Species specificity of pharmacological characteristics of CCK-B receptors

Neurosci Lett. 1993 Aug 6;158(1):1-4. doi: 10.1016/0304-3940(93)90597-e.

Abstract

Novel CCK-B receptor antagonists, tetronothiodin and L-156,586, showed different affinities for CCK-B receptors in brain membranes from human, rat, guinea pig and mouse. [125I]CCK-8 bound to these membranes with a similar affinity. However, tetronothiodin was most potent in rat (IC50 = 3.6 nM), followed by guinea pig (96 nM), human (210 nM) and mouse (280 nM). L-156,586 bound with highest affinity to membranes from guinea pig (11 nM), and with lowest affinity to membranes from mouse (220 nM). These results suggest the existence of species specificity of CCK-B receptors, and that these two compounds are useful tools for discrimination between these receptors.

Publication types

  • Comparative Study

MeSH terms

  • Aged
  • Animals
  • Brain Chemistry / drug effects
  • Cholecystokinin / antagonists & inhibitors
  • Cholecystokinin / metabolism*
  • Furans / pharmacology
  • Guanylyl Imidodiphosphate / pharmacology
  • Guinea Pigs
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Membranes / drug effects
  • Membranes / metabolism
  • Mice
  • Pancreas / drug effects
  • Pancreas / metabolism
  • Rats
  • Receptor, Cholecystokinin B
  • Receptors, Cholecystokinin / antagonists & inhibitors
  • Receptors, Cholecystokinin / drug effects*
  • Species Specificity
  • Thiophenes / pharmacology
  • Virginiamycin / analogs & derivatives
  • Virginiamycin / pharmacology

Substances

  • Furans
  • Receptor, Cholecystokinin B
  • Receptors, Cholecystokinin
  • Thiophenes
  • Virginiamycin
  • 15-dihydro-13,14-anhydrovirginiamycin M1
  • tetronothiodin
  • Guanylyl Imidodiphosphate
  • Cholecystokinin