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The characteristics of cholecystokinin (CCK) receptors in rat pancreatic acini and in various regions of the brain were examined using synthetic CCK-8 or CCK-7 analogues. 3H-propionylated CCK-8 [( 3H]CCK-8) was used as a ligand. 1) The pancreatic CCK receptor had a single high affinity binding component with a dissociation constant, Kd, of 0.76 nM and a maximum number of specific binding sites, Bmax, of 271.91 fmol/mg protein. On the other hand, the CCK receptor in the cerebral cortex had a Kd of 1.66 nM and a Bmax of 30.15 fmol/mg protein. 2) The order of the potencies of CCK-7 and CCK-8 analogues with a substitution at position 3 or 4 to displace [3H]CCK-8 specific binding to the pancreatic acini was as follows: CCK-8 greater than CCK-7 = SucCCK-7 greater than Suc[Sar3]CCK-7 greater than Suc[D-Trp3]CCK-7 greater than Suc[D-Ala3]CCK-7 greater than [D-Trp4]CCK-8 = [D-Ala4] CCK-8. This order of potencies of CCK analogues was greatly different from that in the cerebral cortex. 3) The carboxy-terminal tetra-peptide (CCK-4) and penta-peptide (CCK-5) had very weak potencies in displacing [3H]CCK-8 binding in the pancreatic acini, which were 20 to 30-fold less than their potencies in the cerebral cortex. These results suggest that the recognition sites for CCK analogues in the pancreatic and brain CCK receptors are different.

Comparison of CCK-8 receptors in the pancreas and brain of rats using CCK-8 analogues.