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Chemical probes of endocannabinoid metabolism

Academic Article
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Overview

related to degree

  • Blankman, Jacqueline, Ph.D. in Chemistry, Scripps Research 2006 - 2012

authors

  • Blankman, Jacqueline
  • Cravatt, Benjamin

publication date

  • April 2013

journal

  • Pharmacological Reviews  Journal

abstract

  • The endocannabinoid signaling system regulates diverse physiologic processes and has attracted considerable attention as a potential pharmaceutical target for treating diseases, such as pain, anxiety/depression, and metabolic disorders. The principal ligands of the endocannabinoid system are the lipid transmitters N-arachidonoylethanolamine (anandamide) and 2-arachidonoylglycerol (2-AG), which activate the two major cannabinoid receptors, CB1 and CB2. Anandamide and 2-AG signaling pathways in the nervous system are terminated by enzymatic hydrolysis mediated primarily by the serine hydrolases fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL), respectively. In this review, we will discuss the development of FAAH and MAGL inhibitors and their pharmacological application to investigate the function of anandamide and 2-AG signaling pathways in preclinical models of neurobehavioral processes, such as pain, anxiety, and addiction. We will place emphasis on how these studies are beginning to discern the different roles played by anandamide and 2-AG in the nervous system and the resulting implications for advancing endocannabinoid hydrolase inhibitors as next-generation therapeutics.

subject areas

  • Amidohydrolases
  • Animals
  • Arachidonic Acids
  • Depression
  • Disease Models, Animal
  • Endocannabinoids
  • Enzyme Inhibitors
  • Glycerides
  • Humans
  • Ligands
  • Molecular Structure
  • Monoacylglycerol Lipases
  • Pain
  • Polyunsaturated Alkamides
  • Signal Transduction
  • Substance-Related Disorders
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Identity

PubMed Central ID

  • PMC3639726

International Standard Serial Number (ISSN)

  • 0031-6997

Digital Object Identifier (DOI)

  • 10.1124/pr.112.006387

PubMed ID

  • 23512546
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Additional Document Info

start page

  • 849

end page

  • 871

volume

  • 65

issue

  • 2

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