In:
PLOS ONE, Public Library of Science (PLoS), Vol. 18, No. 3 ( 2023-3-29), p. e0282821-
Abstract:
Advancements in deep plasma proteomics are enabling high-resolution measurement of plasma proteoforms, which may reveal a rich source of novel biomarkers previously concealed by aggregated protein methods. Here, we analyze 188 plasma proteomes from non-small cell lung cancer subjects (NSCLC) and controls to identify NSCLC-associated protein isoforms by examining differentially abundant peptides as a proxy for isoform-specific exon usage. We find four proteins comprised of peptides with opposite patterns of abundance between cancer and control subjects. One of these proteins, BMP1, has known isoforms that can explain this differential pattern, for which the abundance of the NSCLC-associated isoform increases with stage of NSCLC progression. The presence of cancer and control-associated isoforms suggests differential regulation of BMP1 isoforms. The identified BMP1 isoforms have known functional differences, which may reveal insights into mechanisms impacting NSCLC disease progression.
Type of Medium:
Online Resource
ISSN:
1932-6203
DOI:
10.1371/journal.pone.0282821
DOI:
10.1371/journal.pone.0282821.g001
DOI:
10.1371/journal.pone.0282821.g002
DOI:
10.1371/journal.pone.0282821.s001
DOI:
10.1371/journal.pone.0282821.s002
DOI:
10.1371/journal.pone.0282821.s003
DOI:
10.1371/journal.pone.0282821.s004
DOI:
10.1371/journal.pone.0282821.s005
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2023
detail.hit.zdb_id:
2267670-3