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高等学校化学研究 ›› 2015, Vol. 31 ›› Issue (1): 21-24.doi: 10.1007/s40242-014-4317-2

• Articles • 上一篇    下一篇

Mass Spectrometric Analysis Revealing Phosphorylation Modifications of Periostin

ZHAO Yueming1,3, SONG Lina1, LI Lingxia1, LI Xiao'ou3, SHI Qinghong1, HONG Xin1, GUO Jia1, FANG Ling1, HE Chengyan1, LI Hongjun1, ZHAO Haifeng2   

  1. 1. China-Japan Union Hospital of Jilin University, Changchun 130033, P. R. China;
    2. The First Affiliated Hospital of Jiamusi University, Jiamusi 154002, P. R. China;
    3. Tumor Hospital of Jilin Province, Changchun 130012, P. R. China
  • 收稿日期:2014-08-25 修回日期:2014-10-20 出版日期:2015-02-01 发布日期:2015-01-21
  • 通讯作者: HE Chengyan, E-mail:chengyanhe469@vip.sina.com E-mail:chengyanhe469@vip.sina.com
  • 基金资助:

    Supported by the National Natural Science Foundation of China(Nos.81472454, 31100930), the Natural Science Foundation of Jilin Provincial Science and Technology Department, China(Nos.2011713, 20090461, 20110739, 20130413017GH), the Natural Science Foundation of Heilongjiang Province, China(Nos.201000742, D201075, Gc09c317), the Natural Science Foundation of Jilin Provincial Development and Reform Commission, China(No.2013c026-5) and the Natural Science Foundation of Changchun Science and Technology Bureau, China(No.2011125).

Mass Spectrometric Analysis Revealing Phosphorylation Modifications of Periostin

ZHAO Yueming1,3, SONG Lina1, LI Lingxia1, LI Xiao'ou3, SHI Qinghong1, HONG Xin1, GUO Jia1, FANG Ling1, HE Chengyan1, LI Hongjun1, ZHAO Haifeng2   

  1. 1. China-Japan Union Hospital of Jilin University, Changchun 130033, P. R. China;
    2. The First Affiliated Hospital of Jiamusi University, Jiamusi 154002, P. R. China;
    3. Tumor Hospital of Jilin Province, Changchun 130012, P. R. China
  • Received:2014-08-25 Revised:2014-10-20 Online:2015-02-01 Published:2015-01-21
  • Contact: HE Chengyan, E-mail:chengyanhe469@vip.sina.com E-mail:chengyanhe469@vip.sina.com
  • Supported by:

    Supported by the National Natural Science Foundation of China(Nos.81472454, 31100930), the Natural Science Foundation of Jilin Provincial Science and Technology Department, China(Nos.2011713, 20090461, 20110739, 20130413017GH), the Natural Science Foundation of Heilongjiang Province, China(Nos.201000742, D201075, Gc09c317), the Natural Science Foundation of Jilin Provincial Development and Reform Commission, China(No.2013c026-5) and the Natural Science Foundation of Changchun Science and Technology Bureau, China(No.2011125).

摘要:

Human periostin was over-expressed in HEK293T cells, which was enriched by nickel ion affinity resin, and further purified by gel electrophoresis. Phosphopeptides contained in the tryptic digestion of the purified periostin were enriched by TiO2 affinity chromatography, and then analyzed by liquid chromatography-tandem mass spectrometry(LC-MS/MS). LC-MS/MS analysis reveals three phosphorylation modification sites of periostin at IKVIEGpSLQPIIK(682―694), pSLHEKLKQDK(498―507) and p[TT]VLYEC*C*PGYM*R(73―85). The established method could be a great help to profiling the phosphorylation status of periostin under different physiological environments, such as inflammatory and tumor micro-environments.

关键词: Mass spectrometry, Periostin, Phosphorylation

Abstract:

Human periostin was over-expressed in HEK293T cells, which was enriched by nickel ion affinity resin, and further purified by gel electrophoresis. Phosphopeptides contained in the tryptic digestion of the purified periostin were enriched by TiO2 affinity chromatography, and then analyzed by liquid chromatography-tandem mass spectrometry(LC-MS/MS). LC-MS/MS analysis reveals three phosphorylation modification sites of periostin at IKVIEGpSLQPIIK(682―694), pSLHEKLKQDK(498―507) and p[TT]VLYEC*C*PGYM*R(73―85). The established method could be a great help to profiling the phosphorylation status of periostin under different physiological environments, such as inflammatory and tumor micro-environments.

Key words: Mass spectrometry, Periostin, Phosphorylation