IGF I, also known as Mechano Growth Factor, somatomedin-C, IGF-I, and IGF1, is a secreted protein that belongs to the insulin family. The insulin family, comprised of insulin, relaxin, insulin-like growth factors I and II ( IGF-I and IGF-II ), and possibly the beta-subunit of 7S nerve growth factor, represents a group of structurally related polypeptides whose biological functions have diverged. The IGFs, or somatomedins, constitute a class of polypeptides that have a key role in pre-adolescent mammalian growth. IGF-I expression is regulated by GH and mediates postnatal growth, while IGF-II appears to be induced by placental lactogen during prenatal development. IGF1 / IGF-I may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. IGF1 / IGF-I stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also about enhancing glucose uptake. Defects in IGF1 / IGF-I are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) which is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness, and mental retardation.
The insulin-like growth factor-1 receptor (IGF1R) is a transmembrane tyrosine kinase involved in several biological processes including cell proliferation, differentiation, DNA repair, and cell survival. This a disulfide-linked heterotetrameric transmembrane protein consisting of two α and two β subunits, and among which, the α subunit is extracellular while the β subunit has an extracellular domain, a transmembrane domain and a cytoplasmic tyrosine kinase domain. The IGF-I receptor is highly expressed in all cell types and tissues. Essentially all of the biological activities of IGF-I and II have been shown to be mediated via IGF-I R. IGF1R is an important signaling molecule in cancer cells and plays an essential role in the establishment and maintenance of the transformed phenotype. Inhibition of IGF1R signaling thus appears to be a promising strategy to interfere with the growth and survival of cancer cells, is now an attractive anti-cancer treatment target.
Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 (IGFBP2) belongs to the RRM IMP/VICKZ family. IGFBP2 is a cytoplasmic protein and contains four KH domains and two RRM (RNA recognition motif) domains. IGF2BP2 binds to the 5'-UTR of the Insulin-Like Growth Factor 2 (IGF2) mRNA. This binding is isoform-specific. IGF2BP2 may regulate translation of target mRNAs. Genetic variation at the IGF2BP2 gene has been associated with type 2 diabetes (T2D) by genome-wide association studies and by replication analyses.
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