Interaction of gastric inhibitory polypeptide (GIP) with the insulin-secreting pancreatic beta cell line, In lll: characteristics of GIP binding sites.

The interaction of GIP with its receptors in the hamster pancreatic insulin-secreting beta cell line, In lll, has been analyzed. 125I-labelled GIP used as tracer showed the same affinity as native GIP for the GIP binding sites. Binding of the tracer was time, temperature and cell concentration dependent. It was saturable, reversible and highly specific. Under equilibrium conditions, i.e. 2 hours at 13 degrees C, 20% and 25% of the tracer and of GIP binding sites were inactivated, respectively. Native GIP inhibited binding of 125I-labelled GIP in a dose-dependent manner, saturation of the GIP binding sites being obtained at 3. 10(-7) M peptide. Two types of GIP binding sites were found by Scatchard analysis, a small population with a high affinity for GIP (KD = 7 nM) and a large population with a low affinity (KD = 800 nM). The biphasic dissociation process confirmed the GIP binding sites heterogeneity. Apart from GIP, no peptide tested influenced the binding of the 125I-labelled GIP. The present data represents the first analysis of functionally relevant GIP binding sites in a insulin-secreting cell.