Protein Domain : Insulin-like growth factor-binding protein 1 IPR022322

Type	Family
Description	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 [].
Short Name	IGFBP1