Results 301 to 310 of about 394,398 (350)
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Clinical Uses of Insulin-like Growth Factor I
Annals of Internal Medicine, 1994Insulin-like growth factor I (IGF-I) has acute insulin-like metabolic effects and long-term anabolic actions. The therapeutic potential of recombinant human IGF-I treatment is being investigated in various growth hormone-resistant and insulin-resistant disorders. Recent studies have shown that IGF-I may substitute for growth hormone in promoting linear
C A, Bondy +5 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
P E, Vos +3 more
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Growth hormone and insulin-like growth factor-I in odontogenesis
The International Journal of Developmental Biology, 1995This review documents recent insights into the roles of growth hormone and insulin-like growth factor-I during tooth formation. Hereditarily growth hormone-deficient Lewis dwarf rats and hypophysectomized rats have been used to document the influence of growth hormone on growth of the rat incisor and molar teeth in vivo.
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Drug delivery of Insulin-like growth factor I
European Journal of Pharmaceutics and Biopharmaceutics, 2015This review starts off outlining the control of Insulin-like growth factor I (IGF-I) kinetics in Nature and by virtue of a complex system of 6 binding proteins controlling half-life and tissue distribution of this strong anabolic peptide. In addition, alternative splicing is known to result in IGF-I variants with modulated properties in vivo and this ...
Isabel Schultz +2 more
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The insulin-like growth factor-I receptor as an oncogene
Archives of Physiology and Biochemistry, 2009The insulin-like growth factor-I receptor (IGF-IR) mediates the biological actions of both IGF-I and IGF-II. The IGF-IR is expressed in most transformed cells, where it displays potent antiapoptotic, cell-survival, and transforming activities. IGF-IR expression is a fundamental prerequisite for the acquisition of a malignant phenotype, as suggested by ...
Haim, Werner, Ilan, Bruchim
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Defining Insulin-Like Growth Factor-I Deficiency
Hormone Research, 2006• The GH-IGF system should be viewed like other endocrine systems, with a central, trophic hormone (GH) and a peripherally active hormone (IGF-I). • A decrease in IGF-I production, without a concomitant impairment in GH secretion, should be termed 'Primary IGF deficiency'.
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Nutritional regulation of insulin-like growth factor-I
Metabolism, 1995Several lines of evidence indicate that in the human, insulin-like growth factor-I (IGF-I) is nutritionally regulated. Both energy and protein availability are required for maintenance of IGF-I. Measurements of serum IGF-I constitute a sensitive means for monitoring the response of acutely ill patients to nutritional intervention.
J M, Ketelslegers +4 more
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Insulin-like growth factor-I and cancer risk
Growth Hormone & IGF Research, 2004Growth factor pathways are fundamental in normal tissue regulation and development. In many tissues, factors that function in normal growth and development also have important regulatory roles in transformed malignant cells. The insulin-like growth factor (IGF) system is implicated in the regulation of the malignant phenotype by its effects on ...
Yasir H, Ibrahim, Douglas, Yee
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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.
S, 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.
S, Hober +3 more
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