http://www.cnr.it/ontology/cnr/individuo/prodotto/ID270195

Membrane lipids are key-modulators of the endocannabinoid-hydrolase FAAH (Articolo in rivista)

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Membrane lipids are key-modulators of the endocannabinoid-hydrolase FAAH (Articolo in rivista) (literal)

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Alternative label

Dainese, E.;De Fabritiis, G.;Sabatucci, A.;Oddi, S.;Angelucci, C.A.;Di Pancrazio, C.;Giorgino, T.;Stanley, N.;Del Carlo, M.;Cravatt, B.;Maccarrone, M. (2013)
Membrane lipids are key-modulators of the endocannabinoid-hydrolase FAAH
in Biochemical journal (Online)
(literal)

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Dainese, E.;De Fabritiis, G.;Sabatucci, A.;Oddi, S.;Angelucci, C.A.;Di Pancrazio, C.;Giorgino, T.;Stanley, N.;Del Carlo, M.;Cravatt, B.;Maccarrone, M. (literal)

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1: Faculty of Bioscience, and Technology for Food Agriculture and Environment, University of Teramo, Teramo, Italy / European Center for Brain Research (CERC)/Santa Lucia Foundation, Rome, Italy; 2,8: Computational biochemistry and biophysics laboratory, (GRIB-IMIM), University of Pompeu Fabra, Barcelona Biomedical Research Park (PRBB), Barcelona, Spain; 3, 6, 9: Faculty of Bioscience, and Technology for Food Agriculture and Environment, University of Teramo, Teramo, Italy; 4: Faculty of Veterinary Medicine, University of Teramo, Italy / European Center for Brain Research (CERC)/Santa Lucia Foundation, Rome, Italy; 5: Faculty of Veterinary Medicine, University of Teramo, Italy; 7: Institute of Biomedical Engineering, National Research Council of Italy (ISIB-CNR), Padua, Italy; 10: Departments of Cell Biology and Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California; 11: Center of Integrated Research, Campus Bio-Medico University of Rome, Rome, Italy (literal)

Titolo

Membrane lipids are key-modulators of the endocannabinoid-hydrolase FAAH (literal)

Abstract

Lipid composition is expected to play an important role in modulating membrane enzyme activity, in particular if the substrates are themselves lipid molecules. A paradigmatic case is fatty acid amide hydrolase (FAAH), a critical enzyme in terminating the endocannabinoid signalling and an important therapeutic target. Here, using a combined experimental and computational approach, we show that membrane lipids modulate structure, subcellular localization and activity of FAAH. We report that FAAH dimer is stabilized by the lipid bilayer and shows higher membrane binding affinity and enzymatic activity within membranes containing both cholesterol and the natural FAAH substrate, anandamide (AEA). Additionally, colocalization of cholesterol, AEA, and FAAH in mouse neuroblastoma cells suggests a mechanism through which cholesterol increases the substrate accessibility of FAAH. (literal)

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