›› 2013, Vol. 40 ›› Issue (6): 53-57.

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Proteomic Analysis of the Nuclear Phosphorylated Proteins in Diary Cow Mammary Epithelial Cells Treated with Methionine

LU Li-min, LI Qing-zhang, HUANG Jian-guo, LIU Rong, WANG Jia-li, JIN Xin, GAO Xue-jun    

  1. Key Laboratory of Dairy Science, Ministry of Education, Northeast Agricultural University, Harbin 150030, China
  • Received:2012-10-10 Online:2013-06-20 Published:2013-06-20

Abstract: To reveal the major protein related to milk protein synthesis in nucleus of mammary gland epithelial cells and further uncover the mechanism of milk protein synthesis in post-transcription level, two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization/time of flight mass spectrometry (MALDI-TOF-MS) were used to identify the changes of nuclear phosphorylated proteins in DCMECs treated with methionine, and their expression changes were verified by Western blotting analysis in the current study. 5 up-regulated expressed phosphoproteins included staphylococcal nuclease domain-containing protein 1, Septin-6, Glycyl tRNA synthetase, Twinfilin-1 and eukaryotic elongation factor 1-beta. They contributed to multiple functional activities such as DNA transcription, mRNA translation, protein synthesis, cell cycle, cell division and morphological processes.

Key words: nuclear; phosphorylated protein; 2-DE; diary cow; mammary epithelial cells

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