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Inhibition of myocardial lipoprotein lipase by U‐57,908 (RHC 80267)
Author(s) -
Carroll Rogayah,
Severson David L.
Publication year - 1992
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02536481
Subject(s) - triolein , lipoprotein lipase , clinical chemistry , chemistry , lipidology , activator (genetics) , enzyme , lipase , substrate (aquarium) , biochemistry , endocrinology , medicine , biology , ecology , gene
Abstract U‐57,908 (RHC 80267) was shown to inhibit lipoprotein lipase (LPL) activity in cardiac myocytes from rat hearts; the concentrations required for inhibition to 50% of control activity were 1.1 μM and 2.5 μM for myocyte homogenates and a post‐heparin medium preparation, respectively. The inhibition of LPL activity by U‐57,908 was not changed when the concentration of the triolein substrate and apolipoprotein CII activator in the assay was reduced. The availability of U‐57,908 as a potent and selective LPL inhibitor may provide a useful experimental approach in studies on lipoprotein metabolism.