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The IGF-1 receptor seems to be the "physiologic" receptor—it binds IGF-1 at significantly higher affinity than it binds insulin. [9] Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase—meaning it signals by causing the addition of a phosphate molecule on particular tyrosines.
IGF-1 binds to at least two cell surface receptor tyrosine kinases: the IGF-1 receptor (IGF1R), and the insulin receptor. Its primary action is mediated by binding to its specific receptor, IGF1R, which is present on the surface of many cell types in many tissues [further explanation needed]. Binding to the IGF1R initiates intracellular signaling.
The IGF-1 receptor is the "physiological" receptor. IGF-1 binds to it at significantly higher affinity than it binds the insulin receptor. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase—meaning the receptor signals by causing the addition of a phosphate molecule on particular tyrosines. The IGF-2 receptor only ...
The insulin-like growth factor receptors (IGFRs) include the following two receptors: Insulin-like growth factor 1 receptor (IGF-1R)
Rhabdomyosarcoma is a cancer that highly expresses IGF1R receptors. In-vitro studies have been conducted to investigate the viability of picropodophyllin as a treatment. In in-vitro cell cultures, certain lines of rhabdomyosarcoma such as RH30 showed 90% of cells had expression of IGF1R. [3]
Insulin-like growth factors (IGFs) are pivotal in cellular processes contributing to normal physiology as well as certain pathologies (e.g., cancer). [3] The IGF family of proteins, also known as the IGF axis, consists of three ligands (insulin, IGF1, IGF2), three cell surface receptors (insulin receptor [IR], IGF1 receptor [IGF1R], IGF2 receptor [IGF2R]), and seven IGF binding proteins ...