ArticleScientific reports2020
Lectin affinity chromatography and quantitative proteomic analysis reveal that galectin-3 is associated with metastasis in nasopharyngeal carcinoma.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Research Progress and Application Prospects of Bioaffinity Chromatography in Screening Cardiotoxic Components of Chinese Herbal Medicines.ACS omega · 2026Review
- Candesartan cilexetil as a repurposed therapeutic candidate for nasopharyngeal carcinoma: Integrated in vitro and in silico analyses.EXCLI journal · 2026Article
- Clinical glycoproteomics: methods and diseases.MedComm · 2024Review
- Revisiting Multi-Omics Data to Unravel Galectins as Prognostic Factors in Head and Neck Squamous Cell Carcinoma.Biomedicines · 2024Article
- Distinct cholangiocarcinoma cell migration in 2D monolayer and 3D spheroid culture based on galectin-3 expression and localization.Frontiers in oncology · 2022Article
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3 authors at 2 institutions in 1 country.
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Abstract
Nasopharyngeal carcinoma (NPC) is a serious cancer in East and Southeast Asia. Patients are often diagnosed at advanced stages, rendering treatment failure due to high potential of metastasis. This study identified lectin-binding glycoproteins with a potential role in NPC metastasis. Cell lysate and culture medium in highly metastatic 5-8F, and lowly-metastatic 6-10B NPC cell lines were fractionated by ConA- and WGA-affinity chromatography, and subjected to GeLC-MS/MS. A total of 232 and 197 proteins were identified in ConA-enriched fraction of 5-8F and 6-10B cell lysates respectively. In WGA-enriched fraction, 65 and 164 proteins were found in 5-8F and 6-10B cell lysates respectively. Proteins identified in culture medium for both cell lines were 223 and 85 for ConA-enriched fraction, and 94 and 124 for WGA-enriched fraction from 5-8F and 6-10B respectively. Differentially expressed proteins were functionally categorized into cell-cell adhesion, extracellular matrix, glycolysis, protein homeostasis and/or glycosylation enzymes, and lipid metabolism. Interestingly, Galectin-3 (Gal-3) was highly expressed in 5-8F cells but was lowly expressed in 6-10B cells. The Gal-3 knockdown in 5-8F cells, Gal-3 overexpression in 6-10B cells and treatment with Gal-3 inhibitor revealed that Gal-3 was responsible for metastatic phenotypes including adhesion, migration and invasion. So Galectin-3 may serve as a potential target for NPC therapeutic interventions.
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