Insulin receptor activity and insulin sensitivity in mammary gland of lactating rats.

The mammary gland is a tissue that is extremely sensitive to insulin during lactation; during weaning, the effect of insulin is rapidly abolished. The purpose of this study was to characterize the mammary gland insulin receptors and their kinase activity in lactating and weaned mammary gland. The apparent molecular weight of the alpha-subunit was slightly lower in the mammary gland than in liver and white adipose tissue (127,000 vs. 134,000), but the apparent molecular weight of the beta-subunit was similar in the three tissues (95,000). Insulin induced a 10-fold increase in beta-subunit autophosphorylation, and the half-maximal effect was achieved at 2 nM insulin. After 24 h of weaning, the number of insulin receptors was decreased by 30%, but the kinase activity of the beta-subunit was unchanged. During the euglycemic hyperinsulinemic clamp, insulin entirely activated pyruvate dehydrogenase in lactating rat mammary gland, whereas after 24 h of weaning it was unable to increase the proportion of the enzyme in the active form. These results suggest that the site of alteration in the action of insulin on the mammary gland during weaning is distal to the receptor.