Insulin-like growth factor binding proteins and their role in controlling IGF actions Public Deposited

Downloadable Content

Download PDF
Creator
  • Clemmons, David
    • Affiliation: School of Medicine, Department of Medicine, Division of Endocrinology and Metabolism
Abstract
  • The insulin-like growth factor binding proteins (IGFBPs) area family of six proteins that bind to insulin-like growth factor-I and -II with very high affinity. Because their affinity constants are between two- and 50-fold greater than the IGF-I receptor, they control the distribution of the IGFs among soluble IGFBPs in interstitial fluids, IGFBPs bound to cell surfaces or extracellular matrix (ECM) and cell surface receptors. Although there are six forms of insulin-like growth factor binding proteins, most interstitial fluids contain only three or four forms, and usually only one or two predominate. The proteins differ significantly in their biochemical characteristics, and this accounts for many of the differences that have been observed in their biological actions. Several different types of protease cleave these binding proteins. Proteolytic cleavage generally inactivates the binding proteins or reduces their ability to bind to IGF-I or -II substantially. Several cell types have been shown to secrete these proteases; therefore, the factors that regulate protease activity can control binding protein actions indirectly. Other post-translational modifications, such as glycosylation and phosphorylation, have been shown to alter IGF binding protein activity. While binding protein actions have been studied extensively in vitro, many of the in vivo activities of these proteins remain to be defined.
Date of publication
Keyword
Identifier
  • doi:10.1016/S1359-6101(96)00053-6
  • 2-s2.0-0031105225
Related resource URL
Resource type
  • Journal Item
Rights statement
  • In Copyright
Journal title
  • Cytokine and Growth Factor Reviews
Journal volume
  • 8
Journal issue
  • 1
Page start
  • 45
Page end
  • 62
Language
  • English
Version
  • Postprint
ISSN
  • 1359-6101
Parents:

This work has no parents.

Items