Identification of tyrosine-phosphorylated proteins associated with lung cancer metastasis using label-free quantitative analyses

Hsin Yi Wu, Vincent S. Tseng, Lien Chin Chen, Hui Yin Chang, I. Chi Chuang, Yeou Guang Tsay, Pao-Chi Liao

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13 Citations (Scopus)

Abstract

Lung cancer is a lethal disease, and early metastasis is the major cause of treatment failure and cancer-related death. Tyrosine phosphorylated (P-Tyr) proteins are involved in the invasive and metastatic behavior of lung cancer; however, only a limited number of targets were identified. We attempt to characterize P-Tyr proteins and events involved in the metastatic process. In a previous work, we have developed a strategy for identification of protein phosphorylation. Here, this strategy was used to characterize the tyrosine phosphoproteome of lung cancer cells that have different invasive abilities (CL1-0 vs. CL1-5). Using our analytical strategy, we report the identification of 335 P-Tyr sites from 276 phosphoproteins. Label-free quantitative analysis revealed that 36 P-Tyr peptides showed altered levels between CL1-0 and CL1-5 cells. From this list of sites, we extracted two novel consensus sequences and four known motifs for specific kinases and phosphatases including EGFR, Src, JAK2, and TC-PTP. Protein-protein interaction network analysis of the altered P-Tyr proteins illustrated that 11 proteins were linked to a network containing EGFR, c-Src, c-Myc, and STAT, which is known to be related to lung cancer metastasis. Among these 11 proteins, 7 P-Tyr proteins have not been previously reported to be associated with lung cancer metastasis and are of greatest interest for further study. The characterized tyrosine phosphoproteome and altered P-Tyr targets may provide a better comprehensive understanding of the mechanisms of lung cancer invasion/metastasis and discover potential therapies.

Original languageEnglish
Pages (from-to)4102-4112
Number of pages11
JournalJournal of Proteome Research
Volume9
Issue number8
DOIs
Publication statusPublished - 2010 Aug 6

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Chemistry(all)

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