Distribution of anandamide amidohydrolase in rat tissues with special reference to small intestine

Biochim Biophys Acta. 1997 Aug 16;1347(2-3):212-8. doi: 10.1016/s0005-2760(97)00078-7.


Anandamide (arachidonylethanolamide), an endogenous ligand for cannabinoid receptors, is hydrolyzed by an amidohydrolase and its biological activity is lost. Previously, we partially purified the enzyme from porcine brain and anandamide synthesis by its reverse reaction was proposed (Ueda et al., (1995) J. Biol. Chem. 270, 23823-23827). The anandamide hydrolase and synthase activities were examined with various rat tissues. Rat liver showed the highest specific activities (4.4 +/- 0.3 and 4.5 +/- 0.5 nmol/min/mg protein) for the hydrolase and synthase, respectively. In most other tissues such as brain, testis and parotid gland, the ratio of synthase/hydrolase activity was 0.7-1.6. However, small intestine showed a relatively high synthase/hydrolase ratio of about 5.0 (1.0 +/- 0.1 and 0.2 +/- 0.1 nmol/min/mg protein). When a homogenate of small intestine was subjected to acetone extraction to remove lipids, a higher hydrolase activity was found (2.0 +/- 0.2 nmol/min/mg protein). Furthermore, Northern blotting detected an intense mRNA band of anandamide hydrolase in small intestine as well as liver and brain. These results demonstrated for the first time a high content of anandamide hydrolase in small intestine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetone
  • Amidohydrolases / metabolism*
  • Animals
  • Arachidonic Acid / metabolism
  • Blotting, Northern
  • Chromatography, Thin Layer
  • Colon / enzymology
  • Intestine, Small / enzymology
  • Kidney / enzymology
  • Liver / enzymology
  • Parotid Gland / enzymology
  • Rats
  • Rats, Wistar
  • Stomach / enzymology


  • Acetone
  • Arachidonic Acid
  • Amidohydrolases
  • arachidonoylethanolamide synthase
  • fatty-acid amide hydrolase