The effect of insulin-like growth factors (IGF 1 and IGF 2) on insulin degradation was studied with the use of a preparation of insulin protease from rat skeletal muscle. Insulin, IGF 1 and IGF 2 inhibited 125I-insulin degradation by this enzyme. IGF 2 was the most potent inhibitor and IGF 1 was the least potent. These results are similar to what has been reported previously for the insulin-degrading activity in the serum of a diabetic patient who was resistant to sc and im insulin. Insulin protease also degraded 125I-iodo IGF 1 and 125I-iodo IGF 2. 125I-iodo IGF 2 was degraded more rapidly than was 125I-iodo IGF 1. 125I-iodoinsulin was degraded more rapidly than 125I-iodo IGF 2. With all three peptides, immunoprecipitation was a more sensitive measure of degradation than was trichloroacetic acid precipitation. The results suggest that insulin protease may be responsible for the degradation of insulin-like growth factors as well as of insulin.
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http://dx.doi.org/10.1210/endo-113-4-1525 | DOI Listing |
Biol Reprod
November 1998
Department of Physiology, University of Turku, FIN-20520 Turku, Finland.
It is postulated that insulin-like growth factor-I (IGF-I), a 70-amino acid mitogenic polypeptide, regulates Leydig cell steroidogenesis. In the present study, we assessed the effect of IGF-I on LH receptor (LHR) gene expression in an immortalized murine Leydig tumor cell line (BLT-1). Culture of BLT-1 cells in the presence of IGF-I (0.
View Article and Find Full Text PDFEndocrinology
August 1993
Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville 22908.
The present studies were designed to investigate the nature of the actions of insulin-like growth factor-II (IGF-II) on granulosa cell steroidogenesis and assess the potential facilitative interactions between IGF-II and other major regulators of ovarian sterol metabolism, viz. estrogen, FSH, and low density lipoprotein (LDL). In serum-free first passage monolayer cultures of swine granulosa cells, human recombinant IGF-II stimulated progesterone production with a half-maximally effective concentration of 4.
View Article and Find Full Text PDFEndocrinology
August 1988
Department of Obstetrics and Gynecology, Helsinki University Central Hospital, Finland.
Epidermal growth factor (EGF) and insulin-like growth factor I (IGF-I) regulate hormone production in several endocrine cells cultures. We have previously found that 12-O-tetradecanoyl phorbol-13-acetate (TPA), a protein kinase C activator, potentiates the cAMP-mediated secretion of human CB (hCG) in cultured human choriocarcinoma cells. We have now studied whether EGF and IGF-I modify cAMP-mediated hCG secretion in JEG-3 cells, which possess high affinity receptors to these growth factors.
View Article and Find Full Text PDFEndocrinology
June 1988
INSERM U 307, Hôpital Debrousse, Lyon, France.
We have characterized insulin-like growth factor I (IGF-I) and insulin receptors in cultured bovine adrenal cells by binding and cross-linking affinity experiments. At equilibrium the dissociation constant and the number of binding sites per cell for IGF-I were 1.4 +/- (SE) 0.
View Article and Find Full Text PDFEndocrinology
May 1988
Department of Obstetrics and Gynecology, University Central Hospital, Helsinki, Finland.
The placenta expresses genes for insulin-like growth factors (IGFs) and possesses IGF-receptors, suggesting that placental growth is regulated by IGFs in an autocrine manner. We have previously shown that human decidua, but not placenta, synthesizes and secretes a 34 K IGF-binding protein (34 K IGF-BP) called placental protein 12. We now used human choriocarcinoma JEG-3 cell monolayer cultures and recombinant (Thr59)IGF-I as a model to study whether the decidual 34 K IGF-BP is able to modulate the receptor binding and biological activity of IGFs in trophoblasts.
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