Characterization of somatostatin binding sites in isolated rat adipocytes.

Somatostatin binding sites were characterized in isolated rat adipocytes. The binding was found to be saturable, reversible, and time- and temperature-dependent. The somatostatin binding sites are principally located on the cell surface. 125I-[Tyr11]somatostatin binding was not inhibited by glucagon and angiotensin II. By contrast, native somatostatin and somatostatin-28 displaced labeled peptide with a similar ED50: 50 nM. Scatchard analysis pointed to the existence of two classes of binding sites, with a Kd of 7.64 nM for the high-affinity sites and a Kd of 295 nM for the low-affinity ones. Comparison of somatostatin receptor binding and its lipolytic action in isolated rat adipocytes suggested that the spare receptor phenomenon cannot be applied to the lipolytic action of somatostatin in rat adipose tissue.