MISC

2009年

Proteomic Approach to Fc epsilon RI Aggregation-Initiated Signal Transduction Cascade in Human Mast Cells

INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY
  • Kazuko Yamaoka
  • ,
  • Yoshimichi Okayama
  • ,
  • Osamu Kaminuma
  • ,
  • Kazufumi Katayama
  • ,
  • Akio Mori
  • ,
  • Hideki Tatsumi
  • ,
  • Sohichi Nemoto
  • ,
  • Takachika Hiroi

149
開始ページ
73
終了ページ
76
記述言語
英語
掲載種別
DOI
10.1159/000211376
出版者・発行元
KARGER

Background: Mast cells (MCs) play a central role in allergic reactions through high-affinity IgE receptor (Fc epsilon RI)-mediated responses. Many attempts have been performed to investigate MC functions, though molecular bases of the intracellular signaling cascade through Fc epsilon RI, 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 Fc epsilon RI 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 alpha, 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 Fc epsilon RI. Conclusion: Our present phosphoproteome data may provide the clue to understand the molecular mechanisms for the activation of human MCs. Copyright (c) 2009 S. Karger AG, Basel

Web of Science ® 被引用回数 : 16

リンク情報
DOI
https://doi.org/10.1159/000211376
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000266573000014&DestApp=WOS_CPL

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