プロテオミクスを用いた細胞内リン酸化動態の計測

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  • 石濱 泰
    京都大学大学院薬学研究科
  • 今見 考志
    Department of Biochemistry and Molecular Biology, University of British Columbia

書誌事項

タイトル別名
  • Quantitation of Cellular Phosphorylation Dynamics by Phosphoproteomics Approaches
  • Symposium Review プロテオミクスを用いた細胞内リン酸化動態の計測
  • Symposium Review プロテオミクス オ モチイタ サイボウ ナイ リンサンカ ドウタイ ノ ケイソク

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抄録

  Reversible phosphorylation of proteins controlled by kinases and phosphatases is one of the most ubiquitous post-translational modifications, and regulates a variety of cell functions through cellular signal transduction pathways. These signals are involved in various diseases such as cancer and rheumatism, and often cause the disease itself or drive the progression. Quantitative phosphoproteomics based on liquid chromatography-tandem mass spectrometry combined with phosphopeptide enrichment and stable isotope labeling allows profiling thousands of phosphorylation sites on human proteins and has been applied to monitoring cellular phosphorylation dynamics induced by various growth factors, hormones and other perturbations including kinase inhibitors. Here, we employed these technologies to quantify the temporal response of phosphorylation dynamics in SKBR3 breast cancer cells to lapatinib, a kinase inhibitor for epidermal growth factor receptor (EGFR) and EGFR2 (also known as HER2). Among 4953 identified phosphopeptides from 1548 proteins, a small proportion (5-7%) was regulated at least twofold by 1-10 μM lapatinib. The results provide new insights into EGFR/HER2 regulation through region-specific phosphorylation, as well as a global view of the cellular signaling networks associated with the anti-breast cancer action of lapatinib.<br>

収録刊行物

  • 薬学雑誌

    薬学雑誌 134 (4), 521-527, 2014

    公益社団法人 日本薬学会

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