Results 311 to 320 of about 422,814 (354)

Insulin-like growth factor binding proteins as glucoregulators

Metabolism, 1995
Circulating 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 proteins

1997
The 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

1993
Publisher 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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Insulin‐Like Growth Factor Binding Proteins

Comprehensive Physiology, 1990
Abstract The sections in this article are: Gene Structures Insulin‐Like Growth Factor Binding Protein 1 Insulin‐Like Growth Factor Binding Protein 2
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Insulin-Like Growth Factors, Insulin-Like Growth Factor Binding Proteins and Ovarian Androgen Production

Hormone Research, 1994
Increasing evidence indicates that the ovary contains an insulin-like growth factor (IGF) system complete with ligands, binding proteins, and receptors. Through their interaction with IGF receptors on theca-interstitial cell surface membranes, the ligands, IGF-I and IGF-II, synergize with luteinizing hormone (LH) to increase ovarian androgen production.
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Insulin‐like growth factor binding proteins: a proposed superfamily

Acta Paediatrica, 1999
Hwa V, Oh Y, Rosenfeld RG. Insulin‐like growth factor binding proteins: a proposed superfamily. Acta Pzdiatr 1999; Suppl 428:37‐45. Stockholm. ISSN 0803‐5326The conventional concept is that the insulin‐like growth factor binding proteins (IGFBPs) are cysteine‐rich proteins, with conserved N‐ and C‐domains, that are capable of binding insulin‐like ...
V, Hwa, Y, Oh, R G, Rosenfeld
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Insulin-like growth factor-binding protein-6 and cancer

Clinical Science, 2012
The 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 of equine serum

Biochemical and Biophysical Research Communications, 1992
Ligand 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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Characterization of urinary insulin-like growth factor binding proteins

The Journal of Clinical Endocrinology & Metabolism, 1992
The insulin-like growth factors (IGFs) are important mitogens that are present in many body fluids, where they are commonly bound with high affinity to IGF binding proteins (IGFBPs). We investigated human urine for the presence of IGFBPs. Western ligand blots of concentrated, dialyzed normal urine disclosed the presence of two major bands with IGF ...
Y, Hasegawa, P, Cohen, P, Yorgin, R G, Rosenfeld   +3 more
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Functional Role of Insulin-Like Growth Factor Binding Proteins

Hormone Research, 1997
Insulin-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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