Lucerastat, an Iminosugar for Substrate Reduction Therapy: Tolerability, Pharmacodynamics, and Pharmacokinetics in Patients With Fabry Disease on Enzyme Replacement

Clinical Pharmacology and Therapeutics

Volumn 103, Issue 4, 2018, Pages 703-711

  Guérard, Nicolas ^a   Oder, Daniel ^b   Nordbeck, Peter ^b   Zwingelstein, Christian ^c   Morand, Olivier ^a   Welford, Richard W D ^a   Dingemanse, Jasper ^a   Wanner, Christoph ^b  

^a IDORSIA PHARMACEUTICALS LTD   (Switzerland)

^b UNIVERSITY HOSPITAL WÜRZBURG   (Germany)

^c ACTELION PHARMACEUTICALS LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AGALSIDASE ALFA; AGALSIDASE BETA; GLOBOTRIAOSYLCERAMIDE; GLUCOSYLCERAMIDE; LACTOSYLCERAMIDE; LUCERASTAT; 1 DEOXYNOJIRIMYCIN; ALPHA GALACTOSIDASE; CERAMIDE GLUCOSYLTRANSFERASE; ENZYME INHIBITOR; GLUCOSYLTRANSFERASE; MIGALASTAT;

ADULT; AREA UNDER THE CURVE; ARTICLE; ATRIAL FIBRILLATION; BLEEDING; CLINICAL ARTICLE; CONTROLLED STUDY; CYSTITIS; DIZZINESS; DRUG BLOOD LEVEL; DRUG SAFETY; DRUG TOLERABILITY; DRY SKIN; ELIMINATION HALF-LIFE; ENZYME REPLACEMENT; EXPLORATORY RESEARCH; FABRY DISEASE; FATIGUE; FEMALE; FLATULENCE; HOT FLUSH; HUMAN; HYPONATREMIA; LIPID BLOOD LEVEL; MALE; MAXIMUM PLASMA CONCENTRATION; MIDDLE AGED; NAUSEA; OPEN STUDY; PHARMACODYNAMICS; PLASMA CONCENTRATION-TIME CURVE; PRIORITY JOURNAL; RANDOMIZED CONTROLLED TRIAL; RHINOPHARYNGITIS; TIME TO MAXIMUM PLASMA CONCENTRATION; VERTIGO; VIRAL RESPIRATORY TRACT INFECTION; ANALOGS AND DERIVATIVES; ANTAGONISTS AND INHIBITORS; DRUG MONITORING; METABOLISM; ORAL DRUG ADMINISTRATION; PROCEDURES; TREATMENT OUTCOME;

1-DEOXYNOJIRIMYCIN; ADMINISTRATION, ORAL; ADULT; ALPHA-GALACTOSIDASE; DRUG MONITORING; ENZYME INHIBITORS; ENZYME REPLACEMENT THERAPY; FABRY DISEASE; FEMALE; GLUCOSYLTRANSFERASES; HUMANS; MALE; MIDDLE AGED; TREATMENT OUTCOME;

EID: 85038835877     PISSN: 00099236     EISSN: 15326535     Source Type: Journal    
DOI: 10.1002/cpt.790     Document Type: Article

References (50)

