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products ( Lewis et al. 1993 ). Candidate trophoblast growth factors include the insulin-like growth factors (IGFs) ( Han et al. 1996 ), and decidual inhibitors may include insulin-like growth factor-binding protein-1 (IGFBP-1) ( Rutanen et al. 1985
Department of Kinesiology and Nutrition, University of Illinois at Chicago, Chicago, Illinois, USA
Research and Development Division, Jesse Brown Veterans Affairs Medical Center, Chicago, Illinois, USA
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Department of Kinesiology and Nutrition, University of Illinois at Chicago, Chicago, Illinois, USA
Research and Development Division, Jesse Brown Veterans Affairs Medical Center, Chicago, Illinois, USA
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Section of Endocrinology, Diabetes, and Metabolism, Department of Medicine, University of Illinois at Chicago, Chicago, Illinois, USA
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Department of Kinesiology and Nutrition, University of Illinois at Chicago, Chicago, Illinois, USA
Research and Development Division, Jesse Brown Veterans Affairs Medical Center, Chicago, Illinois, USA
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. Insulin-like growth factor (IGF)-1 plays important role in wound healing through its ability to stimulate proliferation and migration of keratinocytes, endothelial cells and fibroblasts ( Kanekar et al. 2000 , Haase et al. 2003 , Deng et al. 2012
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factor binding protein (IBP-1). EMBO Journal 7 2417 –2423. Busby WH Jr, Klapper DG & Clemmons DR 1988 Purification of a 31 000-dalton insulin-like growth factor binding protein from human amniotic fluid. Isolation of
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. 2014 ). Among the hormones known to mediate these effects, the growth hormone (Gh)/insulin-like growth factor 1 (Igf1) axis is one of the most-studied regulators of osmoregulation in fish gill response to salinity stress. Gh/Igf1, considered as an SW
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DWH 1993 Hyaluronic activation of CD44 induces insulin-like growth factor-1 expression by a tumor necrosis factor-a-dependent mechanism in murine macrophages . Journal of Clinical Investigation 91 2368 – 2377 . Nyman T Pekonen F 1993
Translational and Clinical Research Institute, Newcastle University, Newcastle upon Tyne, UK
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in this setting and therefore requires further exploration. Growth hormone (GH) and insulin-like growth factor (IGF-1) are fundamental regulators of longitudinal bone growth and have synergistic effects as well as independent roles in the regulation
Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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Group on Hormones and Signal Transduction, German Cancer Research Center, Heidelberg D-69120, Germany
Laboratory of Genomic Applications, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
Department of Medicine, Baylor College of Medicine, Houston, Texas 77030, USA
Department of Oncological Surgery, Chaim Sheba Medical Center, Tel Hashomer 52621, Israel
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& LeRoith D 1995 Regulation of insulin-like growth factor I receptor gene expression by Sp1: physical and functional interactions of Sp1 at GC boxes and at a CT element. Molecular Endocrinology 9 1147 –1156. Castro-Rivera E
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ABSTRACT
Insulin-like growth factor-I (IGF-I) enhances and epidermal growth factor (EGF) inhibits gonadotrophin-induced aromatization in granulosa cells. Our previous studies have shown that human ovarian granulosa cells synthesize insulin-like growth factor-binding protein-1 (IGFBP-1) which inhibits IGF-stimulated DNA synthesis. The present study addresses the effect of EGF and gonadotrophins in the regulation of IGFBP-1 release by human granulosa cells cultured in serum-free medium. At concentrations of 1–100 μg/l EGF was found to stimulate IGFBP-1 secretion. This was not due to cell proliferation, as the viable cell count remained unaffected. Growth hormone and gonadotrophins had no effect on IGFBP-1 secretion when added alone to culture medium. These results suggest that EGF regulates IGFBP-1 secretion in human granulosa-luteal cells.
Journal of Endocrinology (1992) 134, 127–131
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ABSTRACT
Two hundred Chinese primigravidae had 50 g 3-h oral glucose tolerance tests (OGTTs) twice in pregnancy; between 20 and 24 weeks and between 30 and 34 weeks of gestation. In 149 women, a single sample was taken for insulin-like growth factor-binding protein-1 (IGFBP-1) measurement 0, 1, 2 or 3 h after the glucose load at both visits; in 55 women IGFBP-1 levels were estimated in all four OGTT samples. Fetal growth was assessed by ultrasound performed at the first and second visit and, if possible, at term, and by anthropometry of the neonate. Cord serum IGFBP-1 was measured in 144 of the babies. Mothers who developed gestational diabetes were excluded.
Maternal levels of IGFBP-1 were inversely related to glucose levels at 0, 1 and 2 h in the third trimester of pregnancy. IGFBP-1 measured at 1 h in an OGTT increased between the second and third trimester. There was an inverse correlation between maternal IGFBP-1 measured in the second trimester and all fetal measurements at that time, and with most neonatal measurements and birthweight. Levels of IGFBP-1 in the third trimester were inversely correlated to neonatal abdominal circumference, skinfold thickness and birthweight. Cord blood IGFBP-1 was inversely related to growth of abdominal circumference. The strongest inverse relationship was between IGFBP-1 and maternal weight. Fasting glucose in the second trimester was positively correlated to fetal subcutaneous fat and growth of abdominal circumference. In the third trimester it was related to fetal abdominal circumference, the growth of abdominal circumference, birthweight and neonatal skinfold thickness. In a multiple regression analysis, both glucose and IGFBP-1 were shown to be determinants of birthweight. It is concluded that IGFBP-1 levels are related to glucose tolerance in pregnancy, and that both IGFBP-1 and glucose have a role in determining birthweight.
Journal of Endocrinology (1993) 136, 319–325
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Insulin-like growth factor-binding protein-1 (IGFBP-1) production is increased by somatostatin and its analogues. In order to determine the time course and identify possible mechanisms of this increase in vivo we administered octreotide to rats and determined IGFBP-1 concentrations by RIA. After 60 min of anaesthesia, the mean baseline IGFBP-1 concentrations were 166 (95% confidence interval 123 to 225) ng/ml and increased in saline-infused animals to 729 (488 to 1086) ng/ml after 180 min. IGFBP-1 was stimulated transiently in response to octreotide, with circulating IGFBP-1 concentrations peaking at 1605 (1220 to 2111) ng/ml at 105 min during a continuous infusion of octreotide (100 micrograms/kg per h). In conscious chronically cannulated rats, baseline IGFBP-1 concentrations were 22 (18 to 28) ng/ml, 8-fold less than in the anaesthetised state, and were stimulated in the short term after administration of an octreotide bolus (100 micrograms/kg s.c.) to reach 88 (62 to 126) ng/ml at 60 min. A similar response was seen after i.v. administration to conscious rats. Intravenous bolus of octreotide (100 micrograms/kg) in rats anaesthetised for 3 h resulted in an increase in IGFBP-1 to peak at 1556 (1268 to 1910) ng/ml at 60 min. The IGFBP-1 response to octreotide was diminished in high-fat fed hyperinsulinaemic rats. The pattern of disappearance of iodinated IGFBP-1 from the circulation was not influenced by octreotide. The changes in GH, insulin and glucose concentrations alone did not sufficiently account for the patterns of response observed. We conclude that, in rats, octreotide stimulates IGFBP-1 acutely and this response is potentiated by factors related to anaesthesia.
