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

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...

Full description

Bibliographic Details
Main Authors: Tatjana Sajic, Yansheng Liu, Eirini Arvaniti, Silvia Surinova, Evan G. Williams, Ralph Schiess, Ruth Hüttenhain, Atul Sethi, Sheng Pan, Teresa A. Brentnall, Ru Chen, Peter Blattmann, Betty Friedrich, Emma Niméus, Susanne Malander, Aurelius Omlin, Silke Gillessen, Manfred Claassen, Ruedi Aebersold
Format: Article
Language:English
Published: Elsevier 2018-05-01
Series:Cell Reports
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124718307149
_version_ 1828975118109376512
author Tatjana Sajic
Yansheng Liu
Eirini Arvaniti
Silvia Surinova
Evan G. Williams
Ralph Schiess
Ruth Hüttenhain
Atul Sethi
Sheng Pan
Teresa A. Brentnall
Ru Chen
Peter Blattmann
Betty Friedrich
Emma Niméus
Susanne Malander
Aurelius Omlin
Silke Gillessen
Manfred Claassen
Ruedi Aebersold
author_facet Tatjana Sajic
Yansheng Liu
Eirini Arvaniti
Silvia Surinova
Evan G. Williams
Ralph Schiess
Ruth Hüttenhain
Atul Sethi
Sheng Pan
Teresa A. Brentnall
Ru Chen
Peter Blattmann
Betty Friedrich
Emma Niméus
Susanne Malander
Aurelius Omlin
Silke Gillessen
Manfred Claassen
Ruedi Aebersold
author_sort Tatjana Sajic
collection DOAJ
description 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.
first_indexed 2024-12-14T14:15:24Z
format Article
id doaj.art-f69a33aae6bb4289a7cf96673277a7c8
institution Directory Open Access Journal
issn 2211-1247
language English
last_indexed 2024-12-14T14:15:24Z
publishDate 2018-05-01
publisher Elsevier
record_format Article
series Cell Reports
spelling doaj.art-f69a33aae6bb4289a7cf96673277a7c82022-12-21T22:58:13ZengElsevierCell Reports2211-12472018-05-0123928192831.e510.1016/j.celrep.2018.04.114Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MSTatjana Sajic0Yansheng Liu1Eirini Arvaniti2Silvia Surinova3Evan G. Williams4Ralph Schiess5Ruth Hüttenhain6Atul Sethi7Sheng Pan8Teresa A. Brentnall9Ru Chen10Peter Blattmann11Betty Friedrich12Emma Niméus13Susanne Malander14Aurelius Omlin15Silke Gillessen16Manfred Claassen17Ruedi Aebersold18Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandDepartment of Pharmacology, Cancer Biology Institute, Yale University School of Medicine, West Haven, CT 06516, USADepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandUCL Cancer Institute, University College London, London, UKDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandProteoMediX AG, 8952 Schlieren, SwitzerlandDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158, USADepartment of Biomedicine, University of Basel/University Hospital Basel, and Swiss Institute of Bioinformatics, Basel, SwitzerlandThe Brown Foundation Institute of Molecular Medicine, The University of Texas Health Science Center at Houston, 1825 Pressler, Houston, TX 77030, USADepartment of Medicine, University of Washington, Seattle, WA 98195, USADepartment of Medicine, University of Washington, Seattle, WA 98195, USADepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandDepartment of Clinical Sciences Lund, Surgery, Oncology and Pathology, Lund University, and Skåne University Hospital, Department of Surgery, Lund, SwedenDepartment of Clinical Sciences Lund, Oncology and Pathology, Lund University, and Skåne University Hospital, Department of Oncology, Lund, SwedenDepartment of Oncology and Hematology, Kantonsspital St. Gallen, St. Gallen, SwitzerlandDepartment of Oncology and Hematology, Kantonsspital St. Gallen, St. Gallen, SwitzerlandDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandDepartment of Biology, Institute of Molecular Systems Biology, ETH Zurich, 8093 Zurich, SwitzerlandCancer 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.http://www.sciencedirect.com/science/article/pii/S2211124718307149carcinomalocalized cancerbloodglycoproteinssecretedSWATH-mass spectrometryhuman clinical study
spellingShingle Tatjana Sajic
Yansheng Liu
Eirini Arvaniti
Silvia Surinova
Evan G. Williams
Ralph Schiess
Ruth Hüttenhain
Atul Sethi
Sheng Pan
Teresa A. Brentnall
Ru Chen
Peter Blattmann
Betty Friedrich
Emma Niméus
Susanne Malander
Aurelius Omlin
Silke Gillessen
Manfred Claassen
Ruedi Aebersold
Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
Cell Reports
carcinoma
localized cancer
blood
glycoproteins
secreted
SWATH-mass spectrometry
human clinical study
title Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
title_full Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
title_fullStr Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
title_full_unstemmed Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
title_short Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS
title_sort similarities and differences of blood n glycoproteins in five solid carcinomas at localized clinical stage analyzed by swath ms
topic carcinoma
localized cancer
blood
glycoproteins
secreted
SWATH-mass spectrometry
human clinical study
url http://www.sciencedirect.com/science/article/pii/S2211124718307149
work_keys_str_mv AT tatjanasajic similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT yanshengliu similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT eiriniarvaniti similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT silviasurinova similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT evangwilliams similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT ralphschiess similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT ruthhuttenhain similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT atulsethi similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT shengpan similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT teresaabrentnall similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT ruchen similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT peterblattmann similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT bettyfriedrich similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT emmanimeus similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT susannemalander similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT aureliusomlin similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT silkegillessen similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT manfredclaassen similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms
AT ruediaebersold similaritiesanddifferencesofbloodnglycoproteinsinfivesolidcarcinomasatlocalizedclinicalstageanalyzedbyswathms