ArticleMolecular & cellular proteomics : MCP2011
Targeted identification of metastasis-associated cell-surface sialoglycoproteins in prostate cancer.
Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 81 citations in OpenAlex.
- Metabolic Probing of Sialylated Glycoconjugates with Fluorine-Selenol Displacement Reaction (FSeDR).ACS bio & med chem Au · 2025Article
- Bioorthogonal Chemical Labeling Probes Targeting Sialic Acid Isomers forAnalytical chemistry · 2023Article
- Mass spectrometry based biomarkers for early detection of HCC using a glycoproteomic approach.Advances in cancer research · 2023Review
- Article
- Optimization of small extracellular vesicle isolation from expressed prostatic secretions in urine for in-depth proteomic analysis.Journal of extracellular vesicles · 2022Article
- Investigating the Role of Obesity in Prostate Cancer and Identifying Biomarkers for Drug Discovery: Systems Biology and Deep Learning Approaches.Molecules (Basel, Switzerland) · 2022Article
- Selective Inhibition of Heparan Sulphate and Not Chondroitin Sulphate Biosynthesis by a Small, Soluble Competitive Inhibitor.International journal of molecular sciences · 2021Article
- Mass Spectrometry-Based Glycoproteomics and Prostate Cancer.International journal of molecular sciences · 2021Review
- Discovery and Pharmacological Evaluation of STEAP4 as a Novel Target for HER2 Overexpressing Breast Cancer.Frontiers in oncology · 2021Article
- Application of Nanotechnology in Wood-Based Products Industry: A Review.Nanoscale research letters · 2020Review
- Mapping glycan-mediated galectin-3 interactions by live cell proximity labeling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of LCA-binding Glycans as a Novel Biomarker for Esophageal Cancer Metastasis using a Lectin Array-based Strategy.Journal of Cancer · 2020Article
- Global and site-specific analysis of protein glycosylation in complex biological systems with Mass Spectrometry.Mass spectrometry reviews · 2019Review
- Glycans as Biomarkers in Prostate Cancer.International journal of molecular sciences · 2019Review
- Bifunctional cleavable probes forChemical science · 2019Article
- Systematic and site-specific analysis of N-glycoproteins on the cell surface by integrating bioorthogonal chemistry and MS-based proteomics.Methods in enzymology · 2019Article
- Mass Spectrometry Approaches to Glycomic and Glycoproteomic Analyses.Chemical reviews · 2018Review
- Mass Spectrometry-Based Chemical and Enzymatic Methods for Global Analysis of Protein Glycosylation.Accounts of chemical research · 2018Review
- The enigmatic seminal plasma: a proteomics insight from ejaculation to fertilization.Reproductive biology and endocrinology : RB&E · 2018Review
- Lectin BS-I inhibits cell migration and invasion via AKT/GSK-3β/β-catenin pathway in hepatocellular carcinoma.Journal of cellular and molecular medicine · 2018Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Covalent attachment of carbohydrates to proteins is one of the most common post-translational modifications. At the cell surface, sugar moieties of glycoproteins contribute to molecular recognition events involved in cancer metastasis. We have combined glycan metabolic labeling with mass spectrometry analysis to identify and characterize metastasis-associated cell surface sialoglycoproteins. Our model system used syngeneic prostate cancer cell lines derived from PC3 (N2, nonmetastatic, and ML2, highly metastatic). The metabolic incorporation of AC(4)ManNAz and subsequent specific labeling of cell surface sialylation was confirmed by flow cytometry and confocal microscopy. Affinity isolation of the modified sialic-acid containing cell surface proteins via click chemistry was followed by SDS-PAGE separation and liquid chromatography-tandem MS analysis. We identified 324 proteins from N2 and 372 proteins of ML2. Using conservative annotation, 64 proteins (26%) from N2 and 72 proteins (29%) from ML2 were classified as extracellular or membrane-associated glycoproteins. A selective enrichment of sialoglycoproteins was confirmed. When compared with global proteomic analysis of the same cells, the proportion of identified glycoprotein and cell-surface proteins were on average threefold higher using the selective capture approach. Functional clustering of differentially expressed proteins by Ingenuity Pathway Analysis revealed that the vast majority of glycoproteins overexpressed in the metastatic ML2 subline were involved in cell motility, migration, and invasion. Our approach effectively targeted surface sialoglycoproteins and efficiently identified proteins that underlie the metastatic potential of the ML2 cells.
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