After association with intact Chinese hamster ovary (CHO) cells expressing the rat neurotensin receptor, tritiated neurotensin was rapidly internalized. Internalization was maximal after 30 min and accounted for about 90% of the total associated ligand. Neurotensin internalization was not observed at 0-4 degrees and was inhibited by an excess of unlabelled neurotensin or by the neurotensin non peptide antagonist, SR 48692. Moreover, the incubation of intact cells for 30 min with 10 nM neurotensin resulted in a significant decrease in the number of the cell surface neurotensin receptors. These results indicate that the endocytosis of membrane bound neurotensin in transfected CHO cells resulted from the internalization of the ligand-receptor complex inside the cell, through an agonist-induced process.