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Updated: Aug 2, 2025
The Use of Reverse Phase Protein Arrays RPPA to Explore Protein Expression Variation within Individual Renal Cell Cancers
Published on: January 22, 2013
Integrated glycoproteomic characterization of clear cell renal cell carcinoma
T Mamie Lih1, Kyung-Cho Cho1, Michael Schnaubelt1
1Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.
Abstract:
Clear cell renal cell carcinoma (ccRCC), a common form of RCC, is responsible for the high mortality rate of kidney cancer. Dysregulations of glycoproteins have been shown to associate with ccRCC. However, the molecular mechanism has not been well characterized. Here, a comprehensive glycoproteomic analysis is conducted using 103 tumors and 80 paired normal adjacent tissues. Altered glycosylation enzymes and corresponding protein glycosylation are observed, while two of the major ccRCC mutations, BAP1 and PBRM1, show distinct glycosylation profiles. Additionally, inter-tumor heterogeneity and cross-correlation between glycosylation and phosphorylation are observed. The relation of glycoproteomic features to genomic, transcriptomic, proteomic, and phosphoproteomic changes shows the role of glycosylation in ccRCC development with potential for therapeutic interventions. This study reports a large-scale tandem mass tag (TMT)-based quantitative glycoproteomic analysis of ccRCC that can serve as a valuable resource for the community.
Insights
This study reveals altered protein glycosylation in clear cell renal cell carcinoma (ccRCC), a kidney cancer. Findings link glycosylation changes to ccRCC mutations and offer potential therapeutic targets.
Area of Science:
- Oncology
- Proteomics
- Glycomics
Background:
- Clear cell renal cell carcinoma (ccRCC) is a major cause of kidney cancer mortality.
- Glycoprotein dysregulation is linked to ccRCC, but molecular mechanisms remain unclear.
Purpose of the Study:
- To conduct a comprehensive glycoproteomic analysis of ccRCC.
- To investigate the relationship between glycosylation, mutations, and other molecular changes in ccRCC.
Main Methods:
- Utilized tandem mass tag (TMT)-based quantitative glycoproteomics.
- Analyzed 103 ccRCC tumors and 80 paired normal adjacent tissues.
- Integrated glycoproteomic data with genomic, transcriptomic, proteomic, and phosphoproteomic data.
Main Results:
- Identified altered glycosylation enzymes and protein glycosylation patterns in ccRCC.
- Observed distinct glycosylation profiles associated with BAP1 and PBRM1 mutations.
- Revealed inter-tumor heterogeneity and correlations between glycosylation and phosphorylation.
Conclusions:
- Glycosylation plays a significant role in ccRCC development.
- Glycoproteomic features offer potential for novel therapeutic interventions in kidney cancer.
- This study provides a valuable glycoproteomic resource for ccRCC research.
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