Binding of 125I-insulin to the human histiocytic lymphoma cell line U-937: effect of differentiation with retinoic acid.

The human histiocytic lymphoma line U-937 consists of cells having characters of immature monocytes. We have demonstrated that these cells possess highly specific insulin receptors with binding properties similar to that found for mature human blood monocytes. 125I-insulin binding increased progressively with time to reach a maximum at 90 min at 22 degrees C and was proportional to the number of cells in the incubation medium. Insulin degradation as assessed by TCA precipitation was negligible. Scatchard analysis of the binding data was curvilinear and the total number of insulin binding sites was around 13,500. The average affinity profile gave an 'unoccupied site' affinity constant of 1.34 nM-1. When the U-937 cells were induced to differentiate into morphologically and functionally monocyte-like cells, after incubation with retinoic acid, the total number of binding sites decreased significantly with no change in the affinity of the hormone for its receptor.