Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system

Academic Article
uri icon
  • Overview
  • Research
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Thomas, Elizabeth
  • Cravatt, Benjamin
  • Danielson, P. E.
  • Gilula, N. B.
  • Sutcliffe, J. Gregor

publication date

  • December 1997

journal

  • Journal of Neuroscience Research  Journal

abstract

  • Fatty acid amide hydrolase (FAAH) is a membrane-bound enzyme activity that degrades neuromodulatory fatty acid amides, including oleamide and anandamide. A single 2.5-kb FAAH mRNA is distributed throughout the rat CNS and accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as measured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocortex, hippocampal formation, amygdala, and cerebellum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia.

subject areas

  • Amidohydrolases
  • Animals
  • Arachidonic Acids
  • Blotting, Northern
  • Central Nervous System
  • Endocannabinoids
  • In Situ Hybridization
  • Male
  • Neurons
  • Oleic Acids
  • Polyunsaturated Alkamides
  • RNA, Messenger
  • Rats
  • Rats, Sprague-Dawley
scroll to property group menus

Research

keywords

  • CNS
  • in situ hybridization
  • oleamide
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0360-4012

Digital Object Identifier (DOI)

  • 10.1002/(sici)1097-4547(19971215)50:6<1047::aid-jnr16>3.0.co;2-1

PubMed ID

  • 9452020
scroll to property group menus

Additional Document Info

start page

  • 1047

end page

  • 1052

volume

  • 50

issue

  • 6

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support