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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-AM-42
Peptidomic analysis of mouse tissues
(1Sch. Sci., Kitasato Univ., 2Sch. Med., Kitasato Univ., 3Cent. Disease Proteomics, Sch. Sci., Kitasato Univ., 4Kazusa DNA Research Institute)
oYusei Okuda1, Makoto Itakura2,3, Ryo Konno4, Tomomi Taguchi2, Takeshi Miyatsuka2, Takashi Matsui1,3, Yusuke Kawashima4, Yoshio Kodera1,3
In recent years, proteomics has made significant progress due to advances in mass spectrometry and data analysis techniques, but peptidomics has remained limited in its progress mainly due to difficulties in sample preparation and data analysis. To address these issues, we developed the differential solubilization (DS) method, an efficient peptide extraction method for plasma. Based on this method, we adapted the DS method to a small amount of frozen tissues, successfully identifying 1,535 peptides, including 35 bioactive peptides, from 0.5 mg of frozen mouse hypothalamus. However, unremoved protein components were found to limit the identification of peptides.
In this study, we improved the DS method to efficiently remove protein components. Using this improved method, we extracted peptides from eleven frozen mouse tissues: lung, spleen, kidney, liver, heart, muscle, adrenal gland, pancreas, cerebellum, hippocampus, and cerebral cortex. The extracted peptides were analyzed using timsTOF HT system and identified using PEAKS Studio 12. As a result, we identified 53,310 peptides from 6,500 proteins across the eleven tissues. Of these peptides, 3,701 peptides were derived from 75 prohormone proteins, and 72 peptides were as known bioactive peptides annotated as 'Peptide' in UniProt. In this presentation, comprehensive peptidome analysis data will be discussed.