Autor: |
Scimeca, J C, Ballotti, R, Alengrin, F, Honegger, A M, Ullrich, A, Schlessinger, J, Obberghen, E V |
Zdroj: |
Journal of Biological Chemistry; April 1989, Vol. 264 Issue: 12 p6831-6835, 5p |
Abstrakt: |
The epidermal growth factor (EGF) receptor tyrosine kinase activity is required for both the earliest EGF-stimulated post-binding events (enhancement of inositol phosphate formation and Ca2+influx, activation of Na+/H+exchange), and the ultimate EGF-induced mitogenic response. To assess the role of EGF receptor kinase in EGF-induced metabolic effects (2-deoxyglucose and 2-aminoisobutyric acid uptake), we used NIH3T3 cells (clone 2.2), which do not possess endogenous EGF receptors and which were transfected with cDNA constructs encoding either wild type or kinase-deficient human EGF receptor (HER). In addition, we tested the importance of three HER autophosphorylation sites (Tyr-1068, Tyr-1148, and Tyr-1173) in transduction of EGF-stimulated 2-deoxyglucose uptake. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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