Fabry disease genotype, phenotype, and migalastat amenability: Insights from a national cohort.


Journal

Journal of inherited metabolic disease
ISSN: 1573-2665
Titre abrégé: J Inherit Metab Dis
Pays: United States
ID NLM: 7910918

Informations de publication

Date de publication:
03 2020
Historique:
received: 25 04 2019
revised: 12 07 2019
accepted: 19 08 2019
pubmed: 27 8 2019
medline: 3 7 2021
entrez: 27 8 2019
Statut: ppublish

Résumé

Fabry disease (FD) is a rare X-linked lysosomal storage disorder caused by α-galactosidase A (α-Gal A) deficiency. The progressive accumulation of globotriaosylceramide results in life-threatening complications, including renal, cardiac, and cerebrovascular diseases. The pharmacological chaperone migalastat was recently approved as an alternative to enzyme replacement therapy in patients with amenable mutations. In this article, we investigate the proportion of amenable mutations, related to phenotype, in a population of adult patients with FD in Switzerland. This study included 170 adult patients (n = 64 males) from 46 independent pedigrees with 39 different identified mutations over the last 59 years. Overall, 68% had the classic phenotype and 48% fulfilled the current amenability criteria. Migalastat was stopped in 2/11 (18%) patients: the only male classic patient, because of lack of efficacy based on lyso-Gb3 levels, and one patient with a benign variant. In males, the achieved enzyme activities in peripheral leucocytes under migalastat treatment differed from the activities in HEK-cells after incubation with migalastat (eg, 33% in PL vs 41% HEK-cells for p.F113L; 43% in leucocytes vs 36% in HEK-cells for p.N215S, 24-30% in leucocytes vs 96% in HEK-cells for S238N). In this national cohort, we found a relatively high proportion of patients with amenable GLA mutations, which, however, had heterogeneous extent of amenability: the higher the residual α-Gal A activity, the higher the chaperone effect. Further studies are required to investigate the long-term benefits of migalastat therapy depending on the achieved enzyme activities in different amenable mutations.

Identifiants

pubmed: 31449323
doi: 10.1002/jimd.12167
doi:

Substances chimiques

1-Deoxynojirimycin 19130-96-2
migalastat C4XNY919FW
alpha-Galactosidase EC 3.2.1.22

Types de publication

Journal Article Multicenter Study

Langues

eng

Sous-ensembles de citation

IM

Pagination

326-333

Informations de copyright

© 2019 SSIEM.

Références

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Auteurs

Albina Nowak (A)

Department of Endocrinology and Clinical Nutrition, University Hospital Zurich and University of Zurich, Zurich, Switzerland.
Department of Internal Medicine, Psychiatry University Hospital Zurich, Zurich, Switzerland.

Uyen Huynh-Do (U)

Department of Nephrology and Hypertension, University Hospital Bern and University of Bern, Bern, Switzerland.

Pierre-Alexandre Krayenbuehl (PA)

Department of Internal Medicine, Linth Hospital, Uznach, Switzerland.

Felix Beuschlein (F)

Department of Endocrinology and Clinical Nutrition, University Hospital Zurich and University of Zurich, Zurich, Switzerland.

Raphael Schiffmann (R)

Institute of Metabolic Disease, Baylor Scott & White Research Institute, Dallas, Texas.

Frédéric Barbey (F)

Division of Genetic Medicine, Lausanne University Hospital and University of Lausanne, Lausanne, Switzerland.

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