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There is a 60% homology between IGF-1R and the insulin receptor. The structures of the autophosphorylation complexes of tyrosine residues 1165 and 1166 have been identified within crystals of the IGF1R kinase domain. [6] In response to ligand binding, the α chains induce the tyrosine autophosphorylation of the β chains.
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 "axis" is also commonly referred to as the Growth Hormone/IGF-1 Axis. Insulin-like growth factor 1 (commonly referred to as IGF-1 or at times using Roman numerals as IGF-I) is mainly secreted by the liver as a result of stimulation by growth hormone (GH).
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Down-regulation of IGF1R in bone marrow biopsies of metastatic prostate cancer goes along with down-regulation of IRS-1 and significant reduction of PTEN in 3 out of 12 cases. Most of the tumors still express IRS-1 and IGF1R during progression of the metastatic disease. [44] IRS-1 has a functional role in breast cancer progression and metastasis.
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]