Chaperone therapy update: Fabry disease, GM1-gangliosidosis and Gaucher disease

Brain and Development

Volumn 35, Issue 6, 2013, Pages 515-523

  Suzuki, Yoshiyuki ^a  

^a INTERNATIONAL UNIVERSITY OF HEALTH AND WELFARE   (Japan)

Author keywords

Galactosidase A; Galactosidase; Glucosidase; Chaperone therapy; Fabry disease; GM1 gangliosidosis; Gaucher disease; Misfolding; Morquio B disease

Indexed keywords

ANTIPAIN; BESTATIN; BETA GLUCOSIDASE; CHYMOSTATIN; ELASTATINAL; GLYCOSIDASE INHIBITOR; LEUPEPTIN; MIGALASTAT; MTD 118; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; N OCTYL 4 EPI BETA VALIENAMINE; N OCTYL BETA VALIENAMINE; PEPSTATIN; PHOSPHORAMIDON; UNCLASSIFIED DRUG;

AREA UNDER THE CURVE; BLOOD BRAIN BARRIER; CATALYSIS; CHAPERONE THERAPY; CLINICAL EFFECTIVENESS; CORRELATION ANALYSIS; DIARRHEA; DRUG ABSORPTION; DRUG HALF LIFE; DRUG INDUCED HEADACHE; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME REPLACEMENT; ENZYME SUBSTRATE; FABRY DISEASE; FIBROBLAST; GAUCHER DISEASE; GENE MUTATION; GM1 GANGLIOSIDOSIS; GOLGI COMPLEX; HUMAN; IN VITRO STUDY; LYSOSOME; MAXIMUM PLASMA CONCENTRATION; MIDDLE AGED; MOLECULAR INTERACTION; MOLECULARLY TARGETED THERAPY; NIEMANN PICK DISEASE; NONHUMAN; PHENOTYPE; PROTEIN EXPRESSION; REVIEW; TIME TO MAXIMUM PLASMA CONCENTRATION; TREATMENT RESPONSE;

ANIMALS; FABRY DISEASE; GANGLIOSIDOSIS, GM1; GAUCHER DISEASE; HUMANS; MOLECULAR CHAPERONES;

EID: 84876793140     PISSN: 03877604     EISSN: 18727131     Source Type: Journal    
DOI: 10.1016/j.braindev.2012.12.002     Document Type: Review

References (65)

