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Poster Presentations
Day 1, June 22（Sun.）
Room P (Maesato East, Foyer, Ocean Wing)
- 1P-PM-25
Large-scale profiling of protease and proteolysis in non-small cell lung cancer cell lines using protein terminomics
(1Kyoto Univ., Japan, 2Niigata Univ., Japan)
oRisa Chisaka1, Yuto Taniguchi1, Tatsuya Sagawa1, Kaho Takamuro1, Ayana Tomioka1, Hiroshi Nishida1, Shujiro Okuda2, Yasushi Ishihama1
Proteolysis (protein hydrolysis by proteases) is an important regulatory mechanism involved in protein activity and stability, and its abnormalities are known to lead to the development of various diseases. Although analyses focusing on genomics and splicing have been performed, large-scale analysis of proteolysis-terminal peptides has not been performed. In this study, we performed a large-scale analysis of several non-small cell lung cancer cell lines, combining global proteome analysis with terminome analysis using the CHromatographic AMplification of Protein terminal peptides (CHAMP) method. We attempted to elucidate the regulatory mechanism of proteolysis for each subtype by performing both data-dependent acquisition mode (DDA) and data-independent acquisition mode (DIA).
Hierarchical clustering of proteolysis-terminal peptides was performed based on quantitative values. The proteolysis terminal sequences in each cluster and the cleavage selectivity of the protease for the substrate sequence were used to obtain a Position Weight Matrix (PWM) score defined between one protease and one substrate to search for a candidate responsible protease for each terminal peptide. The results, as measured by DDA, suggested that the activity of a specific group of proteases was commonly enhanced in the four cell lines with EGFR mutations.