Identification and characterization of specific binding sites for somatostatin in cytosol of bovine cystic duct mucosa.
Specific binding sites for somatostatin have been detected in cytosolic fraction of bovine cystic duct mucosa. At 37 degrees C, the interaction of 125I-Tyr11-somatostatin with cytosolic fraction was rapid, reversible, specific and saturable. At equilibrium, the binding of tracer was competitively inhibited by native peptide in the 1 nM to 2 microM range of concentrations. Scatchard analysis of binding data suggested the presence of two distinct classes of somatostatin binding sites: a class with a high affinity (Kd = 7.8 +/- 0.3 nM) and a low capacity (1.3 +/- 0.3 pmol somatostatin/mg protein) and a class with a low affinity (Kd = 129.1 +/- 2.0 nM) and a high capacity (43.5 +/- 6.7 pmol somatostatin/mg protein). The binding sites were shown to be highly specific for somatostatin since neuropeptides present in cystic duct such as Leu-enkephalin, neurotensin, substance P and vasoactive intestinal peptide did practically not show competition. These findings suggest that somatostatin could contribute to the regulation of the functions of the cystic duct mucosa in physiological and pathological conditions.
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002417:Cattle; D003549:Cystic Duct / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009092:Mucous Membrane / Q000378:metabolism; D013004:Somatostatin / Q000031:analogs & derivatives* / Q000378:metabolism
D013004:Somatostatin; C032367:somatostatin, Tyr(11)-