|Human, Mouse, Rat|
Application Methods: Immunoprecipitation, Western Blotting
Background: Diacylglycerol (DAG) lipases comprise two enzymes called DAG lipase α and β, which are the products of two related genes (1). DAG lipases are transmembrane proteins composed of a short amino-terminal intracellular domain, four transmembrane domains, and a large carboxy-terminal cytoplasmic domain containing the active site. These enzymes are responsible for the biosynthesis of 2-acylglycerol from diacylglycerol in a calcium-dependent manner (1). One of the major endocannabinoid ligands that activate cannabinoid receptors, 2-arachidonyl glycerol (2-AG), is produced by DAG lipases (2). Research studies suggest that DAG lipase α is the isoform primarily responsible for the central production of 2-AG (3). DAG lipase β has been implicated in studies of 2-AG production at the periphery in specific cell types and pathophysiological contexts, such as in hepatic stellate cells during alcohol induced fatty liver (4).
Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting
Background: HSL (hormone-sensitive lipase) catalyzes the hydrolysis of triacylglycerol, the rate-limiting step in lipolysis. Lipolytic stimuli activate adenylyl cyclase and thus increase intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA phosphorylates HSL at Ser563, Ser659, and Ser660, which stimulates HSL activity (1,2). In contrast, AMPK phosphorylates HSL at Ser565, which reduces HSL phosphorylation at Ser563 by PKA and inhibits HSL activity (2,3). Recent work indicates that phosphorylation at Ser600 by p44/42 MAPKs also enhances the enzymatic activity of HSL (4).