Abstract
Anandamide and 2-arachidonoylglycerol (2-AG) are two endogenous ligands for the cannabinoid receptors, and their cannabimimetic activities are lost when they are hydrolyzed enzymatically. Cytosol and particulate fractions of porcine brain exhibited a high 2-AG hydrolyzing activity of 100 nmol/min/mg protein. Most of the activity could be attributed to a monoacylglycerol lipase-like enzyme that did not hydrolyze anandamide. It was separated by hydroxyapatite chromatography from anandamide amidohydrolase, which is also capable of hydrolyzing 2-AG as well as anandamide. Thus, porcine brain has at least two enzymes capable of hydrolyzing 2-AG. The 2-AG hydrolase activities of both the cytosolic and particulate enzymes were irreversibly and time-dependently inhibited by methyl arachidonyl fluorophosphonate with ic 50 values as low as 2–3 nM.
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