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Insulin‐like growth factor I actions on steroidogenesis
Acta Paediatrica, 1994The best evidence that insulin‐like growth factor I (IGF‐I) contributes to normal steroidogenesis comes from patients with growth hormone (GH) insensitivity syndrome due to deletion of the GH receptor gene. These patients have severe GH resistance and severe IGF‐I insufficiency, and present with markedly delayed puberty without gonadotrophin ...
Chatelain, P.G.+7 more
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Hormone and Metabolic Research, 1989
Receptor-mediated endocytosis may represent an important mechanism whereby peptide hormones exert their biological effects. The ability of recombinant insulin-like growth factor (IGF)-I to be internalized by cultured cells was evaluated in BRL-3A2 cells, a rat liver-derived cell line which lacks insulin receptors.
Ron G. Rosenfeld+2 more
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Receptor-mediated endocytosis may represent an important mechanism whereby peptide hormones exert their biological effects. The ability of recombinant insulin-like growth factor (IGF)-I to be internalized by cultured cells was evaluated in BRL-3A2 cells, a rat liver-derived cell line which lacks insulin receptors.
Ron G. Rosenfeld+2 more
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Journal of Dairy Research, 1999
The mammary gland is an example of a tissue of epidermal origin that depends for the development of its characteristic morphology on underlying mesenchymal cells. The interaction between mesenchyme and epithelium appears to be mediated by polypetide growth factors.
Forsyth, Isabel A.+2 more
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The mammary gland is an example of a tissue of epidermal origin that depends for the development of its characteristic morphology on underlying mesenchymal cells. The interaction between mesenchyme and epithelium appears to be mediated by polypetide growth factors.
Forsyth, Isabel A.+2 more
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Peptides, 1993
Recombinant human insulin-like growth factor I (hIGF-I) was reacted with azidobenzoyl hydroxysuccinimide to produce a mixture of photoactive hIGF-I derivatives. The mixture was purified by reversed-phase HPLC to yield three mono-substituted azidobenzoyl hIGF-Is.
Lynn Seely+3 more
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Recombinant human insulin-like growth factor I (hIGF-I) was reacted with azidobenzoyl hydroxysuccinimide to produce a mixture of photoactive hIGF-I derivatives. The mixture was purified by reversed-phase HPLC to yield three mono-substituted azidobenzoyl hIGF-Is.
Lynn Seely+3 more
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Journal of Clinical Endocrinology and Metabolism, 1994
Serum levels of insulin-like growth factor-I (IGF-I) increase with age and pubertal development. The large variation in circulating IGF-I levels in adolescence makes it difficult to use the IGF-I value of a single child in the assessment of his growth ...
A. Juul+8 more
semanticscholar +1 more source
Serum levels of insulin-like growth factor-I (IGF-I) increase with age and pubertal development. The large variation in circulating IGF-I levels in adolescence makes it difficult to use the IGF-I value of a single child in the assessment of his growth ...
A. Juul+8 more
semanticscholar +1 more source
Exercise and Circulating Insulin-Like Growth Factor I [PDF]
Determinations of serum concentrations of total insulin-like growth factor I (tIGF-I) are important in the diagnosis, monitoring of treatment and safety evaluation of patients with growth disorders and/or metabolic disease. It is well established that tIGF-I status varies over time.
Ulrika Berg, Peter Fibiger Bang
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Effects of Insulin‐Like Growth Factor I in Man
Acta Paediatrica, 1990ABSTRACT. A 6‐day period of subcutaneous infusion with recombinant human insulin‐like growth factor I in three healthy male volunteers resulted in an increase in the ratio of insulin to C‐peptide levels and significant decreases in triglyceride levels and the ratio of total to high density lipoprotein—cholesterol in serum.
H P Guler+3 more
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Biochemistry, 1994
Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al. (1992) Biochemistry 31, 1749-1756]. These results prompted the question of how IGF-I may overcome this energetic problem in its folding in vivo.
Sophia Hober+3 more
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Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al. (1992) Biochemistry 31, 1749-1756]. These results prompted the question of how IGF-I may overcome this energetic problem in its folding in vivo.
Sophia Hober+3 more
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General and Comparative Endocrinology, 1990
Molecular weight characteristics and plasma concentrations of insulin-like growth factor-I (IGF-I) and its binding protein (IGF-BP) were investigated in the toad, Bufo woodhousei. IGF-I and IGF-BP were measured by radioimmunoassay (RIA, Kd = 0.37 +/- 0.04 ng/ml) and charcoal-separated ligand binding assay, respectively, in male toad plasma and adult ...
Martha K. Pancak-Roessler+2 more
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Molecular weight characteristics and plasma concentrations of insulin-like growth factor-I (IGF-I) and its binding protein (IGF-BP) were investigated in the toad, Bufo woodhousei. IGF-I and IGF-BP were measured by radioimmunoassay (RIA, Kd = 0.37 +/- 0.04 ng/ml) and charcoal-separated ligand binding assay, respectively, in male toad plasma and adult ...
Martha K. Pancak-Roessler+2 more
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Insulin-like growth factor-I: Clinical studies
Drugs of Today, 1998Insulin-like growth factor-I (IGF-I) has endocrine, autocrine and paracrine properties. Receptors for IGF-I are present on virtually all cell types but are located mainly on cells of mesenchymal origin, such as fibroblasts, chondrocytes and osteoblasts. Growth hormone (GH)-dependent and GH-independent actions of IGF-I have been implicated in normal and
J. H. J. Wokke+3 more
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