Characterization of High Affinity Receptors for Insulin-Like Growth Factors I and II on Rat Anterior Pituitary Cells*

Abstract

Primary cultures of rat anterior pituitary cells were assessed for the presence of specific receptors for insulin and for the somatomedin peptides, insulin-like growth factors I and II (IGF-I and IGF-II). Specific binding per 100,000 pituitary cells averaged 9.45 .+-. 1.69% (mean .+-. SD) for [125I]IGF-II, 0.83 .+-. 0.06% for [125I]IGF-I and only 0.11% for [125I]insulin. IGF-II was twice as potent as IGF-I in displacing [125I]IGF-II, while insulin was totally nonreactive. IGF-I was 5-fold more potent than IGF-II at displacing [125I]IGF-I and 1000-fold more potent than insulin. Scatchard analysis of [125I]IFG-II binding revealed a curvilinear plot, which could be resolved into a high affinity receptor with a Ka [affinity constant] of 7.0 .times. 108 M-1 and 120,000 receptor sites/cell, and a low affinity receptor with a Ka of 1.1 .times. 108 M-1 and 720,000 receptor sites/cell. The existence of abundant high affinity somatomedin receptors (especially for IGF-II) on rat anterior pituitary cells is consistent with a potential role for these peptides in the regulation of GH [growth hormone] secretion.