPLASMIC RETICULUM; ENZYME INHIBITION; FABRY DISEASE; GENE MUTATION; HEMOPHILIA; HUMAN; LIVER CIRRHOSIS; NONHUMAN; PATHOGENESIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN QUALITY; PROTEIN STABILITY; PROTEIN TRANSPORT; REVIEW; TRANS GOLGI NETWORK;

ANIMALS; ENDOPLASMIC RETICULUM; HUMANS; IONS; LIGANDS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; MUTATION; PEPTIDES; PHENOTYPE; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 7244245559     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2004.00231.x     Document Type: Review

References (57)

1. Sitia R, Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 2003;426:891-894.
2. Jarosch E, Geiss-Friedlander R, Meusser B, Walter J, Sommer T. Protein dislocation from the endoplasmic reticulum - pulling out the suspect. Traffic 2002;3:530-536.
3. Schubert U, Anton LC, Gibbs J, Norbury CC, Yewdell JW, Bennink JR. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000;404:770-774.
4. Bukau B, Deuerling E, Pfund C, Craig EA. Getting newly synthesized proteins into shape. Cell 2000;101:119-122.
5. Li Y, Moir RD, Sethy-Corachi IK, Warner JR, Willis IA. Repression of ribosome and tRNA synthesis in secretion-defective cells is signaled by a novel branch of the cell integrity pathway. Mol Cell Biol 2000;20:3843-3851.
6. van den Berg B, Ellis RJ, Dobson CM. Effects of macromolecular crowding on protein folding and aggregation. EMBO J 1999;18:6927-6933.
7. Lomas DA, Parfrey H. α1-Antitrypsin deficiency: molecular pathophysiology. Thorax 2004;59:529-535.
8. Oyadomari S, Mori M. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ 2004; 11:381-389.
9. Aridor M, Hannan L. Traffic jam: a compendium of human diseases that affect introcellular transport processes. Traffic 2000;1:836-851.
10. Aridor M, Hannan LA. Traffic jams, II: an update of diseases of intracellular transport. Traffic 2002;3:781-790.
11. Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE, Welsh MJ. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 1992;358:761-764.
12. Wang T, Waters CT, Rothman AMK, Jakins TJ, Römisch K, Trump D. Intracellular retention of mutant retinoschisin is the pathological mechanism underlying X-linked retinoschisis. Hum Mol Genet 2002;11:3097-3105.
13. Loo TW, Clarke DM. Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators. J Biol Chem 1997;272:709-712.
14. Morello J-P, Salahpour A, Laperriere A, Bernier V, Arthus M-F, Lonergan M, Pataja-Repo U, Angers S, Morin D, Bichet DG, Bouvier M. Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J Clin Invest 2000;105:887-895.
15. Powell K, Zeitlin PL. Therapeutic approaches to repair defects in ΔF508 CFTR folding and cellular targeting. Adv Drug Del Rev 2002;54:1395-1408.
16. Fan J-Q. A contradictory treatment for lysosomal storage disorders: inhibitors enhance mutant enzyme activity. Trends Pharmacol Sci 2003;24:355-360.
17. Halaban R, Chang E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert DN. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci U S A 1997;94:6210-6215.
18. Egan ME, Glockner-Pagel J, Ambrose C, Cahill PA, Pappoe L, Balamuth N, Cho E, Canny S, Wagner CA, Geibel J, Caplan MJ. Calcium-pump inhibitors induce functional surface expression of delta F508-CFTR protein in cystic fibrosis epithelial cells. Nat Mad 2002;8:485-492.
19. Egan ME, Pearson M, Weiner SA, Rajendran V, Rubin D, Glockner-Pagel J, Du Canny SK, Lukacs GL, Caplan MJ. Curcumin, a major constituent of turmeric, corrects cystic fibrosis defects. Science 2004;304:600-602.
20. Zeitlin PL, Diener-West M, Rubenstein RC, Boyle MP, Lee CK, Brass-Ernst L. Evidence of CFTR in cystic fibrosis after systemic administration of 4-phenylbutyrate. Mol Ther 2002;6:119-126.
21. Chang AL, Hsu CH, Lin JK, Hsu MM, Ho YF, Shen TS, Ko JY, Lin JT, Lin BR, Ming-Shiang WYuHS, Jee SH, Chen GS, Chen TM, Chen CA, et al. Phase I clinical trial of curcumin, a chemopreventive reagent, in patients with high-risk or pre-malignant lesions. Anticancer Res 2001;21:2895-2900.
22. Song Y, Sonawane ND, Salinas D, Quian L, Pedemonte N, Galietta LJ, Verkman AS. Evidence against rescue of defective Δ F508-CFTR cellular processing by curcumin in cell culture and mouse models. J Biol Chem 2004: e-pub ahead of print.
23. Almond JB, Cohen GM. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002;16:433-443.
24. Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003;426:895-899.
25. Selkoe D. Folding proteins in fatal ways. Nature 2003;426:900-904.
26. + gene is a target of the signaling pathway involving Wis1 MAP-kinase kinase in fission yeast. FEBS Lett 1995; 376:199-201.
27. Wang A, Bolen DW. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 1997;36:9101-9108.
28. Kandror O, Bretschneider N, Kreydin E, Cavalieri D, Goldberg AL. Yeast adapt to near-freezing temperatures by STRE/Msn2,4-dependent induction of trehalose synthesis and certain molecular chaperones. Mol Cell 2004;13:771-781.
