The Experts below are selected from a list of 3 Experts worldwide ranked by ideXlab platform
Axel Ullrich - One of the best experts on this subject based on the ideXlab platform.
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igf1r igf1 Receptor vertebrates Somatomedin Receptor
The Protein Kinase FactsBook#R##N#Protein-Serine Kinases, 1995Co-Authors: Reiner Lammers, Axel UllrichAbstract:The IGF1 Receptor a subunit binds insulin-like growth factor-1 with high affinity. Binding leads to activation of the tyrosine kinase, autophosphorylation of the Receptor itself, and tyrosine phosphorylation of cytoplasmic proteins. In cultured cells, within minutes, membrane transport processes (for example, glucose transport) are stimulated, and within hours physiological activities such as glycogen synthesis and DNA synthesis are stimulated. IGF1R overexpression can lead to cellular transformation. In vivo IGF1R is regulated in its expression with embryonic development or cell differentiation. Its function is presumed to be primarily mitogenic. The protein is synthesized as a single precursor that is dimerized by disulphide bonds and then processed into a heterotetrameric protein with two α and two β subunits. The α subunits are connected to each other and to the β subunits via disulphide bonds and contain the binding site for the ligand, IGF1. The extracellular domain contains 16 potential N-glycosylation sites, and its size varies depending on cell type. An alternative transcript with the substitution of Arg at position 899 for Thr-Gly is expressed ubiquitously. Presence of IGF1R can be assayed on intact cells by binding of [125I]-IGF1. Kinase activity of purified Receptor can be monitored by autophosphorylation.
Reiner Lammers - One of the best experts on this subject based on the ideXlab platform.
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igf1r igf1 Receptor vertebrates Somatomedin Receptor
The Protein Kinase FactsBook#R##N#Protein-Serine Kinases, 1995Co-Authors: Reiner Lammers, Axel UllrichAbstract:The IGF1 Receptor a subunit binds insulin-like growth factor-1 with high affinity. Binding leads to activation of the tyrosine kinase, autophosphorylation of the Receptor itself, and tyrosine phosphorylation of cytoplasmic proteins. In cultured cells, within minutes, membrane transport processes (for example, glucose transport) are stimulated, and within hours physiological activities such as glycogen synthesis and DNA synthesis are stimulated. IGF1R overexpression can lead to cellular transformation. In vivo IGF1R is regulated in its expression with embryonic development or cell differentiation. Its function is presumed to be primarily mitogenic. The protein is synthesized as a single precursor that is dimerized by disulphide bonds and then processed into a heterotetrameric protein with two α and two β subunits. The α subunits are connected to each other and to the β subunits via disulphide bonds and contain the binding site for the ligand, IGF1. The extracellular domain contains 16 potential N-glycosylation sites, and its size varies depending on cell type. An alternative transcript with the substitution of Arg at position 899 for Thr-Gly is expressed ubiquitously. Presence of IGF1R can be assayed on intact cells by binding of [125I]-IGF1. Kinase activity of purified Receptor can be monitored by autophosphorylation.