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Gaucher disease is caused by the defective catabolism of the simple glycosphingolipid, glucosylceramide (GlcCer), due to mutations in the GBA1 gene which encodes for acid β-glucosidase (GCase), the lysosomal enzyme that degrades GlcCer. Today, Gaucher disease patients are routinely treated with recombinant GCase, in a treatment regimen known as enzyme replacement therapy (ERT). We now review the biochemical basis of ERT and discuss how this treatment has advanced since it was first pioneered by Dr. Roscoe Brady in the 1960s. We will place particular emphasis on the three dimensional structure of GCase, and subsequently discuss a relatively new treatment paradigm, substrate reduction therapy (SRT), in which GlcCer synthesis is partially inhibited, thus reducing its accumulation. Both of these approaches are based on studies and concepts developed by Dr. Brady over his remarkable research career spanning six decades.

Original publication

DOI

10.1016/j.ymgme.2016.11.390

Type

Journal article

Journal

Mol Genet Metab

Publication Date

01/2017

Volume

120

Pages

22 - 26

Keywords

Enzyme replacement therapy, Gaucher disease, Glucosylceramide, Substrate reduction therapy, Enzyme Replacement Therapy, Gaucher Disease, Glucosylceramidase, Glucosylceramides, History, 20th Century, History, 21st Century, Humans, Mutation, Protein Structure, Tertiary