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Mass spectrometric analysis revealing phosphorylation modifications of periostin

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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.

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Authors and Affiliations

  1. China-Japan Union Hospital of Jilin University, Changchun, 130033, P. R. China

    Yueming Zhao, Lina Song, Lingxia Li, Qinghong Shi, Xin Hong, Jia Guo, Ling Fang, Chengyan He & Hongjun Li

  2. The First Affiliated Hospital of Jiamusi University, Jiamusi, 154002, P. R. China

    Haifeng Zhao

  3. Tumor Hospital of Jilin Province, Changchun, 130012, P. R. China

    Yueming Zhao & Xiao’ou Li

Authors
  1. Yueming Zhao
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  2. Lina Song
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  3. Lingxia Li
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  4. Xiao’ou Li
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  5. Qinghong Shi
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  6. Xin Hong
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  7. Jia Guo
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  8. Ling Fang
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  9. Chengyan He
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  10. Hongjun Li
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  11. Haifeng Zhao
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Corresponding author

Correspondence to Chengyan He.

Additional information

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).

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Zhao, Y., Song, L., Li, L. et al. Mass spectrometric analysis revealing phosphorylation modifications of periostin. Chem. Res. Chin. Univ. 31, 21–24 (2015). https://doi.org/10.1007/s40242-014-4317-2

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  • DOI: https://doi.org/10.1007/s40242-014-4317-2

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