cas72599-27-0 miglustat

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Miglustat is a hydroxypiperidine that is deoxynojirimycin in which the amino hydrogen is replaced by a butyl group. It has a role as an EC 2.4.1.80 (ceramide glucosyltransferase) inhibitor and an anti-HIV agent. It is a member of piperidines and a tertiary amino compound. It derives from a duvoglustat.|Miglustat, commonly marketed under the trade name Zavesca, is a drug used to treat Gaucher disease. It inhibits the enzyme glucosylceramide synthase, an essential enzyme for the synthesis of most glycosphingolipids. It is only used for patients who cannot be treated with enzyme replacement therapy with imiglucerase. Miglustat is now the first and only approved therapy for patients with Niemann-Pick disease type C (NP-C). It has recently been approved for treatment of progressive neurological symptoms in adult and pediatric patients in the European Union, Brazil, and South Korea. Miglustat was first developed as an anti-HIV agent in the 1990s. However, clinical experience with miglustat showed that therapeutic levels of the drug could not be achieved in patients without a high incidence of adverse effect.|Miglustat is a Glucosylceramide Synthase Inhibitor. The mechanism of action of miglustat is as a Glucosylceramide Synthase Inhibitor.|Miglustat is an oral inhibitor of glucosylceramide synthase which is used in the therapy of type 1 Gaucher disease. Clinical experience with miglustat is limited, but it has not been linked to serum enzyme elevations during therapy or to instances of clinically apparent acute liver injury.|Miglustat is a synthetic, N-alkylated imino analogue of D-glucose. Miglustat competitively and reversibly binds to and inhibits the activity of UDP-glucose ceramide glucosyltransferase, which catalyzes the initial step in the synthesis of glycosphingolipids (GSL). This leads to a decrease in the production of glycosphingolipid, which has important roles in various cellular processes. Miglustat can be used in substrate reduction therapy in diseases in which the enzyme glucocerebrosidase, that is responsible for the breakdown of GSL, is deficient.