Abstract
In biologic fluids, insulinlike growth factors (IGF-I and IGF-II) are bound to high-affinity insulinlike growth factor binding proteins (IGFBPs), of which seven have now been identified (IGFBPs 1-7). In a variety of biologic fluids, several IGFBPs undergo proteolytic degradation. Such degradation can lead to increased IGF bioavailability at the cell surface, facilitating receptor interactions. Herein, recent data identifying several IGFBP-degrading proteinases and their effects on IGF bioactivity is reviewed, and how IGFBP proteolysis is regulated by IGFs and IGFBPs, as well as how IGFBP cleavage analysis provides insights into the structure and function of IGFBPs, is explored.
Original language | English |
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Pages (from-to) | 299-306 |
Number of pages | 8 |
Journal | Trends in Endocrinology and Metabolism |
Volume | 8 |
Issue number | 8 |
DOIs | |
State | Published - Oct 1997 |
Bibliographical note
Funding Information:This work was supported in part by NIH grant DK02776.
Funding
This work was supported in part by NIH grant DK02776.
Funders | Funder number |
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National Institutes of Health (NIH) | DK02776 |
ASJC Scopus subject areas
- Endocrinology, Diabetes and Metabolism
- Endocrinology