Correction of the Enzymic Defect in Cultured Fibroblasts from Patients with Fabry's Disease: Treatment with Purified α-Galactosidase from Ficin

Dawson, Glyn; Matalon, Reuben; Li, Yu Teh

doi:10.1203/00006450-197308000-00002

Cited by 18 publications

(3 citation statements)

References 23 publications

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“…The rationale for enzyme replacement in Fabry's disease was initially based on in vitro correction of the metabolic defect by addition of exogenous ␣-galactosidase A to the media of cultured fibroblasts obtained from hemizygotes with Fabry disease (4). Efforts have been made in Fabry patients and in cell culture to replace the defective enzyme with normal enzyme obtained from various human and recombinant DNA sources (3,5,6).…”

mentioning

confidence: 99%

Expression and Characterization of Glycosylated and Catalytically Active Recombinant Human α-Galactosidase A Produced in Pichia pastoris

Chen

Jin

Egborge

et al. 2000

Protein Expression and Purification

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mentioning

confidence: 99%

Expression and Characterization of Glycosylated and Catalytically Active Recombinant Human α-Galactosidase A Produced in Pichia pastoris

Chen

Jin

Egborge

et al. 2000

Protein Expression and Purification

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“…The rationale for enzyme replacement in this lysosomal storage disease was based on in vitro correction of the metabolic defect by addition of exogenous a-GAL A to the media of cultured skin fibroblasts obtained from hemizygotes with Fabry disease (9). In 1970, we reported the first clinical trial (10) based on the finding that normal plasma contained active a-GAL A (2).…”

mentioning

confidence: 99%

Enzyme therapy in Fabry disease: differential in vivo plasma clearance and metabolic effectiveness of plasma and splenic alpha-galactosidase A isozymes.

Desnick¹,

Dean²,

Grabowski³

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…Many attempts have been undertaken to replace the defective α-galactosidase activity with normal enzyme. Early studies have demonstrated that α-galactosidase A, purified from plants [15] or human placenta [16], was internalised by skin fibroblasts from Anderson-Fabry patients and was capable of catabolising the accumulated substrate. In a clinical trial, enzyme obtained from human placenta and injected into two Fabry patients was shown to be metabolically active [17].…”

Section: Review Of Agalsidase Alfa 21 Overviewmentioning

confidence: 99%

Agalsidase alfa – a preparation for enzyme replacement therapy in Anderson–Fabry disease

Beck

2002

Expert Opinion on Investigational Drugs

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Anderson-Fabry disease is an X-linked multisystemic disorder caused by a genetic deficiency of the lysosomal enzyme a-galactosidase A. The enzyme is responsible for degradation of glycolipids inside the lysosomes. Lack of catalytic activity leads to progressive depositions of undegraded glycolipids in a large number of organs. Crises of severe pain in the extremities (acroparesthesias), hypohidrosis, corneal opacities and dysfunction of several organs (kidney, brain, heart) are the leading symptoms in patients with Anderson-Fabry disease. Females may have the same symptoms as males but to a more variable degree. The variable manifestations seen in heterozygotes can be explained by the Lyon hypothesis. This hypothesis predicts that in X-linked diseases, the carriers are a mosaic of normal and mutant cells in varying proportions and hence have variable expression. As in Gaucher's disease, enzyme replacement therapy recently became available for Anderson-Fabry disease. Two drugs have gained approval in the EU by the European Agency for the Evaluation of Medicinal Products. These are agalsidase beta (Fabrazyme, Genzyme Corporation) and agalsidase alfa (Replagal, Transkaryotic Therapies, Inc.). This review will describe clinical efficacy, safety and tolerability of agalsidase alfa.

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Correction of the Enzymic Defect in Cultured Fibroblasts from Patients with Fabry's Disease: Treatment with Purified α-Galactosidase from Ficin

Cited by 18 publications

References 23 publications

Expression and Characterization of Glycosylated and Catalytically Active Recombinant Human α-Galactosidase A Produced in Pichia pastoris

Expression and Characterization of Glycosylated and Catalytically Active Recombinant Human α-Galactosidase A Produced in Pichia pastoris

Enzyme therapy in Fabry disease: differential in vivo plasma clearance and metabolic effectiveness of plasma and splenic alpha-galactosidase A isozymes.

Agalsidase alfa – a preparation for enzyme replacement therapy in Anderson–Fabry disease

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