1. Germain, D.P. Fabry disease. Orphanet J. Rare Dis. 5, 30 (2010).
2. Boustany, R.M. Lysosomal storage diseases--the horizon expands. Nat. Rev. Neurol. 9, 583–598 (2013).
3. Schiffmann, R. Fabry disease. Handb. Clin. Neurol. 132, 231–248 (2015).
4. Stenson, P.D., Ball, E., Howells, K., Phillips, A., Mort, M. & Cooper, D.N. Human Gene Mutation Database: towards a comprehensive central mutation database. J. Med. Genet. 45, 124–126 (2008).
5. Thomas, A.S. & Hughes, D.A. Fabry disease. Pediatr. Endocrinol. Rev. 12 Suppl 1, 88–101 (2014).
6. Ries, M. & Gal, A. Genotype-phenotype correlation in Fabry disease. Ch. 34. In: Fabry Disease: Perspectives From 5 Years of FOS (eds. Mehta, A., Beck, M. & Sunder-Plassmann, G.) (Springer, Oxford, UK, 2006).
7. Elleder, M. Sequelae of storage in Fabry disease--pathology and comparison with other lysosomal storage diseases. Acta Paediatr. Suppl. 92, 46–53; discussion 54 (2003).
8. MacDermot, K.D., Holmes, A. & Miners, A.H. Anderson-Fabry disease: clinical manifestations and impact of disease in a cohort of 60 obligate carrier females. J. Med. Genet. 38, 769–775 (2001).
9. MacDermot, K.D., Holmes, A. & Miners, A.H. Anderson-Fabry disease: clinical manifestations and impact of disease in a cohort of 98 hemizygous males. J. Med. Genet. 38, 750–760 (2001).
10. Schiffmann, R. Fabry disease. Pharmacol. Ther. 122, 65–77 (2009).
11. Schiffmann, R. & Ries, M. Fabry disease: a disorder of childhood onset. Pediatr. Neurol. 64, 10–20 (2016).
12. Pisani, A. et al. Enzyme replacement therapy in patients with Fabry disease: state of the art and review of the literature. Mol. Genet. Metab. 107, 267–275 (2012).
13. Schiffmann, R. et al. Enzyme replacement therapy in Fabry disease: a randomized controlled trial. JAMA 285, 2743–2749 (2001).
14. Eng, C.M. et al. A phase 1/2 clinical trial of enzyme replacement in Fabry disease: pharmacokinetic, substrate clearance, and safety studies. Am. J. Hum. Genet. 68, 711–722 (2001).
15. Najafian, B., Tondel, C., Svarstad, E., Sokolovkiy, A., Smith, K. & Mauer, M. One year of enzyme replacement therapy reduces globotriaosylceramide inclusions in podocytes in male adult patients with Fabry disease. PLoS One 11, e0152812 (2016).
16. Banikazemi, M. et al. Agalsidase-beta therapy for advanced Fabry disease: a randomized trial. Ann. Intern. Med. 146, 77–86 (2007).
17. Beck, M. et al. Long-term effectiveness of agalsidase alfa enzyme replacement in Fabry disease: a Fabry Outcome Survey analysis. Mol. Genet. Metab. Rep. 3, 21–27 (2015).
18. Weidemann, F. et al. Long-term outcome of enzyme-replacement therapy in advanced Fabry disease: evidence for disease progression towards serious complications. J. Intern. Med. 274, 331–341 (2013).
19. Germain, D.P. et al. Sustained, long-term renal stabilization after 54 months of agalsidase beta therapy in patients with Fabry disease. J. Am. Soc. Nephrol. 18, 1547–1557 (2007).
20. Thurberg, B.L., Randolph Byers, H., Granter, S.R., Phelps, R.G., Gordon, R.E. & O'Callaghan, M. Monitoring the 3-year efficacy of enzyme replacement therapy in Fabry disease by repeated skin biopsies. J. Invest. Dermatol. 122, 900–908 (2004).
21. Thurberg, B.L. et al. Globotriaosylceramide accumulation in the Fabry kidney is cleared from multiple cell types after enzyme replacement therapy. Kidney Int. 62, 1933–1946 (2002).
22. Eng, C.M. et al. Safety and efficacy of recombinant human alpha-galactosidase A replacement therapy in Fabry's disease. N. Engl. J. Med. 345, 9–16 (2001).
23. Ashe, K.M. et al. Efficacy of enzyme and substrate reduction therapy with a novel antagonist of glucosylceramide synthase for Fabry disease. Mol. Med. 21, 389–399 (2015).
24. Sakuraba, H. et al. Corrective effect on Fabry mice of yeast recombinant human alpha-galactosidase with N-linked sugar chains suitable for lysosomal delivery. J. Hum. Genet. 51, 341–352 (2006).
25. Linthorst, G.E., Hollak, C.E., Donker-Koopman, W.E., Strijland, A. & Aerts, J.M. Enzyme therapy for Fabry disease: neutralizing antibodies toward agalsidase alpha and beta. Kidney Int. 66, 1589–1595 (2004).
26. Deegan, P.B. Fabry disease, enzyme replacement therapy and the significance of antibody responses. J. Inherit. Metab. Dis. 35, 227–243 (2012).
