Insulin-like growth factors (IGFs)-I and -II are small secreted peptides that stimulate the survival, and promote the proliferation and differentiation, of many cell types. In biological fluids, these growth factors are usually bound to IGF binding proteins (IGFBPs), which regulate their availability and activity by prolonging their half-life and modulating their receptor interactions. To date, six IGFBP family members have been identified (termed IGFBP1-6). They share a conserved gene (intron-exon) organisation and high IGF binding affinity. Structurally, the proteins also share a common domain architecture, possessing a conserved N-terminal IGFBP domain, a highly variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their C-terminal regions. In addition to their role in the regulation of IGF activity, there is evidence for the direct association of IGFBPs with a variety of extracellular and cell surface molecules, with consequent effects upon important biological processes. These include modulation of bone cell proliferation, and growth arrest of breast and prostate cancer cells. IGFBP1 (also known as amniotic fluid binding protein (AFBP) and placental protein-12) is involved in the regulation of foetal growth: there is a strong inverse correlation between circulating IGFBP1 levels and foetal size. It also functions as a survival factor and pro-regeneration factor in the liver.
Taxonomy/Path:
InterPro : Insulin-like growth factor-binding protein family 1-6, chordata / Insulin-like growth factor-binding protein 1