Inhibition of the insulin-like growth factor (IGF)-IFG-binding protein interaction

Authors
Citation
Rc. Baxter, Inhibition of the insulin-like growth factor (IGF)-IFG-binding protein interaction, HORMONE RES, 55, 2001, pp. 68-72
Citations number
33
Categorie Soggetti
Endocrinology, Nutrition & Metabolism
Journal title
HORMONE RESEARCH
ISSN journal
03010163 → ACNP
Volume
55
Year of publication
2001
Supplement
2
Pages
68 - 72
Database
ISI
SICI code
0301-0163(2001)55:<68:IOTIGF>2.0.ZU;2-3
Abstract
A family of six insulin-like growth factor (IGF) binding proteins transport IGFs in the circulation and regulate their extravascular distribution. The acid-labile subunit (ALS) combines with IGF-binding protein (IGFBP)-3 or I GFBP-5 to form abundant and stable heterotrimeric IGF-transporting complexe s which are confined to the circulation. The factors that determine ALS dis sociation, and regulate IGF and IGFBP passage out of the circulation, are p oorly understood. Binary IGF-IGFBP complexes have high affinities and slow dissociation rates, which may be accelerated by partial IGFBP proteolysis a nd interaction with glycosaminoglycans. IGFBPs can interfere in IGF analyse s, so removal of IGFBPs, and minimization of their influence in IGF assays, is essential to ensure valid quantification of IGFs. Copyright (C) 2001 S. Karger AG, Basel.