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A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol

Academic Article
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Overview

related to degree

  • Blankman, Jacqueline, Ph.D. in Chemistry, Scripps Research 2006 - 2012
  • Simon, Gabriel, Ph.D. in Chemistry, Scripps Research 2004 - 2009

authors

  • Blankman, Jacqueline
  • Simon, Gabriel
  • Cravatt, Benjamin

publication date

  • December 2007

journal

  • Chemistry & Biology  Journal

abstract

  • Endogenous ligands for cannabinoid receptors ("endocannabinoids") include the lipid transmitters anandamide and 2-arachidonoylglycerol (2-AG). Endocannabinoids modulate a diverse set of physiological processes and are tightly regulated by enzymatic biosynthesis and degradation. Termination of anandamide signaling by fatty acid amide hydrolase (FAAH) is well characterized, but less is known about the inactivation of 2-AG, which can be hydrolyzed by multiple enzymes in vitro, including FAAH and monoacylglycerol lipase (MAGL). Here, we have taken a functional proteomic approach to comprehensively map 2-AG hydrolases in the mouse brain. Our data reveal that approximately 85% of brain 2-AG hydrolase activity can be ascribed to MAGL, and that the remaining 15% is mostly catalyzed by two uncharacterized enzymes, ABHD6 and ABHD12. Interestingly, MAGL, ABHD6, and ABHD12 display distinct subcellular distributions, suggesting that they may control different pools of 2-AG in the nervous system.

subject areas

  • Animals
  • Arachidonic Acids
  • Benzamides
  • Biotin
  • Brain
  • COS Cells
  • Carbamates
  • Catalysis
  • Cercopithecus aethiops
  • Endocannabinoids
  • Enzyme Inhibitors
  • Glycerides
  • Hydrolases
  • Lactones
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Monoacylglycerol Lipases
  • Organophosphorus Compounds
  • Proteomics
  • Subcellular Fractions
  • Transfection
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Identity

PubMed Central ID

  • PMC2692834

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/j.chembiol.2007.11.006

PubMed ID

  • 18096503
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Additional Document Info

start page

  • 1347

end page

  • 1356

volume

  • 14

issue

  • 12

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