scholarly journals Design, Synthesis, and In Vitro Evaluation of Carbamate Derivatives of 2-Benzoxazolyl- and 2-Benzothiazolyl-(3-hydroxyphenyl)-methanones as Novel Fatty Acid Amide Hydrolase Inhibitors

2007 ◽  
Vol 50 (17) ◽  
pp. 4236-4242 ◽  
Author(s):  
Mikko J. Myllymäki ◽  
Susanna M. Saario ◽  
Antti O. Kataja ◽  
Joel A. Castillo-Melendez ◽  
Tapio Nevalainen ◽  
...  

2007 ◽  
Vol 50 (23) ◽  
pp. 5868-5868
Author(s):  
Mikko J. Myllymäki ◽  
Susanna M. Saario ◽  
Antti O. Kataja ◽  
Joel A. Castillo-Melendez ◽  
Tapio Nevalainen ◽  
...  


2014 ◽  
Vol 22 (4) ◽  
pp. 1468-1478 ◽  
Author(s):  
Mitsunori Kono ◽  
Takahiro Matsumoto ◽  
Toshihiro Imaeda ◽  
Toru Kawamura ◽  
Shinji Fujimoto ◽  
...  


ChemMedChem ◽  
2016 ◽  
Vol 11 (4) ◽  
pp. 429-443 ◽  
Author(s):  
Tobias Terwege ◽  
Walburga Hanekamp ◽  
David Garzinsky ◽  
Simone König ◽  
Oliver Koch ◽  
...  






2017 ◽  
Vol 815 ◽  
pp. 42-48 ◽  
Author(s):  
Tomonari Watabiki ◽  
Noriko Tsuji ◽  
Tetsuo Kiso ◽  
Tohru Ozawa ◽  
Fumie Narazaki ◽  
...  


2013 ◽  
Vol 720 (1-3) ◽  
pp. 383-390 ◽  
Author(s):  
Mariateresa Cipriano ◽  
Emmelie Björklund ◽  
Alan A. Wilson ◽  
Cenzo Congiu ◽  
Valentina Onnis ◽  
...  


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.



2020 ◽  
Vol 35 (1) ◽  
pp. 815-823 ◽  
Author(s):  
Alessandro Deplano ◽  
Jessica Karlsson ◽  
Mona Svensson ◽  
Federica Moraca ◽  
Bruno Catalanotti ◽  
...  


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