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Nutritional Regulation of the Insulin-Like Growth Factors

Nutritional Regulation of the Insulin-Like Growth Factors INSULIN-LIKE growth factor-I (IGF-I) and IGF-II growth factors that are structurally related to insulin (Table 1). The human IGFs (refered to generically as somatomedins) are single chain peptides of 7.5 kilodaltons (kDa), composed of 70 and 67 amino acid residues for IGF-I and IGF-II, respectively (1–3). Four domains, designated A, B, C, and D are identified in the IGF molecules; the A and B domains being homologous with the A and B chains of insulin, respectively. In contrast with most hormonal peptides, the IGFs are secreted as they are produced. Consequently, there are no organs in which IGFs are concentrated. The liver is believed to be the principal source of circulating IGF-I (4–6) but the highest concentrations of IGFs are observed in blood (7). The IGFs are produced in most organs (8, 9) and exert biological effects on most cell types (10, 11). The ubiquity of sites of production and action has led to the concept that these peptides act by autocrine and paracrine mechanisms (12, 13) as well as by classical endocrine mechanisms (14). This content is only available as a PDF. Author notes * This work was supported by National Institutes of Health Grants HD-26871, HD-08299, HD-28081, and AG-02331, by institutional Training Grant DK-07129, and by grants from the Fund for Medical Scientific Research (Belgium) (3.4538.80 and 3.4544.87) and from the National Fund for Scientific Research (Belgium) (1.5.333.86F). † Jean-Paul Thissen is a Senior Research Assistant of the National Fund for Scientific Research (Belgium) and a Recipient of a Fogarty International Research Fellowship (TW-04384) from the National Institutes of Health. Copyright © 1994 by The Endocrine Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Endocrine Reviews Oxford University Press

Nutritional Regulation of the Insulin-Like Growth Factors

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References (239)

Publisher
Oxford University Press
Copyright
Copyright © 1994 by The Endocrine Society
ISSN
0163-769X
eISSN
1945-7189
DOI
10.1210/edrv-15-1-80
Publisher site
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Abstract

INSULIN-LIKE growth factor-I (IGF-I) and IGF-II growth factors that are structurally related to insulin (Table 1). The human IGFs (refered to generically as somatomedins) are single chain peptides of 7.5 kilodaltons (kDa), composed of 70 and 67 amino acid residues for IGF-I and IGF-II, respectively (1–3). Four domains, designated A, B, C, and D are identified in the IGF molecules; the A and B domains being homologous with the A and B chains of insulin, respectively. In contrast with most hormonal peptides, the IGFs are secreted as they are produced. Consequently, there are no organs in which IGFs are concentrated. The liver is believed to be the principal source of circulating IGF-I (4–6) but the highest concentrations of IGFs are observed in blood (7). The IGFs are produced in most organs (8, 9) and exert biological effects on most cell types (10, 11). The ubiquity of sites of production and action has led to the concept that these peptides act by autocrine and paracrine mechanisms (12, 13) as well as by classical endocrine mechanisms (14). This content is only available as a PDF. Author notes * This work was supported by National Institutes of Health Grants HD-26871, HD-08299, HD-28081, and AG-02331, by institutional Training Grant DK-07129, and by grants from the Fund for Medical Scientific Research (Belgium) (3.4538.80 and 3.4544.87) and from the National Fund for Scientific Research (Belgium) (1.5.333.86F). † Jean-Paul Thissen is a Senior Research Assistant of the National Fund for Scientific Research (Belgium) and a Recipient of a Fogarty International Research Fellowship (TW-04384) from the National Institutes of Health. Copyright © 1994 by The Endocrine Society

Journal

Endocrine Reviews – Oxford University Press

Published: Feb 1, 1994

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