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lüll IGF-binding protein-4: biochemical characteristics and functional consequences Zhou R; Diehl D; Hoeflich A; Lahm H; Wolf EJ Endocrinol 2003[Aug]; 178 (2): 177-93IGFs 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.|Animals[MESH]|Base Sequence[MESH]|Cell Membrane/metabolism[MESH]|Extracellular Matrix/metabolism[MESH]|Female[MESH]|Humans[MESH]|Insulin-Like Growth Factor Binding Protein 4/genetics/*metabolism[MESH]|Kidney Diseases/metabolism[MESH]|Kidney/metabolism[MESH]|Male[MESH]|Mice[MESH]|Molecular Sequence Data[MESH]|Neoplasms/metabolism[MESH]|Osteogenesis/physiology[MESH]|Ovary/metabolism[MESH]|Pregnancy[MESH]|Protein Binding[MESH]|Rats[MESH]|Sequence Alignment[MESH]|Somatomedins/*metabolism[MESH]|Structure-Activity Relationship[MESH]|Tissue Distribution[MESH] |