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An integrated proteomic and glycoproteomic approach uncovers differences in glycosylation occupancy from benign and malignant epithelial ovarian tumors
- Source :
- Clinical Proteomics, Vol 14, Iss 1, Pp 1-9 (2017), Clinical Proteomics
- Publication Year :
- 2017
- Publisher :
- Springer Science and Business Media LLC, 2017.
-
Abstract
- Background Epithelial ovarian carcinomas encompass a heterogeneous group of diseases with a poor 5-year survival rate. Serous carcinoma is the most common type. Most FDA-approved serum tumor markers are glycoproteins. These glycoproteins on cell surface or shed into the bloodstream could serve as therapeutic targets as well as surrogates of tumor. In addition to glycoprotein expressions, the analysis of protein glycosylation occupancy could be important for the understanding of cancer biology as well as the identification of potential glycoprotein changes in cancer. In this study, we used an integrated proteomics and glycoproteomics approach to analyze global glycoprotein abundance and glycosylation occupancy for proteins from high-grade ovarian serous carcinoma (HGSC) and serous cystadenoma, a benign epithelial ovarian tumor, by using LC–MS/MS-based technique. Methods Fresh-frozen ovarian HGSC tissues and benign serous cystadenoma cases were quantitatively analyzed using isobaric tags for relative and absolute quantitation for both global and glycoproteomic analyses by two dimensional fractionation followed by LC–MS/MS analysis using a Orbitrap Velos mass spectrometer. Results Proteins and N-linked glycosite-containing peptides were identified and quantified using the integrated global proteomic and glycoproteomic approach. Among the identified N-linked glycosite-containing peptides, the relative abundances of glycosite-containing peptide and the glycoprotein levels were compared using glycoproteomic and proteomic data. The glycosite-containing peptides with unique changes in glycosylation occupancies rather than the protein expression levels were identified. Conclusion In this study, we presented an integrated proteomics and glycoproteomics approach to identify changes of glycoproteins in protein expression and glycosylation occupancy in HGSC and serous cystadenoma and determined the changes of glycosylation occupancy that are associated with malignant and benign tumor tissues. Specific changes in glycoprotein expression or glycosylation occupancy have the potential to be used in the discrimination between benign and malignant epithelial ovarian tumors and to improve our understanding of ovarian cancer biology. Electronic supplementary material The online version of this article (doi:10.1186/s12014-017-9152-2) contains supplementary material, which is available to authorized users.
- Subjects :
- Proteomics
0301 basic medicine
Pathology
medicine.medical_specialty
Glycosylation
Serous carcinoma
Clinical Biochemistry
lcsh:Medicine
Biology
03 medical and health sciences
Ovarian tumor
chemistry.chemical_compound
0302 clinical medicine
medicine
Molecular Biology
chemistry.chemical_classification
Ovarian high-grade serous carcinoma
Research
lcsh:R
General Medicine
Glycoproteomics
medicine.disease
Serous Cystadenoma
3. Good health
030104 developmental biology
chemistry
030220 oncology & carcinogenesis
Cancer research
Molecular Medicine
Ovarian cancer
Glycoprotein
Subjects
Details
- ISSN :
- 15590275 and 15426416
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Clinical Proteomics
- Accession number :
- edsair.doi.dedup.....1eff19f9c5a653a1d7801c2c82864d00
- Full Text :
- https://doi.org/10.1186/s12014-017-9152-2