Study summary · research use only
Modulation of hepatic insulin receptors by a human growth hormone fragment (hGH 6-13)
Plain-language summary
Paraphrased from the published abstract below — not a verdict on whether anything works.
In this study using rats and isolated rat hepatocytes and hepatic plasma membranes, researchers examined a synthetic amino-terminal human growth hormone fragment, hGH 6-13 (H2N-Leu-Ser-Arg-Leu-Phe-Asp-Asn-Ala-COOH), for its influence on hepatic insulin receptors. In vivo, hGH 6-13 was associated with increased binding of [125I]iodoinsulin to rat hepatic receptors, with analysis indicating an increase in receptor capacity or number. In vitro experiments with isolated hepatocytes and plasma membranes showed no direct interaction between hGH 6-13 and hepatic insulin receptors, but preincubating hepatocytes with the fragment (10 micrograms/ml) at 37 degrees C for 30 min was associated with significantly enhanced [125I]iodoinsulin binding. The authors discussed this difference in terms of a secondary cellular mediator.
Abstract
A synthetic amino-terminal fragment of human growth hormone (hGH) containing the sequence H2N-Leu-Ser-Arg-Leu-Phe-Asp-Asn-Ala-COOH (hGH 6-13) was shown to increase [125I]iodoinsulin binding to rat hepatic receptors in vivo. Analysis of the binding data indicated an increase in the capacity of the insulin receptors or the number of available receptors. In vitro experiments with isolated hepatocytes and hepatic plasma membranes revealed no direct interaction between the hGH 6-13 and the hepatic insulin receptors. When the isolated hepatocytes were preincubated with the synthetic hGH fragment (10 micrograms/ml) at 37 degrees C for 30 min prior to tests for insulin binding, the binding of [125I]iodoinsulin to the hepatic receptors was significantly enhanced. The variance between the in vivo and in vitro findings was considered in terms of the mechanism of hormonal actions mediated through a secondary cellular mediator.
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