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

Publikation

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

Wissenschaftlicher Artikel/Review - 29.05.2018

Sajic Tatjana, Claassen Manfred, Gillessen Sommer Silke, Omlin Aurelius, Malander Susanne, Niméus Emma, Friedrich Betty, Blattmann Peter, Chen Ru, Brentnall Teresa A, Pan Sheng, Sethi Atul, Hüttenhain Ruth, Schiess Ralph, Williams Evan G, Surinova Silvia, Arvaniti Eirini, Liu Yansheng, Aebersold Ruedi

Zitation

Sajic T, Claassen M, Gillessen Sommer S, Omlin A, Malander S, Niméus E, Friedrich B, Blattmann P, Chen R, Brentnall T, Pan S, Sethi A, Hüttenhain R, Schiess R, Williams E, Surinova S, Arvaniti E, Liu Y, Aebersold R. Similarities and Differences of Blood N-Glycoproteins in Five Solid Carcinomas at Localized Clinical Stage Analyzed by SWATH-MS. Cell Rep 2018; 23:2819-2831.e5.

Art

Wissenschaftlicher Artikel/Review (Englisch)

Zeitschrift

Cell Rep 2018; 23

Veröffentlichungsdatum

29.05.2018

eISSN (Online)

2211-1247

Seiten

2819-2831.e5

Kurzbeschreibung/Zielsetzung

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.