Appearance of insulin and insulin-like growth factor-I (IGF-I) receptors throughout the ontogeny of brown trout (Salmo trutta fario).

Insulin and IGF-I receptors were characterized in glycoprotein fractions prepared by affinity chromatography from different developmental stages of brown trout. The specificity of insulin and IGF-I binding was demonstrated by crossed-competition assays: unlabelled insulin displaced bound radiolabelled insulin at concentrations 45-fold lower than unlabelled IGF-I, whilst unlabelled IGF-I displaced bound radiolabelled IGF-I at concentrations 2,000-fold lower than unlabelled insulin. The affinity of these receptors did not change significantly during trout development. Insulin-specific binding was detectable 3 weeks after spawning, after which it increased to a maximum in fry weighing 0.4 g, and decreased progressively to adult levels. IGF-I specific binding was detectable in newly laid eggs and increased to a maximum during organogenesis in eyed eggs. It then decreased progressively during subsequent stages of development to adult levels. The apparent molecular weight (Mr) of the alpha-subunit of brown trout insulin and IGF-I receptors was smaller than that of the alpha-subunit of the rat insulin receptor. Receptor tyrosine kinase activity was stimulated in a dose-dependent manner by insulin and IGF-I. Insulin and IGF-I stimulated tyrosine kinase activity and reached a maximum of 201 +/- 17.6 and 240 +/- 29.6% of basal phosphorylation, respectively.