| Literature DB >> 26790472 |
Chizu Aso1, Mari Araki2, Noriyasu Ohshima3, Kazuaki Tatei2, Tohko Hirano2, Hideru Obinata2, Mikiko Kishi2, Koji Kishimoto2, Akimitsu Konishi2, Fumio Goto4, Hiroyuki Sugimoto5, Takashi Izumi6.
Abstract
Diacylglycerol (DG) lipase, which hydrolyses 1-stearoyl-2-arachidonyl-sn-glycerol to produce an endocannabinoid, 2-arachidonoylglycerol, was purified from the soluble fraction of rat brain lysates. DG lipase was purified about 1,200-fold by a sequential column chromatographic procedure. Among proteins identified by mass spectrometry analysis in the partially purified DG lipase sample, only DDHD domain containing two (DDHD2), which was formerly regarded as a phospholipase A1, exhibited significant DG lipase activity. Rat DDHD2 expressed in Chinese hamster ovary cells showed similar enzymatic properties to partially purified DG lipase from rat brain. The source of DG lipase activity in rat brain was immunoprecipitated using anti-DDHD2 antibody. Thus, we concluded that the DG lipase activity in the soluble fraction of rat brain is derived from DDHD2. DDHD2 is distributed widely in the rat brain. Immunohistochemical analysis revealed that DDHD2 is expressed in hippocampal neurons, but not in glia.Entities:
Keywords: 2-arachidonoylglycerol; diacylglycerol; endocannabinoid; lipase; phospholipase
Mesh：
Substances：
Year: 2016 PMID： 26790472 PMCID： PMC4892392 DOI： 10.1093/jb/mvw002
Source DB: PubMed Journal: J Biochem ISSN： 0021-924X Impact factor: 3.387