Role of Fatty Acid Amide Hydrolase in the Transport of the Endogenous Cannabinoid Anandamide

2001 ◽  
Vol 59 (6) ◽  
pp. 1369-1375 ◽  
Author(s):  
Theresa A. Day ◽  
Fariborz Rakhshan ◽  
Dale G. Deutsch ◽  
Eric L. Barker
2021 ◽  
Vol 22 (3) ◽  
pp. 1047
Author(s):  
Dorsa Rafiei ◽  
Nathan J. Kolla

Altered activity of fatty acid amide hydrolase (FAAH), an enzyme of the endocannabinoid system, has been implicated in several neuropsychiatric disorders, including major depressive disorder (MDD). It is speculated that increased brain FAAH expression is correlated with increased depressive symptoms. The aim of this scoping review was to establish the role of FAAH expression in animal models of depression to determine the translational potential of targeting FAAH in clinical studies. A literature search employing multiple databases was performed; all original articles that assessed FAAH expression in animal models of depression were considered. Of the 216 articles that were screened for eligibility, 24 articles met inclusion criteria and were included in this review. Three key findings emerged: (1) FAAH expression is significantly increased in depressive-like phenotypes; (2) genetic knockout or pharmacological inhibition of FAAH effectively reduces depressive-like behavior, with a dose-dependent effect; and (3) differences in FAAH expression in depressive-like phenotypes were largely localized to animal prefrontal cortex, hippocampus and striatum. We conclude, based on the animal literature, that a positive relationship can be established between brain FAAH level and expression of depressive symptoms. In summary, we suggest that FAAH is a tractable target for developing novel pharmacotherapies for MDD.


2017 ◽  
Vol 174 (21) ◽  
pp. 3837-3847 ◽  
Author(s):  
Erin M Rock ◽  
Guillermo Moreno-Sanz ◽  
Cheryl L Limebeer ◽  
Gavin N Petrie ◽  
Roberto Angelini ◽  
...  

2014 ◽  
Vol 24 (9) ◽  
pp. 1511-1523 ◽  
Author(s):  
Gaurav Bedse ◽  
Roberto Colangeli ◽  
Angelo M. Lavecchia ◽  
Adele Romano ◽  
Fabio Altieri ◽  
...  

2008 ◽  
Vol 54 (1) ◽  
pp. 129-140 ◽  
Author(s):  
Maria Scherma ◽  
Julie Medalie ◽  
Walter Fratta ◽  
Subramanian K. Vadivel ◽  
Alexandros Makriyannis ◽  
...  

2019 ◽  
Vol 4 (1) ◽  
pp. 42-50 ◽  
Author(s):  
Annalaura Sabatucci ◽  
Monica Simonetti ◽  
Daniel Tortolani ◽  
Clotilde B. Angelucci ◽  
Enrico Dainese ◽  
...  

Life Sciences ◽  
2013 ◽  
Vol 92 (8-9) ◽  
pp. 458-462 ◽  
Author(s):  
Pretal P. Muldoon ◽  
Aron H. Lichtman ◽  
Loren H. Parsons ◽  
M. Imad Damaj

Author(s):  
Smita Jain ◽  
Akansha Bisht ◽  
Kanika Verma ◽  
Swarnima Negi ◽  
Sarvesh Paliwal ◽  
...  

2004 ◽  
Vol 379 (1) ◽  
pp. 99-106 ◽  
Author(s):  
Kazuhito TSUBOI ◽  
Christine HILLIGSMANN ◽  
Séverine VANDEVOORDE ◽  
Didier M. LAMBERT ◽  
Natsuo UEDA

Anandamide (N-arachidonoylethanolamine) and other bioactive N-acylethanolamines are degraded to their corresponding fatty acids and ethanolamine. This hydrolysis is mostly attributed to catalysis by FAAH (fatty acid amide hydrolase), which exhibits an alkaline pH optimum. In addition, we have identified another amidase which catalyses the same reaction exclusively at acidic pH values [Ueda, Yamanaka and Yamamoto (2001) J. Biol. Chem. 276, 35552–35557]. In attempts to find selective inhibitors of this acid amidase, we screened various derivatives of palmitic acid, 1-hexadecanol, and 1-pentadecylamine with N-palmitoylethanolamine as substrate. Here we show that N-cyclohexanecarbonylpentadecylamine inhibits the acid amidase from rat lung with an IC50 of 4.5 µM, without inhibiting FAAH at concentrations up to 100 µM. The inhibition was reversible and non-competitive. This compound also inhibited the acid amidase in intact alveolar macrophages. With the aid of this inhibitor, it was revealed that rat basophilic leukaemia cells possess the acid amidase as well as FAAH. Thus the inhibitor may be a useful tool to distinguish the acid amidase from FAAH in various tissues and cells and to elucidate the physiological role of the enzyme.


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