Nutritional regulation of insulin-like growth factor-I

Metabolism. 1995 Oct;44(10 Suppl 4):50-7. doi: 10.1016/0026-0495(95)90221-x.


Several lines of evidence indicate that in the human, insulin-like growth factor-I (IGF-I) is nutritionally regulated. Both energy and protein availability are required for maintenance of IGF-I. Measurements of serum IGF-I constitute a sensitive means for monitoring the response of acutely ill patients to nutritional intervention. Serum IGF-I may also serve as a marker for evaluation of nutritional status. Our findings and those of others in animal models suggest that nutrients influence synthesis and action of IGF-I and its binding proteins (IGFBPs) at multiple levels. In fasting, liver growth hormone (GH) binding is decreased, providing one explanation for decreased IGF-I. In protein restriction, GH receptors are maintained, but there is evidence for a postreceptor defects. The latter results from pretranslational and translational defects. Amino acid availability to the hepatocytes is essential for IGF-I gene expression. Protein malnutrition not only decreases IGF-I production rate, but also enhances its serum clearance and degradation. Finally, there is evidence for selective organ resistance to the growth-promoting effects of IGF-I in protein-restricted rats.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Dietary Proteins / pharmacology
  • Growth Hormone / metabolism
  • Humans
  • Insulin-Like Growth Factor I / metabolism*
  • Nutrition Disorders / metabolism
  • Nutritional Physiological Phenomena / physiology*
  • Receptors, Somatotropin / metabolism


  • Dietary Proteins
  • Receptors, Somatotropin
  • Insulin-Like Growth Factor I
  • Growth Hormone