| First Author | Zhou R | Year | 2003 |
| Journal | J Endocrinol | Volume | 178 |
| Issue | 2 | Pages | 177-93 |
| PubMed ID | 12904166 | Mgi Jnum | J:86026 |
| Mgi Id | MGI:2677911 | Doi | 10.1677/joe.0.1780177 |
| Citation | Zhou R, et al. (2003) IGF-binding protein-4: biochemical characteristics and functional consequences. J Endocrinol 178(2):177-93 |
| abstractText | 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. |
