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Título: | Phosphorylation of calmodulin by permeabilized fibroblasts overexpressing the human epidermal growth factor receptor |
Autor: | Frutos, Trinidad de; Martín-Nieto, José; Villalobo, Antonio CSIC ORCID | Fecha de publicación: | 1997 | Editor: | Walter de Gruyter | Citación: | Biological Chemistry 37881): 31-37 (1997) | Resumen: | Detergent-permeabilized EGFR-T17 fibroblasts, which overexpress the human epidermal growth factor (EGF) receptor, phosphorylate both poly-L-(glutamic acid, tyrosine) and exogenous calmodulin in an EGF-stimulated manner. Phosphorylation of calmodulin requires the presence of cationic polypeptides, such as poly-L-(lysine) or histones, which exert a biphasic effect toward calmodulin phosphorylation. Optimum cationic polypeptide/calmodulin molar ratios of 0.3 and 7 were determined for poly-L-(lysine) and histones, respectively. Maximum levels of calmodulin phosphorylation were attained in the absence of free calcium, and a strong inhibition of this process was observed at very low concentrations (Ki = 0.2 μM) of this cation. The incorporation of phosphate into calmodulin occurred predominantly on tyrosine residue(s) and was stimulated 34-fold by EGF. | Versión del editor: | http://dx.doi.org/10.1515/bchm.1997.378.1.31 | URI: | http://hdl.handle.net/10261/79163 | DOI: | 10.1515/bchm.1997.378.1.31 | Identificadores: | doi: 10.1515/bchm.1997.378.1.31 issn: 1431-6730 e-issn: 1437-4315 |
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Phosphorylation of Calmodulin.pdf | 1,88 MB | Adobe PDF | Visualizar/Abrir |
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