ArticleMolecular & cellular proteomics : MCP2012
Altered expression of sialylated glycoproteins in breast cancer using hydrazide chemistry and mass spectrometry.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed, 65 citations in OpenAlex.
- Upregulation of Sulfated N-Glycans in Serum as Predictive Biomarkers for Early-Stage Breast Cancer.International journal of molecular sciences · 2025Article
- Optimization of glycopeptide enrichment techniques for the identification of clinical biomarkers.Expert review of proteomics · 2024Review
- Cancer-specific glycosylation of CD13 impacts its detection and activity in preclinical cancer tissues.iScience · 2023Article
- Review
- Article
- Comparison of Different HILIC Stationary Phases in the Separation of Hemopexin and Immunoglobulin G Glycopeptides and Their Isomers.Molecules (Basel, Switzerland) · 2020Article
- Nanoantibiotics containing membrane-active human cathelicidin LL-37 or synthetic ceragenins attached to the surface of magnetic nanoparticles as novel and innovative therapeutic tools: current status and potential future applications.Journal of nanobiotechnology · 2020Review
- Glycosylation and its implications in breast cancer.Expert review of proteomics · 2019Review
- Article
- 5-Year Survival in Gastric Adenocarcinoma with Epithelial and Stromal Versican Expression.Iranian journal of pathology · 2019Article
- Dermaseptin-PH: A Novel Peptide with Antimicrobial and Anticancer Activities from the Skin Secretion of the South American Orange-Legged Leaf Frog, Pithecopus (Phyllomedusa) hypochondrialis.Molecules (Basel, Switzerland) · 2017Article
- Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications.Oncotarget · 2017Review
- Functional roles of sialylation in breast cancer progression through miR-26a/26b targeting ST8SIA4.Cell death & disease · 2016Article
- The Uncontrolled Sialylation is Related to Chemoresistant Metastatic Breast Cancer.Pathology oncology research : POR · 2016Article
- Sialylation: an Avenue to Target Cancer Cells.Pathology oncology research : POR · 2016Review
- Glycoproteomic Approach Identifies KRAS as a Positive Regulator of CREG1 in Non-small Cell Lung Cancer Cells.Theranostics · 2016Article
- Plasma Glycoproteomics Reveals Sepsis Outcomes Linked to Distinct Proteins in Common Pathways.Critical care medicine · 2015Article
- Increased expression of MUC1 and sialyl Lewis antigens in different areas of clear renal cell carcinoma.Clinical and experimental nephrology · 2015Article
- Systematic and site-specific analysis ofChemical science · 2015Article
- Insights into the key roles of proteoglycans in breast cancer biology and translational medicine.Biochimica et biophysica acta · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Sialylation is one of the altered protein glycosylations associated with cancer development. The sialoglycoproteins in cancer cells, however, largely remain unidentified because of the lack of a method for quantitative analysis of sialoglycoproteins. This manuscript presents a high throughput method for quantitative analysis of N-linked sialoglycoproteins using conditional hydrazide chemistry, liquid chromatography, and tandem mass spectrometry. We further applied the sialoglycoproteomic method to the profiling of breast cancer tissues and compared findings with the results from the total glycoproteomic analysis using the original hydrazide chemistry method. We identified altered expression of sialoglycoproteins, as well as the total glycoprotein changes associated with breast cancer. Using lectin and Western blot analysis, we characterized one of the sialoglycoproteins, versican, and confirmed that versican was most sialylated and elevated in breast cancer. Furthermore, we showed that versican was detected in both cancer epithelial cells and peritumoral stromal cells using immunohistochemistry. Tissue microarray analysis revealed that epithelial expression of versican had significant relations to lymph node metastasis and pathological stages. This is the first quantitative sialoglycoproteomic and glycoproteomic analysis of breast cancer and noncancerous tissues. These findings present a significant addition of the method to the identification of altered expression of sialylated glycoproteins associated with breast cancer development.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.