Results 251 to 260 of about 207,610 (292)

Insulin-like growth factor-I and insulin-like growth factor-binding proteins in the nephrotic syndrome

Pediatric Nephrology, 1996
Similar to findings in the nephrotic syndrome in humans, rats with the doxorubicin-induced nephrotic syndrome (which resembles minimal change disease) have reduced serum levels of insulin-like growth factor-I (IGF-I). This is mainly caused by glomerular ultrafiltration of IGF-I-containing binding protein complexes, primarily of a molecular weight of ...
S M, Feld, R, Hirschberg
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Insulin‐like growth factor‐binding protein 1 and insulin‐like growth factor‐binding protein 3 in pre‐eclampsia

BJOG: An International Journal of Obstetrics & Gynaecology, 1996
Objective To investigate circulating levels of insulin‐like growth factor‐binding protein 1 (IGFBP‐1) and IGFBP‐3 in the mother and the fetus in pregnancies complicated by pre‐eclampsia, and the relationship between serum levels of IGFBPs and fetal birthweight.Design A prospective study over an 18 month period.Setting A tertiary care ...
H S, Wang, J D, Lee, B J, Cheng, Y K, Soong   +3 more
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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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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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Insulin-like growth factor receptors and binding proteins

Baillière's Clinical Endocrinology and Metabolism, 1996
The insulin-like growth factor receptors are integral membrane proteins and demonstrate separate, but important effects on the regulation of cellular processes. The IGF-I receptor signals multiple cascades via its inherent tyrosine kinase activity. The IGF-II/M-6-P receptor on the other hand is primarily involved in targeting of enzymes to various ...
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Insulin-Like Growth Factor-Binding Proteins and Ovarian Folliculogenesis

Hormone Research, 2008
In 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, Besnard, N., Huet, Camille, Pisselet, C., Monniaux, Danielle   +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 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 Factors, Insulin-Like Growth Factor Binding Proteins and Ovarian Androgen Production

Hormone Research, 2008
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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Folding of Insulin-like Growth Factor I Is Thermodynamically Controlled by Insulin-like Growth Factor Binding Protein

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, A, Hansson, M, Uhlén, B, Nilsson   +3 more
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