The effect of N-octyl-β-valienamine on β-glucosidase activity in tissues of normal mice

Brain and Development

Volumn 32, Issue 10, 2010, Pages 805-809

  Luan, Zhuo ^a   Ninomiya, Haruaki ^a   Ohno, Kousaku ^a   Ogawa, Seiichiro ^b   Kubo, Takatoshi ^c   Iida, Masami ^c   Suzuki, Yoshiyuki ^d  

^a TOTTORI UNIVERSITY   (Japan)

^b KEIO UNIVERSITY   (Japan)

^c SEIKAGAKU CORPORATION   (Japan)

^d INTERNATIONAL UNIVERSITY OF HEALTH AND WELFARE   (Japan)

Author keywords

Glucosidase; Chaperone therapy; Gaucher disease; N octyl valienamine

Indexed keywords

BETA GLUCOSIDASE; GLYCOSIDASE INHIBITOR; N OCTYL BETA VALIENAMINE; NITROGEN; UNCLASSIFIED DRUG; UREA;

ACUTE TOXICITY; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BLOOD CHEMISTRY; BODY WEIGHT; BRAIN; CEREBELLUM; CONTROLLED STUDY; DRUG BIOAVAILABILITY; DRUG EFFECT; DRUG SAFETY; DRUG TISSUE LEVEL; ENZYME ACTIVITY; FLUID INTAKE; HEART; KIDNEY; LIVER; LUNG; MALE; MOUSE; MUSCLE; NONHUMAN; SPLEEN; TISSUE DISTRIBUTION; UREA NITROGEN BLOOD LEVEL; URINALYSIS;

ANIMALS; BETA-GLUCOSIDASE; BLOOD CHEMICAL ANALYSIS; BODY WEIGHT; BRAIN; DOSE-RESPONSE RELATIONSHIP, DRUG; DRINKING; ENZYME INHIBITORS; GAUCHER DISEASE; HEXOSAMINES; MALE; MICE; MICE, INBRED C57BL; TISSUE DISTRIBUTION; URINALYSIS;

EID: 77957907485     PISSN: 03877604     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.braindev.2009.12.005     Document Type: Article

References (25)

