The role of chaperone-assisted folding and quality control in inborn errors of metabolism: Protein folding disorders

Journal of Inherited Metabolic Disease

Volumn 24, Issue 2, 2001, Pages 189-212

  Gregersen, N ^b   Bross, P ^c   Andresen, B S ^a   Pedersen, C B ^c   Corydon, T J ^a   Bolund, L ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b AARHUS UNIVERSITY HOSPITAL   (Denmark)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; FATTY ACID; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; LECTIN; MUTANT PROTEIN; PHENYLALANINE 4 MONOOXYGENASE; PROTEASOME; PROTEIN DISULFIDE ISOMERASE; PROTEINASE; STRUCTURAL PROTEIN;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CELL FATE; CONTROLLED STUDY; FATTY ACID OXIDATION; GENETIC VARIABILITY; HUMAN; HUMAN CELL; HYPERTROPHIC CARDIOMYOPATHY; IN VITRO STUDY; INBORN ERROR OF METABOLISM; LOW TEMPERATURE; METABOLIC DISORDER; MISSENSE MUTATION; NONHUMAN; PATHOLOGY; PATIENT CARE; PHENYLKETONURIA; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN SYNTHESIS; QUALITY CONTROL; RAT;

ANIMALS; HUMANS; METABOLISM, INBORN ERRORS; MOLECULAR CHAPERONES; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0035000631     PISSN: 01418955     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010319001722     Document Type: Article

References (67)

