To investigate a possible action of insulin on the rat kidney papilla,
the binding of I-125-insulin to papilla microsomes was examined. This
binding was specific to insulin in that it was displaced by increasin
g concentrations of unlabelled porcine insulin and to a lesser extent
by porcine proinsulin and IGF-I, but not by IGF-II and bGH. Scatchard
plot of the binding data was curvilinear consistent with either two cl
asses of receptors with different affinities or a single class of rece
ptors that showed negative cooperativity. A small fraction of I-125-in
sulin (maximum 2 %) was degraded during incubation, but with a Km two
order of magnitude higher than the constant of affinity for binding. I
nsulin stimulates the incorporation of phosphate to phosphatidylcholin
e in a dose-dependent manner, reaching a maximum with 10 nM insulin. T
his data showed both the presence of specific insulin receptors in the
kidney papilla and an insulin action through the synthesis of phospho
lipids by insulin.