Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells
โ Scribed by White, Morris F.; Maron, Ruth; Kahn, C. Ronald
- Book ID
- 109741847
- Publisher
- Nature Publishing Group
- Year
- 1985
- Tongue
- English
- Weight
- 485 KB
- Volume
- 318
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/318183a0
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
The insulin receptor (IR) tyrosine kinase is essential for the regulation of different cellular functions by insulin. This may occur by a direct phosphorylation of membrane and/or cytoplasmic proteins by the IR tyrosine kinase. Hence it is important to identify putative physiological substrates for
NA and Ca9-22 cells derived from squamous cell carcinomas of the tongue possess a large number of epidermal growth factor (EGF) receptors (2.0 x 10" and 1.3 x l o 6 receptorsicell, respectively). In these cell lines, EGF stimulated receptor autophosphorylation and phosphatidylinositol (PI) turnover.
Colony-stimulating factor 1 (CSF-1) selectively supports the survival, proliferation, and maturation of hemopoietic cells of the monocytehacrophage lineage. Although the cellular receptor for CSF-1, (the c-fms protein) is a protein-tyrosine kinase activated by the binding of CFS-I, the role of phosp