JAK3 associates with the human interleukin 4 receptor and is tyrosine phosphorylated following receptor triggering.
Oncogene
; 10(9): 1757-61, 1995 May 04.
Article
em En
| MEDLINE
| ID: mdl-7538655
ABSTRACT
In human B cells, interleukin 4 (IL4) acts in regulating proliferation, antigen expression, isotype switching and differentiation. These different effects are mediated through the IL4R complex including the IL2R gamma chain (gamma c) and a specific p130/140 binding unit referred below as human Interleukin 4 Receptor (IL4-R). Here, we studied the signal transduction events following IL4R activation and leading to CD23 expression on resting B cells. We demonstrate that IL4R triggering induced the tyrosine phosphorylation of JAK3 and of a p170 protein. Coimmunoprecipitation of JAK3 with the IL4R suggests a physical association which exists prior to IL4R complex stimulation. Orthovanadate treatment, while having no effect on IL4-induced p130 phosphorylation, leads to the hyperphosphorylation of the p170 and inhibits IL4-induced CD23 expression. These suggest that two mandatory steps exist in early IL4 signaling one controlled by JAK3 activation and the other by the p170 phosphoprotein.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Tirosina Quinases
/
Linfócitos B
/
Proteínas Proto-Oncogênicas
/
Receptores de Interleucina
Tipo de estudo:
Risk_factors_studies
Limite:
Child
/
Humans
Idioma:
En
Revista:
Oncogene
Assunto da revista:
BIOLOGIA MOLECULAR
/
NEOPLASIAS
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
França