Author:
Armstrong John McD.,Bornstein Joseph,Bromley Janet O.,Macaulay S. Lance,Ng Frank M.
Abstract
Abstract.
The insulin-like effects of human growth hormone and the synthetic part sequence, Nα-acetyl-hGH 7–13, on glycogen synthase and phosphorylase have been compared in an in vivo system using 16–18-day-old rats. Both the hormone and its part sequences had similar effects, increasing muscle glycogen synthase a activity and decreasing liver phosphorylase a activity, without affecting phosphorylase activity in muscle or synthase activity in liver. Insulin had similar effects, but also increased liver synthase a activity. The effects of all three substances could be abolished by prior treatment of the animals with anti-insulin serum, showing that the effects of growth hormone and its part sequences were insulin-dependent. Both growth hormone and the synthetic peptide increased the binding of insulin to liver plasma membrane. It is concluded that the insulin-like activity of human growth hormone is associated with a region containing residues 7 to 13 of the hormone molecule, and that this activity is insulin-dependent. It is suggested that both growth hormone and the synthetic peptide produce insulin-like activity by enhancing the binding of circulating insulin to its receptor.
Subject
Endocrinology,General Medicine,Endocrinology, Diabetes and Metabolism
Cited by
12 articles.
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