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Start Over Author "Rolling C" Topic receptors, interleukin
2 results on '"Rolling C"'

1. IL4 and IL13 receptors share the gamma c chain and activate STAT6, STAT3 and STAT5 proteins in normal human B cells.

Author

Rolling C, Treton D, Pellegrini S, Galanaud P, and Richard Y

Subjects
Antigens, CD chemistry, B-Lymphocytes immunology, Child, Humans, Immunoglobulin Constant Regions immunology, Immunoglobulin gamma-Chains immunology, Interleukin-13 metabolism, Interleukin-13 Receptor alpha1 Subunit, Interleukin-4 metabolism, Janus Kinase 1, Janus Kinase 3, Phosphorylation, Protein-Tyrosine Kinases metabolism, Receptors, Interleukin chemistry, Receptors, Interleukin-13, Receptors, Interleukin-2 immunology, Receptors, Interleukin-4, Recombinant Proteins metabolism, STAT3 Transcription Factor, STAT5 Transcription Factor, STAT6 Transcription Factor, Time Factors, Tyrosine metabolism, Antigens, CD metabolism, B-Lymphocytes metabolism, DNA-Binding Proteins metabolism, Milk Proteins, Receptors, Interleukin metabolism, Trans-Activators metabolism
Abstract

IL13 induces the same biological effects as IL4 in normal human B cells. We show that as in the IL4R complex, both IL4R alpha and IL2R gamma c are components of the IL13R and that both cytokines induced STAT6, STAT3 and STAT5 activation in B cells. In spite of this similar downstream signalling, IL4 and IL13 used a different set of Janus kinases: IL13 is unable to activate JAK1 and JAK3.

Published
1996
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2. JAK3 associates with the human interleukin 4 receptor and is tyrosine phosphorylated following receptor triggering.

Author

Rolling C, Treton D, Beckmann P, Galanaud P, and Richard Y

Subjects
Child, Humans, Interleukin-4 pharmacology, Janus Kinase 2, Janus Kinase 3, Lymphocyte Activation, Palatine Tonsil, Phosphorylation, Phosphotyrosine, Receptors, Interleukin-4, Signal Transduction, Tyrosine analogs & derivatives, Tyrosine metabolism, B-Lymphocytes metabolism, Protein-Tyrosine Kinases metabolism, Proto-Oncogene Proteins, Receptors, Interleukin metabolism
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.

Published
1995

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