Results 231 to 240 of about 14,817,072 (278)

On the nomenclature of the insulin-like growth factor binding proteins

Molecular and Cellular Endocrinology, 1989
Abstract 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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Colocalization of insulin-like growth factor-binding protein with insulin-like growth factor I

American Journal of Physiology-Renal Physiology, 1991
We 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, D R, Clemmons, M A, Venkatachalam   +2 more
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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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The Role of Insulin-Like Growth Factor Binding Proteins in Development

Reviews in Endocrine and Metabolic Disorders, 2005
J M, Pell, D A M, Salih, L J, Cobb, G, Tripathi, A, Drozd   +4 more
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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 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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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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General aspects of insulin-like growth factor binding proteins

Endocrine, 1997
Insulin-like growth factor binding proteins (IGFBPs) belong to a family of at least six homologous proteins that bind insulin-like growth factors (IGFs) and modulate many of their biological actions. IGFBPs are produced by a wide variety of tissues and their circulating levels are regulated by both hormonal and metabolic factors.
K, Chan, E M, Spencer
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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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