PXD003794

PXD003794 is an original dataset announced via ProteomeXchange.

Title	Glycomic and proteomic analyses of malignant ascites fluid were used to identify potential metastatic biomarkers of epithelial ovarian cancer : Partial
Description	Ovarian cancer is a major cause of cancer mortality among women largely due to late diagnosis of advanced stage metastatic disease. More extensive molecular analysis of metastatic ovarian cancer is needed to identify post-translational modifications of proteins particularly associated with metastatic disease so that we can better understand the metastatic process and identify potential therapeutic targets. Proteins are the target of many recently developed cancer treatments, but an often neglected aspect of biomarker discovery is protein glycosylation, especially those involving tumor-associated carbohydrate antigens (TACAs) such as sialyl-Lewis(x) (SLe(x) and sialyl-Lewis(a) (SLe(a), which have been identified in various cancers. Although it is already known that considerable changes in protein glycosylation are major contributors to the initiation, progression and metastasis of tumors, specifics about glycosylation changes particularly important to the metastatic process are still lacking. In this report we describe the results of a combined glycomic and proteomic study of metastatic ovarian cancer (OC) ascites fluids. Glycoproteins in ascites fluid were enriched by affinity binding to lectins (ConA or WGA) and other affinity matrices. Separate glycomic and proteomic analyses were performed as well as glycopeptide analyses. Relative abundances of different N-glycan groups and proteins were identified from original ascites fluids and corresponding lectin bound samples. Levels of biomarkers CA125, MUC1 and fibronectin were also monitored in these samples by Western blot analysis. N-glycan analysis of ascites fluids showed the presence of large, highly fucosylated and sialylated, complex and hybrid glycans, some of which were not observed in normal serum. Proteins in OC ascites that were more abundant or not present in the serum control, were haptoglobin, fibronectin, lumican, fibulin, hemopexin, ceruloplasmin, alpha-1-antitrypsin and alpha-1-antichymotrypsin. Glycopeptide analysis identified N- and O-glycans in clusterin, hemopexin, and fibulin that were present in OC ascites.
HostingRepository	PRIDE
AnnounceDate	2016-08-15
AnnouncementXML	Submission_2016-08-15_01:57:23.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Brett Phinney
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	iodoacetamide derivatized residue
Instrument	LTQ FT; LTQ

Revision	Datetime	Status	ChangeLog Entry
0	2016-03-16 02:55:12	ID requested
⏵ 1	2016-08-15 01:57:25	announced

Miyamoto S, Ruhaak LR, Stroble C, Salemi MR, Phinney B, Lebrilla CB, Leiserowitz GS, Glycoproteomic Analysis of Malignant Ovarian Cancer Ascites Fluid Identifies Unusual Glycopeptides. J Proteome Res, 15(9):3358-76(2016) [pubmed]

curator keyword: Biomedical

submitter keyword: ascites,concanavalin A,epithelial ovarian cancer

Brett Phinney
contact affiliation	UC Davis Proteomics Core
contact email	bsphinney@ucdavis.edu
lab head
Brett Phinney
contact affiliation	UC Davis Proteomics Core
contact email	bsphinney@ucdavis.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003794
     1. Label: PRIDE project
     2. Name: Glycomic and proteomic analyses of malignant ascites fluid were used to identify potential metastatic biomarkers of epithelial ovarian cancer : Partial