JPOST Repositoryapplication/xmlhttps://storage.jpostdb.org/JPST003905/files/RAW_MS_Proteome.csvhttps://storage.jpostdb.org/JPST003905/files/RAW_MS_Phospho.csvhttps://storage.jpostdb.org/JPST003905/files/N-Un_RC5_1_6744.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-PO4_RC4_1_6717.d.ziphttps://storage.jpostdb.org/JPST003905/files/N-PO4_RC1_1_6729.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-Un_RC8_1_6759.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-Un_RC7_1_6755.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-Un_RC7_1_6752.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-PO4_RC3_1_6722.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-Un_RC7_1_6754.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-PO4_RC4_1_6716.d.ziphttps://storage.jpostdb.org/JPST003905/files/N-Un_RC5_1_6742.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-PO4_RC3_1_6721.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-Un_RC8_1_6758.d.ziphttps://storage.jpostdb.org/JPST003905/files/N-Un_RC5_1_6743.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-PO4_RC4_1_6714.d.ziphttps://storage.jpostdb.org/JPST003905/files/N-PO4_RC1_1_6730.d.ziphttps://storage.jpostdb.org/JPST003905/files/N-PO4_RC1_1_6731.d.ziphttps://storage.jpostdb.org/JPST003905/files/C3M-Un_RC8_1_6757.d.ziphttps://storage.jpostdb.org/JPST003905/files/C2H-PO4_RC3_1_6720.d.zipprimaryOK200Proteomics(1) Dr. Churat Weeraphan, (2) Assoc. Prof. Dr. Supinya Thanapongpichat and (3) Assoc. Prof. Dr. Hansuk BuncherdHomo Sapiens (human)https://repository.jpostdb.org/entry/JPST003905Chulabhorn Research InstitutejPOSTfalsePhosphorylated filamin-A at Serine 1459 from plasma-derived small extracellular vesicles as a promising biomarker for high-risk adenoma and colorectal cancerParallel proteomic and phosphoproteomic analyses were conducted on plasma-derived small extracellular vesicles (sEVs) obtained from healthy individuals with negative colonoscopy (N), patients with advanced precancerous polyps (high-risk adenoma; HRA), and patients with colorectal cancer (CRC). In the discovery cohort, plasma samples were processed for sEV isolation using size-exclusion chromatography. The sEV isolates were digested with mass spectrometry-grade trypsin, and the resulting peptides were quantified using the Pierce Quantitative Colorimetric Peptide Assay. Peptides from each group (n = 10) were pooled, and 100 µg of the pooled peptides were aliquoted for phosphopeptide enrichment using the ProteoExtract Phosphopeptide Enrichment TiO2 Kit. Both the enriched phosphopeptides and corresponding unenriched peptides were analyzed in parallel using label-free quantitative mass spectrometry in three technical replicates. Findings were validated in individual samples (n = 50) through immunoblot analysis in the validation cohort.Mon Apr 06 00:00:00 BST 2026PXD0656829606