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Membrane lipids are key modulators of the endocannabinoid-hydrolase FAAH

Academic Article
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Overview

authors

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

publication date

  • February 2014

journal

  • Biochemical Journal  Journal

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 FAAH (fatty acid amide hydrolase), an enzyme critical in terminating endocannabinoid signalling and an important therapeutic target. In the present study, using a combined experimental and computational approach, we show that membrane lipids modulate the structure, subcellular localization and activity of FAAH. We report that the FAAH dimer is stabilized by the lipid bilayer and shows a higher membrane-binding affinity and enzymatic activity within membranes containing both cholesterol and the natural FAAH substrate AEA (anandamide). Additionally, co-localization of cholesterol, AEA and FAAH in mouse neuroblastoma cells suggests a mechanism through which cholesterol increases the substrate accessibility of FAAH.

subject areas

  • Amidohydrolases
  • Animals
  • Cell Line
  • Cell Membrane
  • Cholesterol
  • Detergents
  • Dimerization
  • Endocannabinoids
  • Endoplasmic Reticulum
  • Enzyme Activation
  • Enzyme Inhibitors
  • Hydrolysis
  • Liver
  • Mice
  • Models, Biological
  • Neurons
  • Peptide Fragments
  • Protein Conformation
  • Protein Stability
  • Protein Transport
  • Rats
  • Recombinant Proteins
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Research

keywords

  • cholesterol
  • endocannabinoid
  • fatty acid amide hydrolase (FAAH)
  • lipid
  • membrane
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Identity

International Standard Serial Number (ISSN)

  • 1470-8728 (Electronic) 0264-6021 (Linking)

Digital Object Identifier (DOI)

  • 10.1042/bj20130960

PubMed ID

  • 24215562
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Additional Document Info

start page

  • 463

end page

  • 472

volume

  • 457

issue

  • 3

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