Results 201 to 210 of about 200,349 (246)
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Insulin-Like Growth Factor-Binding Proteins and Ovarian Folliculogenesis
Hormone Research, 2008In the ovary, insulin-like growth factors (IGFs) enhance both proliferation and differentiation of follicular cells by potentiating gonadotropin’s actions. The biological effects of IGFs are strikingly modulated by IGF-binding proteins (IGFBPs), whose levels in follicular fluid dramatically change during folliculogenesis.
Monget, Philippe +4 more
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Insulin-like Growth Factor Binding Proteins in Development
2005IGFBPs regulate growth and development by regulating IGF transport to tissues and IGF bioavailability to IGF receptors at cell membrane level. IGFBP excess leads predominantly to inhibition of IGF action and growth retardation with impaired organogenesis. Absence of human and also mouse ALS leads to decreased IGF-I levels in circulation and causes mild
Josef V, Silha, Liam J, Murphy
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Colocalization of insulin-like growth factor-binding protein with insulin-like growth factor I
American Journal of Physiology-Renal Physiology, 1991We report the localization of insulin-like growth factor I (IGF-I) and a 25-kDa form of insulin-like growth factor-binding protein (IGF-BP-1) in adult rat kidney. The antigens were localized using a rabbit anti-human IGF-I antibody, and a rabbit anti-human IGF-BP-1 antibody raised against human 25-kDa IGF-BP-1 purified from amniotic fluid ...
S, Kobayashi +2 more
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On the nomenclature of the insulin-like growth factor binding proteins
Molecular and Cellular Endocrinology, 1989Abstract The insulin-like growth factors (IGF) I and II circulate in plasma complexed to carrier or binding proteins. Based on their chromatographically determined molecular size they have been designated 150–200 kDa and 30–40 kDa IGF binding proteins (BP).
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Insulin-like growth factor binding proteins as glucoregulators
Metabolism, 1995Circulating insulin-like growth factors (IGFs) represent an important pool of potential hypoglycemic activity, which is largely inhibited by their sequestration in a heterotrimeric complex comprising growth factor, IGF-binding protein-3 (IGFBP-3), and acid-labile subunit (ALS). Less than 1% of total IGFs circulate in the free form, yet even this amount
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Insulin-like growth factor-binding protein-6 and cancer
Clinical Science, 2012The IGF (insulin-like growth factor) system is essential for physiological growth and it is also implicated in a number of diseases including cancer. IGF activity is modulated by a family of high-affinity IGF-binding proteins, and IGFBP-6 is distinctive because of its marked binding preference for IGF-II over IGF-I.
Leon A, Bach, Ping, Fu, Zhiyong, Yang
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Insulin-like growth factor binding proteins
1997The insulin-like growth factor binding proteins (IGFBPs) bind both IGF-I and IGF-II with high affinity. They control IGF half-lives, rates of efflux from the vascular space, distribution within extracellular fluids, and their equilibrium with cell surface receptors.
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Insulin-like Growth Factor Binding Proteins
1993Publisher Summary This chapter discusses the insulin-like growth factor (IGF) binding proteins—namely, IGF-I and IGF-II. The IGFs are purified from human plasma and cell culture medium by virtue of their ability to stimulate the growth of cartilage or cultured fibroblasts, or their insulin-like activity.
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Functional Role of Insulin-Like Growth Factor Binding Proteins
Hormone Research, 2009Insulin-like growth factors (IGF-I, IGF-II) are important regulators of cell division and differentiation. In their free form, IGFs form a complex with specific binding proteins (IGFBPs), six of which have now been characterized. These IGFBPs differ in their ability to bind IGF-I and/or IGF-II, and, depending on their location and metabolic ...
M B, Ranke, M, Elmlinger
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Insulin-like growth factor binding proteins of equine serum
Biochemical and Biophysical Research Communications, 1992Ligand blotting analysis of serum from the horse using radiolabelled IGF-I revealed a protein at 96 kDa which was not present in serum from goat, cow, sheep, deer or donkey. These latter species all displayed five labelled bands in the range 24 to 41 kDa. Conversely, these were only weakly labelled in serum from the horse. Size exclusion chromatography
C G, Prosser, R D, McLaren
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