Comprehensive Physiology Wiley Online Library

The Regulation of Amino Acid and Protein Metabolism by Growth Hormone

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 In Vitro Actions of Growth Hormone and Insulin‐Like Growth Factor I on Protein Metabolism
1.1 Effects of Growth Hormone In Vitro
1.2 Effects of Insulin‐Like Growth Factor I In Vitro
1.3 In Vitro Actions of Growth Hormone and Insulin‐Like Growth Factor I on Protein Degradation
2 In vivo Actions of Growth Hormone and Insulin‐Like Growth Factor I on Protein Metabolism
2.1 Effects of Growth Hormone In Vivo
2.2 Effects of Insulin‐Like Growth Factor I In Vivo
3 Comparison of the Actions of Growth Hormone, Insulin‐Like Growth Factor I, and Insulin on Protein Metabolism in vivo
4 Interactions of Growth Hormone with Gonadal Steroids
5 Growth Hormone and Insulin‐Like Growth Factor I as Therapy in Catabolic States
6 Summary
Figure 1. Figure 1.

Comparison of the effects of growth hormone (GH), insulin‐like growth factor I (IGF‐I), and insulin on forearm muscle phenylalanine balance (Phe Bal), protein synthesis (Phe Uptake), and protein degradation (Phe Release). Each bar indicates the change in the respective outcome measure caused by each hormone. All three hormones are anabolic (a positive shift in Phe Bal). GH causes net anabolism, however, through increasing protein synthesis. Insulin, in contrast, promotes anabolism by decreasing degradation. IGF‐I exerts both actions, which appear to be dose dependent 72.

Figure 2. Figure 2.

Integrative view of muscle protein anabolism. Overall, muscle protein anabolism is a balance of the individual effects on protein synthesis and degradation. Whereas insulin acts primarily to suppress protein degradation, growth hormone (GH) stimulates protein synthesis. Testosterone may stimulate synthesis directly or via altering muscle sensitivity to GH. Insulin‐like growth factor‐I (IGF‐I) is synthesized in a paracrine mode in muscle under the regulation of GH, which may in turn act back on muscle to stimulate synthesis and suppress protein degradation.



Figure 1.

Comparison of the effects of growth hormone (GH), insulin‐like growth factor I (IGF‐I), and insulin on forearm muscle phenylalanine balance (Phe Bal), protein synthesis (Phe Uptake), and protein degradation (Phe Release). Each bar indicates the change in the respective outcome measure caused by each hormone. All three hormones are anabolic (a positive shift in Phe Bal). GH causes net anabolism, however, through increasing protein synthesis. Insulin, in contrast, promotes anabolism by decreasing degradation. IGF‐I exerts both actions, which appear to be dose dependent 72.



Figure 2.

Integrative view of muscle protein anabolism. Overall, muscle protein anabolism is a balance of the individual effects on protein synthesis and degradation. Whereas insulin acts primarily to suppress protein degradation, growth hormone (GH) stimulates protein synthesis. Testosterone may stimulate synthesis directly or via altering muscle sensitivity to GH. Insulin‐like growth factor‐I (IGF‐I) is synthesized in a paracrine mode in muscle under the regulation of GH, which may in turn act back on muscle to stimulate synthesis and suppress protein degradation.

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David A. Fryburg, Eugene J. Barrett. The Regulation of Amino Acid and Protein Metabolism by Growth Hormone. Compr Physiol 2011, Supplement 24: Handbook of Physiology, The Endocrine System, Hormonal Control of Growth: 515-536. First published in print 1999. doi: 10.1002/cphy.cp070517