RRC ID 6604
著者 Yamaoka K, Okayama Y, Kaminuma O, Katayama K, Mori A, Tatsumi H, Nemoto S, Hiroi T.
タイトル Proteomic Approach to FcepsilonRI aggregation-initiated signal transduction cascade in human mast cells.
ジャーナル Int Arch Allergy Immunol
Abstract BACKGROUND:Mast cells (MCs) play a central role in allergic reactions through high-affinity IgE receptor (FcepsilonRI)-mediated responses. Many attempts have been performed to investigate MC functions, though molecular bases of the intracellular signaling cascade through FcepsilonRI, 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 FcepsilonRI 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 FcepsilonRI.
CONCLUSION:Our present phosphoproteome data may provide the clue to understand the molecular mechanisms for the activation of human MCs.
巻・号 149 Suppl 1
ページ 73-6
公開日 2009-1-1
DOI 10.1159/000211376
PII 000211376
PMID 19494509
MeSH Cation Transport Proteins / metabolism Heterogeneous-Nuclear Ribonucleoproteins / metabolism Humans Mast Cells / metabolism* Phosphoproteins / metabolism* Phosphorylation Proteomics Qa-SNARE Proteins / metabolism Receptors, IgE / metabolism* Receptors, Interleukin / metabolism Signal Transduction* Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Tyrosine / metabolism*
IF 2.917
引用数 16
WOS 分野 ALLERGY IMMUNOLOGY
リソース情報
ヒト・動物細胞