| Autor: |
Yamaoka, Kazuko, Okayama, Yoshimichi, Kaminuma, Osamu, Katayama, Kazufumi, Mori, Akio, Tatsumi, Hideki, Nemoto, Sohichi, Hiroi, Takachika |
| Předmět: |
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| Zdroj: |
International Archives of Allergy & Immunology; 2009 Supplement 1, Vol. 149, p73-76, 4p, 1 Chart |
| Abstrakt: |
Background: Mast cells (MCs) play a central role in allergic reactions through high-affinity IgE receptor (FcεRI)-mediated responses. Many attempts have been performed to investigate MC functions, though molecular bases of the intracellular signaling cascade through FcεRI, especially in human MCs, remain scant and unexplored. Methods: Human MCs were differentiated from CD34+ cells by culture with stem cell factor, IL-6 and IL-3. The differential phosphorylation profiles of protein tyrosine residues in the resulting MCs with or without FcεRI aggregation were examined by two-dimensional gel electrophoresis. The candidate phosphoproteins of interest were picked, in-gel digested and mass spectrometry fingerprinted. Results: Approximately 40 proteins in MCs were phosphorylated on their tyrosine residues in response to activation and some of them were identified. Particularly IL-31 receptor α, solute carrier family 39, syntaxin 5 and heterogeneous nuclear ribonucleoprotein are newly identified as phosphoproteins that are potentially involved in the MC signaling cascade through FcεRI. Conclusion: Our present phosphoproteome data may provide the clue to understand the molecular mechanisms for the activation of human MCs. Copyright © 2009 S. Karger AG, Basel [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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