1. Online Mendelian Inheritance in Man (OMIM). An Online Catalog of Human Genes and Genetic Disorders. Baltimore: McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University. http://www.omim.org/.
2. De Duve C., Wattiaux R. Functions of lysosomes. Annu Rev Physiol 1966, 28:435-492.
3. Suzuki Y., Ogawa S., Sakakibara Y. Chaperone therapy for neuronopathic lysosomal diseases: competitive inhibitors as chemical chaperones for enhancement of mutant enzyme activities. Perspect Med Chem 2009, 3:7-19.
4. Brady R.O. Emerging strategies for the treatment of hereditary metabolic storage disorders. Rejuvenation Res 2006, 9:237-244.
5. Suzuki Y., Sakuraba H., Hayashi K., Suzuki K., Imahori K. β-Galactosidase-neuraminidase deficiency: restoration of β-galactosidase activity by protease inhibitors. J Biochem 1981, 90:271-273.
6. Sakuraba H., Aoyagi T., Suzuki Y. Galactosialidosis (β-galactosidase-neuraminidase deficiency): a possible role of serine-thiol proteases in the degradation of β-galactosidase molecules. Clin Chim Acta 1982, 125:275-282.
7. Ko Y.M., Yamanaka T., Umeda M., Suzuki Y. Effects of thiol protease inhibitors on intracellular degradation of exogenous β-galactosidase in cultured human skin fibroblasts. Exp Cell Res 1983, 148:525-529.
8. M1-gangliosidosis and Morquio B disease. The online metabolic and molecular bases of inherited disease 2008, 1-101. McGraw-Hill, New York, http://www.ommbid.com/. D. Valle, A.L. Beaudet, B. Vogelstein, K.W. Kinzler, S.F. Antonarakis, A. Ballabio (Eds.).
9. M1-gangliosidosis: a common mutation among Japanese adult/chronic cases. Am J Hum Genet 1991, 49:435-442.
10. Oshima A., Yoshida K., Shimmoto M., Fukuhara Y., Sakuraba H., Suzuki Y. Human β-galactosidase gene mutations in morquio B disease. Am J Hum Genet 1991, 49:1091-1093.
11. M1-gangliosidosis in adults: clinical and molecular analysis of 16 Japanese patients. Ann Neurol 1992, 31:328-332.
12. Okumiya T., Ishii S., Kase R., Kamei S., Sakuraba H., Suzuki Y. α-Galactosidase gene mutations in Fabry disease: heterogeneous expressions of mutant enzyme proteins. Hum Genet 1995, 95:557-561.
13. Ishii S., Kase R., Sakuraba H., Suzuki Y. The functional role of glutamine-280 and threonine-282 in human α-galactosidase. Biochim Biophys Acta 1995, 1270:163-167.
14. Okumiya T., Ishii S., Takenaka T., Kase R., Kamei S., Sakuraba H., et al. Galactose stabilizes various missense mutants of α-galactosidase in Fabry disease. Biochem Biophys Res Commun 1995, 214:1219-1224.
15. Ishii S., Kase R., Sakuraba H., Suzuki Y. Characterization of a mutant α-galactosidase gene product for the late-onset cardiac form of Fabry disease. Biochem Biophys Res Commun 1993, 197:1585-1589.
16. Suzuki Y. β-Galactosidase deficiency: an approach to chaperone therapy. J Inherit Metab Dis 2006, 29:471-476.
17. The Human Gene Mutation Database (HGMD). Cardiff: Cardiff University. http://www.hgmd.cf.ac.uk.
18. Bishop D.F., Calhoun D.H., Bernstein H.S., Hantzopoulos P., Quinn M., Desnick R.J. Human α-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. Proc Natl Acad Sci U S A 1986, 83:4859-4863.
19. Ishii S., Sakuraba H., Suzuki Y. Point mutations in the upstream region of the α-galactosidase A gene exon 6 in an atypical variant of Fabry disease. Hum Genet 1992, 89:29-32.
20. Kase R., Bierfreund U., Klein A., Kolter T., Utsumi K., Itoha K., et al. Characterization of two α-galactosidase mutants (Q279E and R301Q) found in an atypical variant of Fabry disease. Biochim Biophys Acta 2000, 1501:227-235.
21. Frustaci A., Chimenti C., Ricci R., Natale L., Russo M.A., Pieroni M., et al. Improvement in cardiac function in the cardiac variant of Fabry's disease with galactose-infusion therapy. N Engl J Med 2001, 345:25-32.
22. Asano N., Kato A., Miyauchi M., Kizu H., Tomimori T., Matsui K., et al. Specific α-galactosidase inhibitors, N-methylcalystegines - structure/activity relationships of calystegines from Lycium chinense. Eur J Biochem 1997, 248:296-303.
23. Asano N., Kato A., Matsui K., Watson A.A., Nash R.J., Molyneux R.J., et al. The effects of calystegines isolated from edible fruits and vegetables on mammalian liver glycosidases. Glycobiology 1997, 7:1085-1088.
24. Fan J.Q., 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.
25. Tominaga L., Ogawa Y., Taniguchi M., Ohno K., Matsuda J., Oshima A., et al. Galactonojirimycin derivatives restore mutant human β-galactosidase activities expressed in fibroblasts from enzyme-deficient knockout mouse. Brain Dev 2001, 23:284-287.
26. Meikle P.J., Hopwood J.J., Clague A.E., Carey W.F. Prevalence of lysosomal storage disorders. JAMA 1999, 281:249-254.
27. Ozkara H.A., Topcu M. Sphingolipidoses in Turkey. Brain Dev 2004, 26:363-366.
28. M1-gangliosidosis. Correlation of clinical and biochemical data. Arch Neurol 1971, 24:58-64.
29. M1 in cultured skin fibroblasts and correlation with clinical types. Hum Genet 1978, 43:127-131.
30. Suzuki Y., Suzuki K. Glycosphingolipid β-galactosidases. I. Standard assay procedures and characterization by electrofocusing and gel filtration of the enzymes in normal human liver. J Biol Chem 1974, 249:2098-2104.
31. Suzuki Y., Suzuki K. Glycosphingolipid β-galactosidases. II. Electrofocusing characterization of the enzymes in human globoid cell leukodystrophy (Krabbe's disease). J Biol Chem 1974, 249:2105-2108.
