Kistowski, Michal and Dębski, Janusz and Karczmarski, Jakub and Paziewska, Agnieszka and Olędzki, Jacek and Mikula, Michał and Ostrowski, Jerzy and Dadlez, Michal (2017) A Strong Neutrophil Elastase Proteolytic Fingerprint Marks the Carcinoma Tumor Proteome. Molecular & Cellular Proteomics, 16 (2). pp. 213-227.
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Abstract
Proteolytic cascades are deeply involved in critical stages of cancer progression. During the course of peptide-wise analysis of shotgun proteomic data sets representative of colon adenocarcinoma (AC) and ulcerative colitis (UC), we detected a cancer-specific proteolytic fingerprint com- posed of a set of numerous protein fragments cleaved C-terminally to V, I, A, T, or C residues, significantly over-represented in AC. A peptide set linked by a common VIATC cleavage consensus was the only prominent can- cer-specific proteolytic fingerprint detected. This se- quence consensus indicated neutrophil elastase as a source of the fingerprint. We also found that a large frac- tion of affected proteins are RNA processing proteins associated with the nuclear fraction and mostly cleaved within their functionally important RNA-binding domains. Thus, we detected a new class of cancer-specific pep- tides that are possible markers of tumor-infiltrating neu- trophil activity, which often correlates with the clinical outcome. Data are available via ProteomeXchange with identifiers: PXD005274 (Data set 1) and PXD004249 (Data set 2). Our results indicate the value of peptide-wise anal- ysis of large global proteomic analysis data sets as op- posed to protein-wise analysis, in which outlier differen- tial peptides are usually neglected.
Item Type: | Article |
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Subjects: | Q Science > QR Microbiology |
Divisions: | Mass Spectrometry Laboratory |
ID Code: | 1413 |
Deposited By: | Michał Kistowski |
Deposited On: | 09 Nov 2017 09:53 |
Last Modified: | 08 Mar 2018 15:34 |
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