Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Label-Free Quantitative Proteomics and N-terminal Analysis of Human Metastatic Lung Cancer Cells

  • Min, Hophil (Department of Biomedical Sciences, Medical Research Center, Seoul National University College of Medicine) ;
  • Han, Dohyun (Department of Biomedical Sciences, Medical Research Center, Seoul National University College of Medicine) ;
  • Kim, Yikwon (Department of Biomedical Sciences, Medical Research Center, Seoul National University College of Medicine) ;
  • Cho, Jee Yeon (Division of Life Sciences and Biotechnology, Korea University) ;
  • Jin, Jonghwa (Department of Biomedical Sciences, Medical Research Center, Seoul National University College of Medicine) ;
  • Kim, Youngsoo (Department of Biomedical Sciences, Medical Research Center, Seoul National University College of Medicine)
  • Received : 2014.02.20
  • Accepted : 2014.04.08
  • Published : 2014.06.30
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Abstract

Proteomic analysis is helpful in identifying cancerassociated proteins that are differentially expressed and fragmented that can be annotated as dysregulated networks and pathways during metastasis. To examine metastatic process in lung cancer, we performed a proteomics study by label-free quantitative analysis and N-terminal analysis in 2 human non-small-cell lung cancer cell lines with disparate metastatic potentials - NCI-H1703 (primary cell, stage I) and NCI-H1755 (metastatic cell, stage IV). We identified 2130 proteins, 1355 of which were common to both cell lines. In the label-free quantitative analysis, we used the NSAF normalization method, resulting in 242 differential expressed proteins. For the N-terminal proteome analysis, 325 N-terminal peptides, including 45 novel fragments, were identified in the 2 cell lines. Based on two proteomic analysis, 11 quantitatively expressed proteins and 8 N-terminal peptides were enriched for the focal adhesion pathway. Most proteins from the quantitative analysis were upregulated in metastatic cancer cells, whereas novel fragment of CRKL was detected only in primary cancer cells. This study increases our understanding of the NSCLC metastasis proteome.

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References

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