29. Gekko K, Timasheff SN. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 1981;20:4667-4676.
30. Zou O, Bennion BJ, Daggett V, Murphy KP. The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea. J Am Chem Soc 2002;124:1192-1202.
31. Sampedro JG, Uribe S. Trehalose-enzyme interactions result in structure stabilization and activity inhibition. Mol Cell Biochem 2004;256:319-327.
32. Shimizu S. Estimation of excess solvation numbers of water and cosolvents from preferential interaction and volume tric experiments. J Chem Phys 2004;120:4989-4990.
33. Phadtare S. Recent developments in bacterial cold-shock response. Curr Issues Mol Biol 2004;6:125-136.
34. Dignam JD. Preparation of extracts from higher eukaryotes. Methods Enzymol 1990;182:194-203.
35. Hjelmeland LM. Solubilization of native membrane proteins. Methods Enzymol 1990;182:252-264.
36. Shearer AG, Hampton RY. Structural control of endoplasmic reticulum-associated degradation: effect of chemical chaperones on 3-hydroxy-3-methylglutaryl-CoA reductase. J Biol Chem 2004;279:188-196.
37. Tamarappoo BK, Verkman AS. Defective aquaporin-2 trafficking in nephrogenic diabetes insipidus and correction by chemical chaperones. J Clin Invest 1998;101:2257-2267.
38. Burrows JAJ, Willis LK, Perlmutter DH. Chemical chaperones mediate increased secretion of mutant α1-antitrypsin Z. A potential pharmacological strategy for prevention of liver injury and emphysema in α1-AT deficiency. Proc Natl Acad Sci U S A 2000;97:1796-1801.
39. Morello J-P, Petaja-Repo U, Bichet DG, Bouvier M. Pharmacological chaperones: a new twist on receptor folding. Trends Pharmacol Sci 2000;21:466-469.
40. Bernier V, Lagace M, Bichet DG, Bouvier M. Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocrin Metab 2004;15:222-228.
41. Farmery MR, Bulleid NJ. Major histocompatibility class I folding, assembly, and degradation: a paradigm for two-stage quality control in the endoplasmic reticulum. Frog Nucleid Acid Res Mol Biol 2001;67:235-268.
42. Fisher EA, Ginsberg HN. Complexity in the secretory pathway the assembly and secretion of apolipoprotein B-containing lipoproteins. J Biol Chem 2002;277:17377-17380.
43. Fan JQ, Ishii S, Asano N, Suzuki Y. Accelerated transport and maturation of lysosomal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat Med 1999;5:112-115.
44. Frustaci A, Chimenti C, Ricci R, Natale L, Russo MA, Pieroni M, Eng CM, Desnick RJ. Improvement in cardiac function in the cardiac variant of Fabry's disease with galactose-infusion therapy. N Engl J Med 2001;345:25-32.
45. Dormer RL, Derand R, McNeilly CM, Mettey Y, Bulteau-Pignoux L, Metaye T, Vierfond JM, Gray MA, Calietta LJ, Morris MR, Pereira MM, Doull IJ, Becq F, McPherson MA. Correction of the delF508-CFTR activity with benzo(c)quinolizinium compounds though facilitation of its processing in cystic fibrosis airway cells. J Cell Sci 2001;114:4073-4081.
46. Spear E, Ng DTW. The unfolded protein response: no longer just a special teams player. Traffic 2001;2:515-523.
47. Zhang K, Kaufman RJ. Signaling the unfolded protein response from the endoplasmic reticulum. J Biol Chem 2004;279:25935-25938.
48. Pahl HL. Signal transduction from the endoplasmic reticulum to the cell nucleus. Physiol Rev 1999;79:683-701.
49. Knorre A, Wagner M, Schaefer HE, Colledge WH, Pahl HL. DeltaF508-CFTR causes constitutive NF-κB activation through an ER-overload response in cystic fibrosis lungs. Biol Chem 2002;383:271-282.
50. Lawless MW, Greene CM, Mulgrew A, Taggart CC, O'Neill SJ, McElvaney NG. Activation of endoplasmic reticulum-specific stress responses with the conformational disease Z α1-antitrypsin deficiency. J Immunol 2004;172:5722-5726.
51. Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 1992;357:605-607.
52. Davis RL, Shrimpton AE, Holohan PD, Bradshaw C, Feiglin D, Collins GH, Sonderegger P, Kinter J, Becker LM, Lacbawan F, Krasnewich D, Muenke M, Lawrence DA, Yerby MS, Shaw CM, et al. Familial dementia caused by polymerization of mutant neuroserpin. Nature 1999;401:376-379.
53. Ellis RJ. Do molecular chaperones have to be proteins? Biochem Biophys Res Commun 1997;238:687-692.
54. Nishikawa S, Fewell SW, Kato Y, Brodsky JL, Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 2001;153:1061-1069.
55. Mahadeva R, Dafforn TR, Carrell RW, Lomas DA. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z α1-antitrypsin-related cirrhosis. J Biol Chem 2002;277:6771-6774.
56. Miranda E, Römisch K, Lomas DA. Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J Biol Chem 2004;279:28283-28291.
57. Rivera VM, Wang X, Wardwell S, Courage NL, Volchuk A, Keenan T, Holt DA, Gilman M, Orci L, Cerasoli F, Rothman JE, Clackson T. Regulation of protein secretion through controlled aggregation in the endoplasmic reticulum. Science 2000;287:826-830.