1. Beutler E., Grabowski G.A. Gaucher disease. The metabolic and molecular bases of inherited disease 2001, 3635-3668. McGraw-Hill, New York. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
2. Butters T.D. Gaucher disease. Curr Opin Chem Biol 2007, 11:412-418.
3. Barton N.W., Brady R.O., Dambrosia J.M., Di Bisceglie A.M., Doppelt S.H., Hill S.C., et al. Replacement therapy for inherited enzyme deficiency-macrophage-targeted glucocerebrosidase for Gaucher's disease. N Engl J Med 1991, 324:1464-1470.
4. Cox T., Lachmann R., Hollak C., Aerts J., van Weely S., Hrebicek M., et al. Novel oral treatment of Gaucher's disease with N-butyldeoxynojirimycin (OGT918) to decrease substrate biosynthesis. Lancet 2000, 355:1481-1485.
5. Grabowski G.A., Leslie N., Wenstrup R. Enzyme therapy for Gaucher disease: the first 5 years. Blood Rev 1998, 12:115-133.
6. Platt F.M., Jeyakumar M., Andersson U., Priestman D.A., Dwek R.A., Butters T.D. Inhibition of substrate synthesis as a strategy for glycolipids lysosomal storage disease therapy. J Inherit Metab Dis 2001, 24:275-290.
7. Schiffmann R., Heyes M.P., Aerts J.M., Dambrosia J.M., Patterson M.C., DeGraba T., et al. Prospective study of neurological responses to treatment with macrophage-targeted glucocerebrosidase in patients with type 3 Gaucher's disease. Ann Neurol 1997, 42:613-621.
8. Prows C.A., Sanchez N., Daugherty C., Grabowski G.A. Gaucher disease: enzyme therapy in the acute neuronopathic variant. Am J Med Genet 1997, 71:16-21.
9. Aoki M., Takahashi Y., Miwa Y., Iida S., Sukegawa K., Horai T., et al. Improvement of neurological symptoms by enzyme replacement therapy for Gaucher disease type IIIb. Eur J Pediatr 2001, 160:63-64.
10. 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.
11. Ron I., Horowitz M. ER retention and degradation as the molecular basis underlying Gaucher disease heterogeneity. Hum Mol Genet 2005, 14:2387-2398.
12. Ogawa S., Ashiura M., Uchida C., Watanabe S., Yamazaki C., Yamagishi K., et al. Synthesis of potent beta-d-glucocerebrosidase inhibitors: N-alkyl-β-valienamines. Bioorg Med Chem Lett 1996, 6:929-932.
13. Lin H., Sugimoto Y., Ohsaki Y., Ninomiya H., Oka A., Taniguchi M., et al. N-Octyl-β-valienamine upregulates activity of F213I mutant β-glucosidase in cultured cells: a potential chemical chaperone therapy for Gaucher disease. Biochim Biophys Acta 2004, 1689:219-228.
14. Lei K., Ninomiya H., Suzuki M., Inoue T., Sawa M., Iida M., et al. Enzyme enhancement activity of N-octyl-beta-valienamine on beta-glucosidase mutants associated with Gaucher disease. Biochim Biophys Acta 2007, 1772:587-596.
15. Dvir H., Harel M., McCarthy A.A., Toker L., Silman I., Futerman A.H., et al. X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease. EMBO Rep 2003, 4:704-709.
16. Suzuki Y., Ichinomiya S., Kurosawa M., Ohkubo M., Watanabe H., Iwasaki H., et al. Chemical chaperone therapy: clinical effect in murine G(M1)-gangliosidosis. Ann Neurol 2007, 62:671-675.
17. Vaccaro A.M., Muscillo M., Tatti M., Salvioli R., Gallozzi E., Suzuki K. Effect of a heat-stable factor in human placenta on glucosylceramidase, glucosylsphingosine glucosyl hydrolase, and acid β-glucosidase activities. Clin Biochem 1987, 20:429-433.
18. Matsuda J., Suzuki O., Oshima A., Yamamoto Y., Noguchi A., Takimoto K., et al. Chemical chaperone therapy for brain pathology in G(M1)-gangliosidosis. Proc Natl Acad Sci USA 2003, 100:15912-15917.
19. 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.
20. Luan Z., Higaki K., Aguilar-Moncayo M., Ninomiya H., Ohno K., García-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.
21. Z. Luan, L. Li, H. Ninomiya, K. Ohno, S. Ogawa, T. Kubo et al., The pharmacological chaperone effect of N-octyl-beta-valienamine on human mutant acid beta-glucosidases, Blood Cells Mol Dis, 2009, doi:10.1016/j.bcmd.2009.10.003.
22. Fan J.Q., Ishii S., Asano N., Suzuki Y. Accelerated transport and maturation of lysosomeal α-galactosidase A in Fabry lymphoblasts by an enzyme inhibitor. Nat Med 1999, 5:112-115.
23. Sawkar A.R., Cheng W.C., Beutler E., Wong C.H., Balch W.E., Kelly J.W. Chemical chaperones increase the cellular activity of N370S β-glucosidase: a therapeutic strategy for Gaucher disease. Proc Natl Acad Sci USA 2002, 99:15428-15433.
24. Tropak M.B., Reid S.P., Guiral M., Withers S.G., Mahuran D. Pharmacological enhancement of β-hexosaminidase activity in fibroblasts from adult Tay-Sachs and Sandhoff patients. J Biol Chem 2004, 279:13478-13487.
25. Parenti G., Zuppaldi A., Gabriela Pittis M., Rosaria Tuzzi M., Annunziata I., Meroni G., et al. Pharmacological enhancement of mutated α-glucosidase activity in fibroblasts from patients with Pompe disease. Mol Ther 2007, 15:508-514.