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Journal of Endocrinology (2003) 178, 177-193       DOI: 10.1677/joe.0.1780177
© 2003 Society for Endocrinology
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Journal of Endocrinology, Vol 178, Issue 2, 177-193
Copyright © 2003 by Society for Endocrinology

Articles

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

R Zhou, D Diehl, A Hoeflich, H Lahm, and E Wolf


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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