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Endocrinology, Vol 126, 622-630, Copyright © 1990 by Endocrine Society

ARTICLES

Regulation of insulin-like growth factor-I ribonucleic acid expression, polypeptide secretion, and binding protein activity by growth hormone in porcine preadipocyte cultures

HR Gaskins, JW Kim, JT Wright, LA Rund and GJ Hausman
Department of Foods and Nutrition, University of Georgia, Athens 30602.

Insulin-like growth factor-I (IGF-I) is a mitogenic polypeptide postulated to mediate the effect of GH on adipose tissue development. To determine if the effect of GH could be mediated by the local production of IGF-I, we have characterized IGF-I RNA expression, polypeptide secretion, and binding protein activity in primary preadipocyte cultures derived from porcine adipose tissues. GH acutely regulated the abundance of multiple IGF-I RNA transcripts and resulted in a 2-fold increase in secreted immunoreactive IGF-I (iIGF-I) polypeptide in medium conditioned for 48 h by preadipocyte cultures relative to those not receiving GH. Immunocytochemical data indicated that IGF-I is synthesized by presumptive and mature adipocytes. The effect of GH on iIGF-I secretion was observed in cultures derived from both fetal and postnatal animals, while secreted IGF-binding protein activity was increased due to GH only in cultures from fetal animals. The increase in local IGF-I production in response to GH was associated with a decrease in adipocyte development, suggesting that local IGF-I may contribute to suppression of differentiated phenotype.


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