Integrated Proteomic and Glycoproteomic Characterization of Human High-Grade Serous Ovarian Carcinoma

Clinical Proteomic Tumor Analysis Consortium

Research output: Contribution to journalArticlepeer-review

35 Scopus citations


Many gene products exhibit great structural heterogeneity because of an array of modifications. These modifications are not directly encoded in the genomic template but often affect the functionality of proteins. Protein glycosylation plays a vital role in proper protein functions. However, the analysis of glycoproteins has been challenging compared with other protein modifications, such as phosphorylation. Here, we perform an integrated proteomic and glycoproteomic analysis of 83 prospectively collected high-grade serous ovarian carcinoma (HGSC) and 23 non-tumor tissues. Integration of the expression data from global proteomics and glycoproteomics reveals tumor-specific glycosylation, uncovers different glycosylation associated with three tumor clusters, and identifies glycosylation enzymes that were correlated with the altered glycosylation. In addition to providing a valuable resource, these results provide insights into the potential roles of glycosylation in the pathogenesis of HGSC, with the possibility of distinguishing pathological outcomes of ovarian tumors from non-tumors, as well as classifying tumor clusters.

Original languageEnglish (US)
Article number108276
JournalCell reports
Issue number3
StatePublished - Oct 20 2020

Bibliographical note

Funding Information:
This work was supported by the National Cancer Institute (NCI) Clinical Proteomic Tumor Analysis Consortium (CPTAC; grants U24CA160036 and U24CA210985 ).

Publisher Copyright:
© 2020 The Authors


  • HGSC
  • glycoproteomics
  • glycosylation
  • high-grade serous ovarian carcinoma
  • mass spectrometry
  • proteomics
  • tumor clusters


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