1. Andresen BS, Bross P, Udvari S, et al (1997) The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in compound heterozygous patients: is there correlation between genotype and phenotype? Hum Mol Genet 6: 695-707.
2. Andresen BS, Olpin S, Poorthuis BJ, et al (1999) Clear correlation of genotype with disease phenotype in very-long-chain acyl-CoA dehydrogenase deficiency. Am J Hum Genet 64: 479-494.
3. Bonne G, Carrier L, Richard P, et al (1998) Familial hypertrophic cardiomyopathy: from mutations to functional defects. Circ Res 83: 580-593.
4. Bross P, Andresen BS, Winter V, et al (1993) Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim Biophys Acta 1182: 264-274.
5. Bross P, Jespersen C, Jensen TG, et al (1995a) Effects of two mutations detected in medium chain acyl-CoA dehydrogenase (MCAD)-deficient patients on folding, oligomer assembly, and stability of MCAD enzyme. J Biol Chem 270: 10284-10290.
6. Bross P, Andresen BS, Knudsen I, et al (1995b) Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene. FEBS Lett 377: 249-252.
7. Bross P, Corydon TJ, Andresen BS, et al (1999) Protein misfolding and degradation in genetic disease. Hum Mutat 14: 186-198.
8. Bukau B and Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
9. Bukau B, Deuerling E, Pfund C, et al (2000) Getting newly synthesized proteins into shape. Cell 101: 119-122.
10. Burrows JA, Willis LK, Perlmutter DH (2000) Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: a potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc Natl Acad Sci USA 97: 1796-1801.
11. Carrell RW, Lomas DA (1997) Conformational disease. Lancet 350: 134-138.
12. Casari G, De Fusco M, Ciarmatori S, et al (1998) Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93: 973-983.
13. Corydon MJ, Gregersen N, Lehnert W, et al (1996) Ethylmalonic aciduria is associated with an amino acid variant of short-chain acyl-coenzyme A dehydrogenase. Pediatr Res 39: 1059-1066.
14. Corydon TJ, Bross P, Jensen TG, et al (1998) Rapid degradation of short-chain acyl-CoA dehydrogenase (SCAD) variants with temperature-sensitive folding defects occur after import into mitochondria. J Biol Chem 273: 13065-13071.
15. Corydon MJ, Vockley J, Rinaldo P, et al (2001) Role of common gene variations in the molecular pathogenesis of short-chain acyl-CoA dehydrogenase deficiency. Pediatr Res 49: 18-23.
16. Corydon TJ, Wilsbech M, Jespersgaard C, et al (2000b) Human and mouse mitochondrial orthologs of bacterial clpX. Mamm Genome 11: 899-905.
17. Culbertson MR (1999) RNA surveillance. Unforeseen consequences for gene expression, inherited genetic disorders and cancer. Trends Genet 15: 74-80.
18. Feldman DE, Frydman J (2000) Protein folding in vivo: the importance of molecular chaperones. Curr Opin Struct Biol 10: 26-33.
19. Frischmeyer PA, Dietz HC (1999) Nonsense-mediated mRNA decay in health and disease. Hum Mol Genet 8: 1893-1900.
20. Frydman J, Hohfeld J (1997) Chaperones get in touch: the Hip-Hop connection. Trends Biochem Sci 22: 87-92.
21. Fuchs E (1996) The cytoskeleton and disease: genetic disorders in intermediate filaments. Annu Rev Genet 30: 197-231.
22. Gamez A, Perez B, Ugarte M, et al (2000) Expression analysis of phenylketonuria mutations. Effect on folding and stability of the phenylalanine hydroxylase protein. J Biol Chem 275: 29737-29742.
23. Gething MJ, Sambrook J (1992) Protein folding in the cell. Nature 355: 33-45.
24. Gottesman S, Wickner S, Maurizi MR (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
25. Gregersen N, Winter VS, Corydon MJ, et al (1998) Identification of four new mutations in the short-chain acyl-CoA dehydrogenase (SCAD) gene in two patients: one of the variant alleles, 511C>T, is present at an unexpectedly high frequency in the general population, as was the case for 625G>A, together conferring susceptibility to ethylmalonic aciduria. Hum Mol Genet 7: 619-627.
26. Hammond C, Helenius A (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J Cell Biol 126: 41-52.
27. Hard FU (1996) Molecular chaperones in cellular protein folding. Nature 381: 571-579.
28. Hazan J, Fonknechten N, Mavel D, et al (1999) Spastin, a new AAA protein, is altered in the most frequent form of autosomal dominant spastic paraplegia. Nature Genetics 23: 296-303.
29. Horwich AL, Low KB, Fenton WA, et al (1993) Folding in vivo of bacterial cytoplasmic proteins - role of GroEL. Cell 74: 909-917.
30. Hurtley SM, Helenius A (1989) Protein oligomerization in the endoplasmic reticulum. Annu Rev Cell Biol 5: 277-307.
31. Imamura A, Tamura S, Shimozawa N, et al (1998) Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders. Hum Mol Genet 7: 2089-2094.
32. Jensen TG, Bross P, Andresen BS, et al (1995) Comparison between medium-chain acyl-CoA dehydrogenase mutant proteins overexpressed in bacterial and mammalian cells. Hum Mutat 6: 226-231.
33. Jorgensen MM, Jensen ON, Holst H, et al (2000) Grp78 is involved in retention of mutant low-density lipoprotein receptor protein in the endoplasmic reticulum. J Biol Chem 275: 33861-33868.
34. Kalin N, Claass A, Sommer M, et al (1999) DeltaF508 CFTR protein expression in tissues from patients with cystic fibrosis. J Clin Invest 103: 1379-1389.