32. Suzuki Y., Miyatake T., Fletcher T.F., Suzuki K. Glycosphingolipid β-galactosidases. III. Canine form of globoid cell leukodystrophy; comparison with the human disease. J Biol Chem 1974, 249:2109-2112.
33. M1-gangliosides. J Biol Chem 1974, 249:2113-2117.
34. Suzuki Y., Nakamura N., Fukuoka K., Shimada Y., Uono M. β-Galactosidase deficiency in juvenile and adult patients. Report of six Japanese cases and review of literature. Hum Genet 1977, 36:219-229.
35. M1-gangliosidosis: abnormalities in biosynthesis and early processing of β-galactosidase in fibroblasts. Biochem Biophys Res Commun 1988, 152:794-800.
36. M1-gangliosidosis fibroblasts. Nature 1978, 275:754-755.
37. M1-gangliosidosis. Clin Genet 1990, 38:274-280.
38. M1-gangliosidosis. Mol Genet Metab 2008, 94:204-211.
39. M1-gangliosidosis. Proc Natl Acad Sci U S A 2003, 100:15912-15917.
40. M1-gangliosidosis. Glycoconj J 1997, 14:729-736.
41. Lin H., Sugimoto Y., Ohsaki Y., Ninomiya H., Oka A., Taniguchi M., et al. N-octyl-β-valienamine up-regulates activity of F213I mutant β-glucosidase in cultured cells: a potential chemical chaperone therapy for Gaucher disease. Biochim Biophys Acta 2004, 1689:219-228.
42. Iwasaki H., Watanabe H., Iida M., Ogawa S., Tabe M., Higaki K., et al. Fibroblast screening for chaperone therapy in β-galactosidosis. Brain Dev 2006, 28:482-486.
43. M1-gangliosidosis. Ann Neurol 2007, 62:671-675.
44. M1-gangliosidosis. Cell Mol Life Sci 2008, 65:351-353.
45. M1-gangliosidosis. Mol Genet Metab 2012, 106:92-98.
46. M1-gangliosidosis. Chem Commun 2012, 48:6514-6516.
47. M1-gangliosidosis patient. Eur J Paediatr Neurol 2009, 13:160-164.
48. M1-gangliosidosis. Biochem Biophys Res Commun 2008, 367:616-622.
49. M1-gangliosidosis mouse and its restoration by chemical chaperone. J Neurochem 2011, 118:399-406.
50. Higaki K., Li L., Bahrudin U., Okuzawa S., Takamuram A., Yamamoto K., et al. Chemical chaperone therapy: chaperone effect on mutant enzyme and cellular pathophysiology in β-galactosidase deficiency. Hum Mutat 2011, 32:843-852.
51. Jo H., Yugi K., Ogawa S., Suzuki Y., Sakakibara Y. Molecular basis of chemical chaperone effects of N-octyl-β-valienamine on human β-glucosidase in low/neutral pH conditions. J Proteomics Bioinform 2010, 3:104-112.
52. Luan Z, Li L, Higaki K, Nanba E, Suzuki Y, Ohno K. The chaperone activity and toxicity of ambroxol on Gaucher cells and normal mice. Brain Dev, in press.
53. Ogawa S., Ashiura M., Uchida C., Watanabe S., Yamazaki C., Yamagishi K., et al. Synthesis of potent β-d-glucocerebrosidase inhibitors: N-alkyl-β-valienamines. Bioorg Med Chem Lett 1996, 6:929-932.
54. Lei K., Ninomiya H., Suzuki M., Inoue T., Sawa M., Iida M., et al. Enzyme enhancement activity of N-octyl-β-valienamine on β-glucosidase mutants associated with Gaucher disease. Biochim Biophys Acta 2007, 1772:587-596.
55. Luan Z., Higaki K., Aguilar-Moncayo M., Ninomiya H., Ohno K., Garcia-Moreno M.I., et al. Chaperone activity of bicyclic nojirimycin analogues for Gaucher mutations in comparison with N-(n-nonyl)deoxynojirimycin. ChemBioChem 2009, 10:2780-2792.
56. Luan Z., Li L., Ninomiya H., Ohno K., Ogawa S., Kubo T., et al. The pharmacological chaperone effect of N-octyl-β-valienamine on human mutant acid β-glucosidases. Blood Cells Mol Dis 2010, 44:48-54.
57. Luan Z., Ninomiya H., Ohno K., Ogawa S., Kubo T., Iida M., et al. The effect of N-octyl-β-valienamine on β-glucosidase activity in tissues of normal mice. Brain Dev 2010, 32:805-809.
58. Luan Z., Higaki K., Aguilar-Moncayo M., Li L., Ninomiya H., Nanba E., et al. A fluorescent sp(2)-Iminosugar with pharmacological chaperone activity for Gaucher disease: synthesis and iIntracellular distribution studies. ChemBioChem 2010, 11:2453-2464.
59. Li L., Higaki K., Ninomiya H., Luan Z., Iida M., Ogawa S., et al. Chemical chaperone therapy: luciferase assay for screening of β-galactosidase mutations. Mol Genet Metab 2010, 101:364-369.
60. Maegawa G.H., Tropak M.B., Buttner J.D., Rigat B.A., Fuller M., Pandit D., et al. Identification and characterization of ambroxol as an enzyme enhancement agent for Gaucher disease. J Biol Chem 2009, 284:23502-23516.
61. Lachmann R.H. Enzyme replacement therapy for lysosomal storage diseases. Curr Opin Pediatr 2011, 23:588-593.
62. Aerts J.M., Hollak C.E., Boot R.G., Groener J.E., Maas M. Substrate reduction therapy of glycosphingolipid storage disorders. J Inherit Metab Dis 2006, 29:449-456.
63. Wraith J.E., Vecchio D., Jacklin E., Abel L., Chadha-Boreham H., Luzy C., et al. Miglustat in adult and juvenile patients with Niemann-Pick disease type C: long-term data from a clinical trial. Mol Genet Metab 2010, 99:351-357.
64. Masciullo M, Santoro M, Modoni A, Ricci E, Guitton J, Tonali P, et al. Substrate reduction therapy with miglustat in chronic GM2 gangliosidosis type Sandhoff: results of a 3-year follow-up. J Inherit Metab Dis [serial on the Internet] 2010: Available from:. http://www.ncbi.nlm.nih.gov/pubmed/20821051.
65. Oshima A., Tsuji A., Nagao Y., Sakuraba H., Suzuki Y. Cloning, sequencing, and expression of cDNA for human β-galactosidase. Biochem Biophys Res Commun 1988, 157:238-244.