IGF-binding protein-4: biochemical characteristics and functional consequences

in Journal of Endocrinology
Authors:
R Zhou
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,
D Diehl
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,
A Hoeflich
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H Lahm
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E Wolf
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DOI:
https://doi.org/10.1677/joe.0.1780177
Volume/Issue:
Volume 178: Issue 2
Article Type:
Other
Page Range:
177–193
Online Publication Date:
01 Aug 2003
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IGFs have multiple functions regarding cellular growth, survival and differentiation under different physiological and pathological conditions. IGF effects are modulated systemically and locally by six high-affinity IGF-binding proteins (IGFBP-1 to -6). Despite their structural similarity, each IGFBP has unique properties and exhibits specific functions. IGFBP-4, the smallest IGFBP, exists in both non-glycosylated and N-glycosylated forms in all biological fluids. It is expressed by a wide range of cell types and tIssues, and its expression is regulated by different mechanisms in a cell type-specific manner. IGFBP-4 binds IGF-I and IGF-II with similar affinities and inhibits their actions under almost all in vitro and in vivo conditions. In this review, we summarize the available data regarding the following aspects of IGFBP-4: genomic organization, protein structure-function relationship, expression and its regulation, as well as IGF-dependent and -independent actions. The biological significance of IGFBP-4 for reproductive physiology, bone formation, renal pathophysiology and cancer is discussed.

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Print ISSN:
0022-0795
Online ISSN:
1479-6805
Page(s):
17
Article Type:
Other
Print Publication Date:
01 Aug 2003
Online Publication Date:
01 Aug 2003