35. Katsanis N, Beales PL, Woods MO, et al (2000) Mutations in MKKS cause obesity, retinal dystrophy and renal malformations associated with Bardet-Biedl syndrome. Nature Genetics 26: 67-70.
36. Kayaalp E, Treacy E, Waters PJ, et al (1997) Human phenylalanine hydroxylase mutations and hyperphenylalaninemia phenotypes: a metanalysis of genotype-phenotype correlations. Am J Hum Genet 61: 1309-1317.
37. Kelley WL (1998) The J-domain family and the recruitmnent of chaperone power. Trends Biochem Sci 23: 222-227.
38. Kieweg V, Krautle FG, Nandy A, et al (1997) Biochemical characterization of purified, human recombinant Lys304→Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme. Eur J Biochem 246: 548-556.
39. Leonhard K, Guiard B, Pellecchia G, et al (2000) Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol Cell 5: 629-638.
40. Lindquist S, Craig EA (1988) The heat-shock proteins. Annu Rev Genet 22: 631-677.
41. Litt M, Kramer P, LaMorticella DM, et al (1998) Autosomal dominant congenital cataract associated with a missense mutation in the human alpha crystallin gene CRYAA. Hum Mol Genet 7: 471-474.
42. Martin J (1997) Molecular chaperones and mitochondrial protein folding. J Bioenerg Biomembr 29: 35-43.
43. Molinari M, Helenius A (2000) Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288: 331-333.
44. Nagy E, Maquat LE (1998) A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem Sci 23: 198-199.
45. Naito E, Indo Y, Tanaka K (1989) Short chain acyl-coenzyme A dehydrogenase (SCAD) deficiency. Immunochemical demonstration of molecular heterogeneity due to variant SCAD with differing stability. J Clin Invest 84: 1671-1674.
46. Neuwald AF, Aravind L, Spouge JL, et al (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27-43.
47. Perlmutter DH (1999) Misfolded proteins in the endoplasmic reticulum. Lab Invest 79: 623-638.
48. Pind S, Riordan JR, Williams DB (1994) Participation of the endoplasmic reticulum chaperone calnexin (P88, Ip90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269: 12784-12788.
49. Saijo T, Tanaka K (1995) Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of medium chain Acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. J Biol Chem 270: 1899-1907.
50. Saijo T, Welch WJ, Tanaka K (1994) Intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD) - demonstration of impaired transfer of K304E-variant MCAD from its complex with Hsp60 to the native tetramer. J Biol Chem 269: 4401-4408.
51. Scherzinger E, Sittler A, Schweiger K, et al (1999) Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc Natl Acad Sci USA 96: 4604-4609.
52. Selkoe DJ (1996) Amyloid beta-protein and the genetics of Alzheimer's disease. J Biol Chem 271: 18295-18298.
53. Stone DL, Slavotinek A, Bouffard GG, et al (2000) Mutation of a gene encoding a putative chaperonin causes McKusick-Kaufman syndrome. Nature Genetics 25: 79-82.
54. Taroni F, Verderio E, Dworzak F, et al (1993) Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients. Nature Genetics 4: 314-319.
55. Thomas PJ, Qu BH, Pedersen PL (1995) Defective protein folding as a basis of human disease. Trends Biochem Sci 20: 456-459.
56. Thulasiraman V, Yang CF, Frydman J (1999) In vivo newly translated polypeptides are sequestered in a protected folding environment. EMBO J 18: 85-95.
57. Vainberg IE, Lewis SA, Rommelaere H, et al (1998) Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93: 863-873.
58. Vicart P, Caron A, Guicheney P, et al (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nature Genetics 20: 92-95.
59. Vockley J, Nguyen T, Corydon MJ, et al (2000) Biochemical, functional characterization, and clinical implications of the common polymorphic variations in SCAD. J Inherit Metab Dis 23(Supplement 1): 122.
60. Wang N, Gottesman S, Willingham MC, et al (1993) A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc Natl Acad Sci USA 90: 11247-11251.
61. Waters PJ, Parniak MA, Nowacki P, et al (1998) In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function. Hum Mutat 11: 4-17.
62. Waters PJ, Parniak MA, Akerman BR, et al (1999) Missense mutations in the phenylalanine hydroxylase gene (PAH) can cause accelerated proteolytic turnover of PAH enzyme: a mechanism underlying phenylketonuria. J Inherit Metab Dis 22: 208-212.
63. Waters PJ, Parniak MA, Akerman BR, et al (2000) Characterization of phenylketonuria missense substitutions, distant from the phenylalanine hydroxylase active site, illustrates a paradigm for mechanism and potential modulation of phenotype. Mol Genet Metab 69: 101-110.
64. Wu Y, Whitman I, Molmenti E, et al (1994) A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. Proc Natl Acad Sci USA 91: 9014-9018.
65. Zerr I, Schulz-Schaeffer WJ, Giese A, et al (2000) Current clinical diagnosis in Creutzfeldt-Jakob disease: identification of uncommon variants. Ann Neurol 48: 323-329.
66. Zhang JX, Braakman I, Matlack KES, et al (1997) Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol Biol Cell 8: 1943-1954.
67. Zhu Z, Yao J, Johns T, et al (1998) SURF1, encoding a factor involved in the biogenesis of cytochrome c oxidase, is mutated in Leigh syndrome. Nature Genetics 20: 337-343.