Cholecystokinin in vivo reduces binding to rat hypothalamic beta-adrenergic sites |
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Authors: | R L Kochman T R Grey J D Hirsch |
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Affiliation: | Department of Biological Research, G. D. Searle and Co., 4901 Searle Parkway, Skokie, IL 60077, USA |
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Abstract: | Intraperitoneal injection of sulfated cholecystokinin octapeptide (CCK-8; 10 micrograms/kg) resulted in an increase in the IC50 for isoproterenol (4.2 microM to 23.3 microM) in displacing 1 nM 3H-dihydroalprenolol binding to rat hypothalamic membranes. 3H-p-Aminoclonidine binding was also lower in membranes prepared from CCK-treated rats, but the decrease was not statistically significant. In vitro, CCK(1-100 nM) had no effect on either alpha- or beta-adrenergic binding or on the 5'-guanylylimidodiphosphate modulation of binding. The results indicate that CCK does not act directly upon adrenergic receptors, but may reduce beta-adrenergic affinity through indirect means. |
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Keywords: | Cholecystokinin Hypothalamus Adrenergic receptor Isoproterenol p-Aminoclonidine Dihydroalprenolol |
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