Insulin-like growth factor receptors in rat placental membranes.

The nature and relative quantity of insulin-like growth factor (IGF) receptors in rat placental microsomal membranes was investigated by competitive binding studies and covalent cross-linking followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Binding studies revealed that 100 micrograms membrane protein specifically bound 26.5% of [125I]iodo-IGF-II, 19.6% of [125I]iodomultiplication-stimulating activity III-2 [( 125I]iodo-MSA-III-2), and 11.5% [125I]iodo-IGF-I. IGF-II was equipotent with MSA-III-2, and both were approximately twice as potent as IGF-I in competing with [125I]iodo-IGF-I for binding. In contrast, IGF-I competed for the binding of [125I]iodo-MSA and [125I]iodo-IGF-II with only 5-20% the potency of unlabeled MSA and IGF-II. Insulin competed weakly with [125I] iodo-IGF-I for binding (achieving half-maximal displacement at 20 micrograms/ml), but did not compete with [125I]iodo-MSA for binding. This evidence suggested that while IGF-I binds to both IGF-I and IGF-II receptors, the majority of IGF-I binding is due to an interaction with IGF-II receptors. Studies using [125I]iodo-IGF-I covalently cross-linked to placental membrane receptors followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis confirmed that molecular species characteristic of the subunits of IGF-I receptors are present in rat placenta. It is concluded that rat placenta, like human placenta, contains receptors for both types of IGFs. Unlike human placenta, the majority of the receptors are of the IGF-II type.