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An IGF binding protein is an inhibitor of fgf stimulation

✍ Scribed by J. Villaudy; J. Delbé; C. Blat; G. Desauty; A. Golde; L. Harel

Publisher
John Wiley and Sons
Year
1991
Tongue
English
Weight
505 KB
Volume
149
Category
Article
ISSN
0021-9541

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✦ Synopsis

Abstract

We purified to homogeneity a growth inhibiting diffusible factor (IDF45) secreted by dense cultures of mouse 3T3 cells and which was able to inhibit 100% of DNA synthesis stimulated by serum in chick embryo fibroblasts (CEF) (Blat et al., 1989a). We then demonstrated that this factor was an IGF‐binding protein (Blat et al., 1989b). Indeed, its N‐terminal amino acid sequence was homologous to that of rat IGFBP‐3. Our present results show that basic fibroblast growth factor (bFGF) induced, respectively, a fivefold and threefold increase in DNA synthesis in mouse embryo fibroblasts (MEF) and CEF. IDF45 inhibited the stimulation induced by bFGF by about 65%, while stimulation induced by insulin, PDGF, or EGF was only weakly or not at all inhibited by IDF45. When bFGF stimulation was determined in the presence of a high concentration of insulin in conditions which minimize the effect of endogenous IGF‐I or ‐II, this stimulation was decreased by about 50% in the presence of IDF45. This result suggests that addition of bFGF stimulates IGF secretion, thereby resulting in partial loss of inhibition, by IDF45, of bFGF stimulation.

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