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Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS

Sajic, Tatjana ; Liu, Yansheng ; Arvaniti, Eirini ; Surinova, Silvia ; Williams, Evan G. ; Schiess, Ralph ; Hüttenhain, Ruth ; Sethi, Atul ; Pan, Sheng and Brentnall, Teresa A. , et al. (2018) In Cell Reports 23(9). p.5-2831
Abstract

Cancer is mostly incurable when diagnosed at a metastatic stage, making its early detection via blood proteins of immense clinical interest. Proteomic changes in tumor tissue may lead to changes detectable in the protein composition of circulating blood plasma. Using a proteomic workflow combining N-glycosite enrichment and SWATH mass spectrometry, we generate a data resource of 284 blood samples derived from patients with different types of localized-stage carcinomas and from matched controls. We observe whether the changes in the patient's plasma are specific to a particular carcinoma or represent a generic signature of proteins modified uniformly in a common, systemic response to many cancers. A quantitative comparison of the... (More)

Cancer is mostly incurable when diagnosed at a metastatic stage, making its early detection via blood proteins of immense clinical interest. Proteomic changes in tumor tissue may lead to changes detectable in the protein composition of circulating blood plasma. Using a proteomic workflow combining N-glycosite enrichment and SWATH mass spectrometry, we generate a data resource of 284 blood samples derived from patients with different types of localized-stage carcinomas and from matched controls. We observe whether the changes in the patient's plasma are specific to a particular carcinoma or represent a generic signature of proteins modified uniformly in a common, systemic response to many cancers. A quantitative comparison of the resulting N-glycosite profiles discovers that proteins related to blood platelets are common to several cancers (e.g., THBS1), whereas others are highly cancer-type specific. Available proteomics data, including a SWATH library to study N-glycoproteins, will facilitate follow-up biomarker research into early cancer detection. Sajic et al. perform a multi-tumor plasma proteomic study in which they enrich and analyze tissue-secreted plasma glycoproteins to examine blood protein changes in early-stage localized cancers. They demonstrate that many proteins secreted upon platelet activation are changed in several tissue carcinomas, whereas others have changes specific to a single carcinoma type.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
blood, carcinoma, glycoproteins, human clinical study, localized cancer, secreted, SWATH-mass spectrometry
in
Cell Reports
volume
23
issue
9
pages
5 - 2831
publisher
Cell Press
external identifiers
  • scopus:85047177528
  • pmid:29847809
ISSN
2211-1247
DOI
10.1016/j.celrep.2018.04.114
language
English
LU publication?
yes
id
bde9a99b-d694-48eb-9c9f-e0c0514ca4cf
date added to LUP
2018-06-04 10:12:11
date last changed
2024-03-01 20:14:57
@article{bde9a99b-d694-48eb-9c9f-e0c0514ca4cf,
  abstract     = {{<p>Cancer is mostly incurable when diagnosed at a metastatic stage, making its early detection via blood proteins of immense clinical interest. Proteomic changes in tumor tissue may lead to changes detectable in the protein composition of circulating blood plasma. Using a proteomic workflow combining N-glycosite enrichment and SWATH mass spectrometry, we generate a data resource of 284 blood samples derived from patients with different types of localized-stage carcinomas and from matched controls. We observe whether the changes in the patient's plasma are specific to a particular carcinoma or represent a generic signature of proteins modified uniformly in a common, systemic response to many cancers. A quantitative comparison of the resulting N-glycosite profiles discovers that proteins related to blood platelets are common to several cancers (e.g., THBS1), whereas others are highly cancer-type specific. Available proteomics data, including a SWATH library to study N-glycoproteins, will facilitate follow-up biomarker research into early cancer detection. Sajic et al. perform a multi-tumor plasma proteomic study in which they enrich and analyze tissue-secreted plasma glycoproteins to examine blood protein changes in early-stage localized cancers. They demonstrate that many proteins secreted upon platelet activation are changed in several tissue carcinomas, whereas others have changes specific to a single carcinoma type.</p>}},
  author       = {{Sajic, Tatjana and Liu, Yansheng and Arvaniti, Eirini and Surinova, Silvia and Williams, Evan G. and Schiess, Ralph and Hüttenhain, Ruth and Sethi, Atul and Pan, Sheng and Brentnall, Teresa A. and Chen, Ru and Blattmann, Peter and Friedrich, Betty and Niméus, Emma and Malander, Susanne and Omlin, Aurelius and Gillessen, Silke and Claassen, Manfred and Aebersold, Ruedi}},
  issn         = {{2211-1247}},
  keywords     = {{blood; carcinoma; glycoproteins; human clinical study; localized cancer; secreted; SWATH-mass spectrometry}},
  language     = {{eng}},
  month        = {{05}},
  number       = {{9}},
  pages        = {{5--2831}},
  publisher    = {{Cell Press}},
  series       = {{Cell Reports}},
  title        = {{Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS}},
  url          = {{http://dx.doi.org/10.1016/j.celrep.2018.04.114}},
  doi          = {{10.1016/j.celrep.2018.04.114}},
  volume       = {{23}},
  year         = {{2018}},
}