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  • Reduced glucosylceramide in the mouse model of Fabry disease: correction by successful enzyme replacement therapy.

Reduced glucosylceramide in the mouse model of Fabry disease: correction by successful enzyme replacement therapy.

Gene (2013-12-18)
Rui Quinta, Daniel Rodrigues, Marisa Assunção, Maria Fatima Macedo, Olga Azevedo, Damião Cunha, Pedro Oliveira, Maria Clara Sá Miranda
ABSTRACT

Fabry disease is an X-linked lysosomal storage disease (LSD) caused by deficient activity of α-Galactosidase A (α-Gal A). As a result, glycosphingolipids, mainly globotriaosylceramide (Gb3), progressively accumulate in body fluids and tissues. Studies aiming at the identification of secondary lipid alterations in Fabry disease may be potentially useful for the monitorization of the response to enzyme replacement therapy (ERT) and development of future therapies. The focus of this study was to evaluate if α-Gal A deficiency has an effect on two key groups of molecules of sphingolipids metabolism: glucosylceramides (GlucCers) and ceramides (Cers). Studies performed in a mouse model of Fabry disease showed reduced level of GlucCer and normal level of Cer in plasma, liver, spleen, kidney and heart. Moreover, analysis of GlucCer isoforms in Fabry knockout mice showed that GlucCer isoforms are unequally reduced in different tissues of these animals. ERT had a specific effect on the liver's GlucCer levels of Fabry knockout mice, increasing hepatic GlucCer to the levels observed in wild type mice. In contrast to Fabry knockout mice, plasma of Fabry patients had normal GlucCer and Cer but an increased GlucCer/Cer ratio. This alteration showed a positive correlation with plasma globotriaosylsphingosine (lyso-Gb3) concentration. In conclusion, this work reveals novel secondary lipid imbalances caused by α-Gal A deficiency.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
α-Galactosidase from green coffee beans, ammonium sulfate suspension, ≥9 units/mg protein
Avanti
Lyso GB3 (synthetic), powder
Sigma-Aldrich
α-Galactosidase, positionally specific from Escherichia coli, recombinant, expressed in E. coli, buffered aqueous solution