Paper Report for: Barricklow_2013_Arch.Biochem.Biophys_536_1
Reference
Title: 2-Arachidonoylglycerol is a substrate for butyrylcholinesterase: A potential mechanism for extracellular endocannabinoid regulation Barricklow J, Blatnik M Ref: Archives of Biochemistry & Biophysics, 536:1, 2013 : PubMed
2-Arachidonoylglycerol (2-AG) is a component of the endocannabinoid receptor pathway and is primarily hydrolyzed by monoacylglycerol lipase (MAGL) in vivo. We found that the non-specific serine esterase, butyrylcholinesterase (BChE), can hydrolyze 2-AG with reasonable affinity and may present a new compensatory mechanism for endocannabinoid regulation. In vitro hydrolysis reactions of 2-AG with equine BChE were analyzed by liquid chromatography tandem mass spectrometry (LC-MS/MS) positive/negative electrospray ionization (ESI+/-) to measure the formation of arachidonic acid (AA) and the loss of 2-AG over time (min). The resulting Michaelis-Menten approximations reveal that BChE has affinity towards 2-AG in phosphate buffer at neutral pH (7.4). The calculated Vmax, Km and kcat were 12.1nmols(-1), 57.5muM, and 0.074s(-1), respectively, which produced a diffusion-controlled rate of association (kcat/Km) of 1.3x10(3)M(-1)s(-1). Human BChE 2-AG hydrolysis was measured by immunoprecipitating BChE from fresh plasma and monitoring 2-AG loss and AA formation over time. These findings show that BChE can hydrolyze 2-AG which may be evidence of a more specific role for BChE in endocannabinoid regulation.
        
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Barricklow J, Blatnik M (2013) 2-Arachidonoylglycerol is a substrate for butyrylcholinesterase: A potential mechanism for extracellular endocannabinoid regulation Archives of Biochemistry & Biophysics536: 1-5
Barricklow J, Blatnik M (2013) Archives of Biochemistry & Biophysics536: 1-5