Evidence for phosphatidylinositol anchorage of opioid binding proteins in rat brain

Brain Res. 1990 Dec 24;537(1-2):381-5. doi: 10.1016/0006-8993(90)90391-n.

Abstract

Treatment of rat brain sections and of thalamic and striatal membranes with phosphatidylinositol phospholipase C (PIPLC), an enzyme known to hydrolyse only phosphatidylinositol and its derivatives, significantly alters the specific binding of mu- and delta-opioid ligands on their receptors. These results suggest that some opioid binding proteins are membrane-anchored by a glycosylphosphatidylinositol (GPI) linkage.

MeSH terms

  • Animals
  • Autoradiography
  • Brain Chemistry / physiology*
  • Corpus Striatum / metabolism
  • Enkephalin, D-Penicillamine (2,5)-
  • Enkephalins / metabolism
  • In Vitro Techniques
  • Iodine Radioisotopes
  • Membranes / metabolism
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphatidylinositols / metabolism*
  • Phosphoric Diester Hydrolases
  • Protein Binding / physiology
  • Rats
  • Receptors, Opioid / metabolism*
  • Thalamus / metabolism
  • beta-Endorphin / metabolism

Substances

  • Enkephalins
  • Iodine Radioisotopes
  • Phosphatidylinositols
  • Receptors, Opioid
  • beta-Endorphin
  • Enkephalin, D-Penicillamine (2,5)-
  • Phosphoric Diester Hydrolases
  • Phosphatidylinositol Diacylglycerol-Lyase