Abstract
Most cytokines stimulate the p21ras pathway, leading to MAP kinase activation. One exception is interleukin-4 (IL-4), which has been shown not to activate this pathway in hematopoietic cells. However, IL-4 acts on a broad range of cells, including keratinocytes, in which it induces IL-6 production. We report here that IL-4 stimulation of human keratinocytic cell lines or primary cultures activates MAP kinase. In these cells, IL-4 stimulation induces the tyrosine phosphorylation of p42/44 MAP kinase as well as its catalytic activity. We also observed an increased phosphorylation of p46shc, an SH2-containing protein involved in the Ras pathway, as a result of IL-4 stimulation in human keratinocytic cell lines but not in T lymphocytes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing*
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Adaptor Proteins, Vesicular Transport*
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Cells, Cultured
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Humans
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Interleukin-4 / pharmacology*
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Keratinocytes / metabolism
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Lymphocyte Activation
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Phosphorylation
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Phosphotyrosine / metabolism*
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Proteins / metabolism*
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Recombinant Proteins
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Shc Signaling Adaptor Proteins
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Signal Transduction
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Src Homology 2 Domain-Containing, Transforming Protein 1
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T-Lymphocytes / metabolism
Substances
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Adaptor Proteins, Signal Transducing
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Adaptor Proteins, Vesicular Transport
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Proteins
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Recombinant Proteins
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SHC1 protein, human
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Shc Signaling Adaptor Proteins
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Src Homology 2 Domain-Containing, Transforming Protein 1
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Interleukin-4
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Phosphotyrosine
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Calcium-Calmodulin-Dependent Protein Kinases