| Literature DB >> 16931330 |
Susanna M Saario1, Ville Palomäki, Marko Lehtonen, Tapio Nevalainen, Tomi Järvinen, Jarmo T Laitinen.
Abstract
Previous studies indicate that in brain tissue the endocannabinoid 2-AG is inactivated by monoglyceride lipase (MGL)-catalyzed hydrolysis, and a recent report has indicated that MGL activity could be specifically inhibited by URB754 . In the present study, URB754 failed to inhibit 2-AG hydrolysis in rat brain preparations. In addition, brain cryosections were employed to assess whether URB754 could facilitate the detection of 2-AG-stimulated G protein activity. Nevertheless, whereas pretreatment with PMSF readily allowed detection of 2-AG-stimulated G protein activity, URB754 was ineffective. In contrast to previous claims, brain FAAH activity was also resistant to URB754. Thus, in our hands URB754 was not able to block the endocannabinoid-hydrolyzing enzymes and cannot serve as a lead structure for future development of MGL-specific inhibitors.Entities:
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Year: 2006 PMID： 16931330 DOI： 10.1016/j.chembiol.2006.07.008
Source DB: PubMed Journal: Chem Biol ISSN： 1074-5521