Demonstration of a putative receptor site for cholecystokinin in rat brain

Sally E. Hays, Margery C. Beinfeld, Robert T. Jensen, Frederick K. Goodwin, Steven M. Paul

Research output: Contribution to journalArticlepeer-review

158 Scopus citations


High affinity (apparent Kd {reversed tilde equals} 0.65 nM) and saturable (Bmax {reversed tilde equals} 6.6 fmoles/mg protein) binding sites for cholecystokinin (CCK) have been demonstrated in crude synaptosomal membranes from rat cerebral cortex. Scatchard analysis of the equilibrium binding data indicates a single population of non-interacting sites. The specific binding of 125I-CCK33 to brain membranes is reversible (t 1 2 {reversed tilde equals} 6 minutes), and can be inhibited by structurally related CCK analogues but not by unrelated neuropeptides or drugs. Specific CCK binding reaches equilibrium at a temperature-dependent rate, and is abolished when membranes are pre-treated with heat. Kinetic and competition studies suggest that these high affinity binding sites represent physiologically-relevant receptors for CCK in brain.

Original languageEnglish
Pages (from-to)53-62
Number of pages10
Issue number1
StatePublished - Jul 1980


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