27. Hollak, C.E. & Linthorst, G.E. Immune response to enzyme replacement therapy in Fabry disease: impact on clinical outcome? Mol. Genet. Metab. 96, 1–3 (2009).
28. Rombach, S.M. et al. Long-term effect of antibodies against infused alpha-galactosidase A in Fabry disease on plasma and urinary (lyso)Gb3 reduction and treatment outcome. PLoS One 7, e47805 (2012).
29. Lenders, M., Stypmann, J., Duning, T., Schmitz, B., Brand, S.M. & Brand, E. Serum-mediated inhibition of enzyme replacement therapy in Fabry disease. J. Am. Soc. Nephrol. 27, 256–264 (2016).
30. Germain, D.P. et al. Treatment of Fabry's disease with the pharmacologic chaperone migalastat. N. Engl. J. Med. 375, 545–555 (2016).
31. Markham, A. Migalastat: first global approval. Drugs 76, 1147–1152 (2016).
32. Germain, D.P. & Fan, J.Q. Pharmacological chaperone therapy by active-site-specific chaperones in Fabry disease: in vitro and preclinical studies. Int. J. Clin. Pharmacol. Ther. 47(suppl. 1), S111–S117 (2009).
33. Benjamin, E.R. et al. The validation of pharmacogenetics for the identification of Fabry patients to be treated with migalastat. Genet. Med. 19, 430–439 (2016).
34. Platt, F.M. & Jeyakumar, M. Substrate reduction therapy. Acta Paediatr. 97, 88–93 (2008).
35. Lachmann, R.H. Miglustat: substrate reduction therapy for glycosphingolipid lysosomal storage disorders. Drugs Today 42, 29–38 (2006).
36. Sechi, A., Dardis, A. & Bembi, B. Profile of eliglustat tartrate in the management of Gaucher disease. Ther. Clin. Risk Manag. 12, 53–58 (2016).
37. Marshall, J. et al. Substrate reduction augments the efficacy of enzyme therapy in a mouse model of Fabry disease. PLoS One 5, e15033 (2010).
38. Welford, R.W.D. et al. Lucerastat, an iminosugar substrate reduction therapy for Fabry disease: preclinical evidence. 13th Annual WORLD Symposium, San Diego, CA, 13–17 February 2017. Abstract 360.
39. Guérard, N., Morand, O. & Dingemanse, J. Lucerastat, an iminosugar with potential as substrate reduction therapy for glycolipid storage disorders: safety, tolerability, and pharmacokinetics in healthy subjects. Orphanet J. Rare Dis. 12, 9 (2017).
40. Guerard, N., Zwingelstein, C., Dingemanse, J. Lucerastat, an iminosugar for substrate reduction therapy: pharmacokinetics, tolerability, and safety in subjects with mild, moderate, and severe renal function impairment. 13th Annual WORLD Symposium, San Diego, CA, 13–17 February 2017. Abstract 122.
41. Warnock, D.G. et al. Antiproteinuric therapy and Fabry nephropathy: factors associated with preserved kidney function during agalsidase-beta therapy. J. Med. Genet. 52, 860–866 (2015).
42. Lang, R.M. et al. Recommendations for chamber quantification. Eur. Heart J. Cardiovasc. Imaging 7, 79–108 (2006).
43. Butters, T.D. et al. Molecular requirements of imino sugars for the selective control of N-linked glycosylation and glycosphingolipid biosynthesis. Tetrahedron Asymmetry 11, 113–124 (2000).
44. Remenova, T., Morand, O., Amato, D., Chadha-Boreham, H., Tsurutani, S. & Marquardt, T. A double-blind, randomized, placebo-controlled trial studying the effects of Saccharomyces boulardii on the gastrointestinal tolerability, safety, and pharmacokinetics of miglustat. Orphanet J. Rare Dis. 10, 81–90 (2015).
45. Goker-Alpan, O. et al. Reduction of plasma globotriaosylsphingosine levels after switching from agalsidase alfa to agalsidase beta as enzyme replacement therapy for Fabry disease. JIMD Rep. 25, 95–106 (2015).
46. van Breemen, M.J. et al. Reduction of elevated plasma globotriaosylsphingosine in patients with classic Fabry disease following enzyme replacement therapy. Biochim. Biophys. Acta. 1812, 70–76 (2011).
47. Ferraz, M.J. et al. Lysosomal glycosphingolipid catabolism by acid ceramidase: formation of glycosphingoid bases during deficiency of glycosidases. FEBS Lett. 590, 716–725 (2016).
48. Smid, B.E. et al. Biochemical response to substrate reduction therapy versus enzyme replacement therapy in Gaucher disease type 1 patients. Orphanet J. Rare Dis. 11, 28 (2016).
49. Weidemann, F. et al. Patients with Fabry disease after enzyme replacement therapy dose reduction versus treatment switch. J. Am. Soc. Nephrol. 25, 837–849 (2014).
50. Auray-Blais, C. & Boutin, M. Novel gb(3) isoforms detected in urine of Fabry disease patients: a metabolomic study. Curr. Med. Chem. 19, 3241–3252 (2012).