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Showing 1 to 7 of 7 for “"insulin-like growth factor binding proteins"”.

  1. Insulin-like Growth Factor Binding Proteins in the Plasma of Growing Horses

    Insulin-like growth factor binding proteins (IGFBP) are modulators of insulin-like growth factor I (IGF-I), which functions as a regulator of cartilage and bone development. Rapid growth and high starch diets have been associated with increased circulating concentrations of IGF-I, which lead to …

    vt Repository record for Insulin-like Growth Factor Binding Proteins in the Plasma of Growing Horses (opens in a new tab)

  2. Modifikace peptidového substrátu pro pappalysiny zavedením pseudopeptidu do štěpeného místa

    … of a modified peptide based on the structure of insulin-like growth factor binding proteins (IGFBPs), which are substrates of pappalysin metalloproteases (PAPPA-A, PAPP-A2). These enzymes regulate the bioavailability of insulin-like growth factors (IGF) by cleaving the IGFBPs. The peptide …

    charles-prague Repository record for Modifikace peptidového substrátu pro pappalysiny zavedením pseudopeptidu do štěpeného místa (opens in a new tab)

  3. Characterization of Insulin-like Growth Factor Binding Protein-3 (IGFBP-3) interaction with the Bovine Aortic Endothelial (BAE) cell surface: Examination of the Role of Heparan Sulfate Proteoglycans (HSPG)

    Insulin-like growth factor binding proteins (IGFBPs) are known to be important modulators of the insulin-like growth factor (IGF-I). However, their precise role is as yet unclear. Further, recent studies have indicated that IGFBP-3 has a receptor mediated growth inhibitory response of its own. In …

    vt Repository record for Characterization of Insulin-like Growth Factor Binding Protein-3 (IGFBP-3) interaction with the Bovine Aortic Endothelial (BAE) cell surface: Examination of the Role of Heparan Sulfate Proteoglycans (HSPG) (opens in a new tab)

  4. Effect of the Insulin-like Growth Factor (IGF) Axis on the Transport Properties of Endothelial and Epithelial Cells In Vitro

    … layer permeability, tight and adherens junction proteins, IGF-IR, and a downstream signaling components of IGF-IR. In comparison with parental cells, IGF-I secreting cells had high levels of IGF-IRs, but low levels of the junction components E-cadherin, b-catenin, and occludin. The differences in …

    vt Repository record for Effect of the Insulin-like Growth Factor (IGF) Axis on the Transport Properties of Endothelial and Epithelial Cells In Vitro (opens in a new tab)

  5. Strategies to Improve Reproductive Efficiency in Cattle with Dietary Intervention

    … may have on reproductive hormones, follicular growth, and pregnancy rates. The high starch diet tended to have a greater placental associated glycoprotein concentration, a greater number of large follicles on the day of breeding and a 20% numerically greater overall conception rate. The high …

    vt Repository record for Strategies to Improve Reproductive Efficiency in Cattle with Dietary Intervention (opens in a new tab)

  6. The Role of Insulin-like Growth Factor-I and IGF-binding Proteins in Mammary Gland Development

    Development of the mammary gland is likely mediated by locally produced growth factors acting in concert with circulating mitogens. To investigate the importance of mammary synthesis of insulin-like growth factor-I (IGF-I) and IGF-binding proteins (IGFBP), the initial objective was to evaluate the …

    vt Repository record for The Role of Insulin-like Growth Factor-I and IGF-binding Proteins in Mammary Gland Development (opens in a new tab)

  7. Determining the endometrial phenotype of women with abnormal uterine bleeding

    … be upregulated, whilst the regulation involving insulin like growth factor binding proteins (IGFBPs) or VEGF (marker of angiogenesis) were downregulated. Immunohistochemistry, confirmed expected spatial-temporal immunolocalisation of AR in AUB-L. However, PR, PRB, and ERα secretory phase …

    edinburgh Repository record for Determining the endometrial phenotype of women with abnormal uterine bleeding (opens in a new tab)