Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/78573
COMPARTIR / EXPORTAR:
SHARE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Calmodulin inhibits the epidermal growth factor receptor tyrosine kinase |
Autor: | San José, Esteban; Benguria, Alberto CSIC ORCID; Geller, P.; Villalobo, Antonio CSIC ORCID | Fecha de publicación: | 1992 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 267(21): 15237-15245 (1992) | Resumen: | We demonstrate in this report that the epidermal growth factor (EGF) receptor from rat liver can be isolated by calmodulin affinity chromatography by binding in the presence of Ca2+ and elution with a Ca2+-chelating agent. The bulk of the EGF receptor is not eluted by a NaCl gradient in the presence of Ca2+. We ascertained the identity of the isolated receptor by immunoblot and immunoprecipitation using a polyclonal antibody against an EGF receptor from human origin. The purified receptor is autophosphorylated in tyrosine residues in an EGF-stimulated manner, and EGF-dependent phosphorylation of serine residues was also detected. Both the EGF and the transforming growth factor-α stimulate the tyrosine-directed protein kinase activity of the isolated receptor with similar affinities. Furthermore, we demonstrate that calmodulin inhibits the EGF-dependent tyrosine-directed protein kinase activity associated to the receptor in a concentration- dependent manner. This inhibition is partially Ca2+ dependent and is not displaced by increasing the concentration of EGF up to an EGF/calmodulin ratio of 10 (mol/mol). In addition, calmodulin was phosphorylated in an EGF- stimulated manner in the presence of a basic protein (histone) as cofactor and in the absence, but not in the presence, of Ca2+. | URI: | http://hdl.handle.net/10261/78573 | Identificadores: | issn: 0021-9258 e-issn: 1083-351X |
Aparece en las colecciones: | (IIBM) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
Page view(s)
257
checked on 23-abr-2024
Download(s)
40
checked on 23-abr-2024
Google ScholarTM
Check
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.