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

Journal Article · Thu Oct 01 00:00:00 EDT 2020 · Cell Reports

DOI:https://doi.org/10.1016/j.celrep.2020.108276· OSTI ID:2565844

Hu, Yingwei ^[1]; Pan, Jianbo; Shah, Punit; Ao, Minghui; Thomas, Stefani N.; Liu, Yang; Chen, Lijun; Schnaubelt, Michael; Clark, David J.; Rodriguez, Henry; Boja, Emily S.; Hiltke, Tara; Kinsinger, Christopher R.; Rodland, Karin D.; Li, Qing Kay; Qian, Jiang; Zhang, Zhen; Chan, Daniel W.; Zhang, Hui; Pandey, Akhilesh ; Paulovich, Amanda; Hoofnagle, Andrew; Zhang, Bing; Mani, D. R.; Liebler, Daniel C.; Ransohoff, David F.; Fenyo, David; Tabb, David L.; Levine, Douglas A.; Kuhn, Eric; White, Forest M.; Whiteley, Gordon A.; Zhu, Heng; Shih, Ie-Ming; Bavarva, Jasmin; McDermott, Jason E.; Whiteaker, Jeffrey; Ketchum, Karen A.; Clauser, Karl R.; Ruggles, Kelly; Elburn, Kimberly; Ding, Li; Hannick, Linda; Zimmerman, Lisa J.; Watson, Mark; Thiagarajan, Mathangi; Ellis, Matthew J.C.; Oberti, Mauricio; Mesri, Mehdi; Sanders, Melinda E.; Borucki, Melissa; Gillette, Michael A.; Snyder, Michael; Edwards, Nathan J.; Vatanian, Negin; Rudnick, Paul A.; McGarvey, Peter B.; Mertins, Philip; Townsend, R. Reid; Thangudu, Ratna R.; Smith, Richard D.; Rivers, Robert C.; Slebos, Robert J.C.; Payne, Samuel H.; Davies, Sherri R.; Cai, Shuang; Stein, Stephen E.; Carr, Steven A.; Skates, Steven J.; Madhavan, Subha; Liu, Tao; Chen, Xian; Zhao, Yingming; Wang, Yue; Shi, Zhiao

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1. Johns Hopkins University, Baltimore, MD (United States); Clinical Proteomic Tumor Analysis Consortium (CPTAC). et al.

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.

• Research Organization: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
• Sponsoring Organization: National Institutes of Health (NIH); USDOE
• Contributing Organization: Clinical Proteomic Tumor Analysis Consortium (CPTAC)
• Grant/Contract Number: AC05-76RL01830
• OSTI ID: 2565844
• Alternate ID(s): OSTI ID: 2565841
• Report Number(s): PNNL-SA--191200
• Journal Information: Cell Reports, Journal Name: Cell Reports Journal Issue: 3 Vol. 33; ISSN 2211-1247
• Publisher: Elsevier
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CPTAC
HGSC
glycoproteomics
glycosylationmass spectrometry
high-grade serous ovarian carcinoma
proteomics
tumor clusters