Evagorou_2010_Eur.J.Protistol_46_289

Reference

Title : Hydrolysis of 2-arachidonoylglycerol in Tetrahymena thermophila. Identification and partial characterization of a Monoacylglycerol Lipase-like enzyme - Evagorou_2010_Eur.J.Protistol_46_289
Author(s) : Evagorou A , Anagnostopoulos D , Farmaki E , Siafaka-Kapadai A
Ref : Eur J Protistol , 46 :289 , 2010
Abstract :

Tetrahymena thermophila is a model organism for molecular and cellular biology. Previous studies from our group showed that Tetrahymena contains major components of the endocannabinoid system, such as various endocannabinoids and FAAH. In mammalian cells the endocannabinoid 2-arachidonoylglycerol is inactivated mainly by MAGL. In this study we showed that 2-arachidonoylglycerol and 2-oleoylglycerol are hydrolyzed by the combined actions of MAGL and FAAH. MAGL-like activity was examined in the presence of FAAH specific inhibitors, URB597 or AM374 and showed optimum pH of 8-9, apparent K(M) of 14.1muM and V(max) of 5.8nmol/minxmg. The enzyme was present in membrane bound and cytosolic isoforms; molecular mass was determined at approximately 45 and approximately 40kDa. MAGL and FAAH could also inactivate endogenous signaling lipids, which might play an important role in Tetrahymena as suggested in mammals. Tetrahymena could be used as a model system for testing drugs targeting enzymes of the endocannabinoid system.

PubMedSearch : Evagorou_2010_Eur.J.Protistol_46_289
PubMedID: 20889319

Related information

Inhibitor URB597

Citations formats

Evagorou A, Anagnostopoulos D, Farmaki E, Siafaka-Kapadai A (2010)
Hydrolysis of 2-arachidonoylglycerol in Tetrahymena thermophila. Identification and partial characterization of a Monoacylglycerol Lipase-like enzyme
Eur J Protistol 46 :289

Evagorou A, Anagnostopoulos D, Farmaki E, Siafaka-Kapadai A (2010)
Eur J Protistol 46 :289