- Development of small-molecule inhibitors targeting adipose triglyceride lipase.
Development of small-molecule inhibitors targeting adipose triglyceride lipase.
Nature chemical biology (2013-10-08)
Nicole Mayer, Martina Schweiger, Matthias Romauch, Gernot F Grabner, Thomas O Eichmann, Elisabeth Fuchs, Jakov Ivkovic, Christoph Heier, Irina Mrak, Achim Lass, Gerald Höfler, Christian Fledelius, Rudolf Zechner, Robert Zimmermann, Rolf Breinbauer
PMID24096302
RESUMEN
Adipose triglyceride lipase (ATGL) is rate limiting in the mobilization of fatty acids from cellular triglyceride stores. This central role in lipolysis marks ATGL as an interesting pharmacological target as deregulated fatty acid metabolism is closely linked to dyslipidemic and metabolic disorders. Here we report on the development and characterization of a small-molecule inhibitor of ATGL. Atglistatin is selective for ATGL and reduces fatty acid mobilization in vitro and in vivo.
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Esterase from porcine liver, ammonium sulfate suspension, ≥150 units/mg protein (biuret)
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Carboxylesterase 2 human, recombinant, expressed in baculovirus infected BTI insect cells
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Carboxylesterase 1 isoform b human, recombinant, expressed in baculovirus infected BTI insect cells
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Esterase from Bacillus stearothermophilus, recombinant, expressed in E. coli, ≥4.0 U/mg
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Carboxylesterase 2 human, recombinant, expressed in mouse NSO cells, ≥95% (SDS-PAGE)
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Carboxylesterase 1 isoform c human, recombinant, expressed in baculovirus infected BTI insect cells
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Esterase Isoenzyme 1 porcine liver, recombinant, recombinant, expressed in E. coli, ≥30.0 U/g