Signal transduction by a chimeric insulin-like growth factor-1 (IGF-1) receptor having the carboxyl-terminal domain of the insulin receptor
作者： S. Tartare , I. Mothe , A. Kowalski-Chauvel , J.P. Breittmayer , R. Ballotti
DOI: 10.1016/S0021-9258(19)78144-7
关键词:
摘要: Insulin-like growth factor-1 receptors (IGF-1R) and insulin (IR) are closely related tyrosine kinases. However, the IR plays a major role in metabolism control, whereas IGF-1R is mainly involved differentiation. With these observations mind, we wished to define regions of responsible for generation biological specificity. We constructed chimeric which carboxyl-terminal domain was replaced by that IR. This receptor (IGF/CTIR) expressed NIH3T3 cells, compared its activity with wild-type receptors. The IGF/CTIR fully functional regarding kinase properties. Comparison IGF-1 effects on respectively, indicated more efficient stimulating glycogen synthesis p44mapk than IGF-1R. Interestingly, IGF/CTIR16 cells expressing only 250,000 better stimulated 600,000 Similarly, activation slightly higher cells. These results suggest tightly coupled stimulation pathway propose this crucial transmission could account, at least part,
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