A strong neutrophil elastase proteolytic fingerprint marks the carcinoma tumor proteome
PBN-AR
Instytucja
Centrum Onkologii - Instytut im. Marii Skłodowskiej-Curie
Informacje podstawowe
Główny język publikacji
en
Czasopismo
Molecular & Cellular Proteomics (45pkt w roku publikacji)
ISSN
1535-9476
EISSN
1535-9484
Wydawca
American Society for Biochemistry and Molecular Biology, American Society for Biochemistry and Molecular Biology
DOI
URL
Rok publikacji
2017
Numer zeszytu
2
Strony od-do
213-227
Numer tomu
16
Identyfikator DOI
Liczba arkuszy
0.7
Autorzy
(liczba autorów: 8)
Pozostali autorzy
+ 6
Streszczenia
Język
en
Treść
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 composed of a set of numerous protein fragments cleaved C-terminally to V, I, A, T, or C residues, significantly overrepresented in AC. A peptide set linked by a common VIATC cleavage consensus was the only prominent cancer-specific proteolytic fingerprint detected. This sequence consensus indicated neutrophil elastase as a source of the fingerprint. We also found that a large fraction 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 peptides that are possible markers of tumor-infiltrating neutrophil 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 analysis of large global proteomic analysis data sets as opposed to protein-wise analysis, in which outlier differential peptides are usually neglected
Inne
System-identifier
COI23be1c50582044eabdd5c0015e1503ee
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