ArticleMolecular cancer2003
Expression of peanut agglutinin-binding mucin-type glycoprotein in human esophageal squamous cell carcinoma as a marker.
Article in Molecular cancer, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Intestinal Mucin Glycosylation: Structural Regulation, Homeostasis Maintenance and Disease Association.Biomolecules · 2025Review
- A cluster randomized controlled trial to evaluate the efficacy of esophageal and gastric cancer screening in mortality reduction in a non-high-incidence area: methodology and initial results.Annals of translational medicine · 2022Article
- Etiology, cancer stem cells and potential diagnostic biomarkers for esophageal cancer.Cancer letters · 2019Review
- Mucus and Mucins: do they have a role in the inhibition of the human immunodeficiency virus?Virology journal · 2017Review
- Interaction of the Oncofetal Thomsen-Friedenreich Antigen with Galectins in Cancer Progression and Metastasis.Frontiers in oncology · 2016Review
- The role of crude saliva and purified salivary mucins in the inhibition of the Human Immunodeficiency Virus type 1.Virology journal · 2012Article
- None-endoscopic Screening for Esophageal Squamous Cell Carcinoma- A Review.Middle East journal of digestive diseases · 2012Review
- Sequential Changes in Aberrant Crypt Foci and Lectin Expression in the Early and Late Stages of DMH-Induced Colon Carcinogenesis in Rats.Gut and liver · 2012Article
- Cancer vaccines and carbohydrate epitopes.Vaccine · 2011Review
- PpGalNacT2 participating in vanadium-induced HL-60 cell differentiation.Molecular biology reports · 2011Article
- Sialidase fusion protein as a novel broad-spectrum inhibitor of influenza virus infection.Antimicrobial agents and chemotherapy · 2006Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe TF (Thomson-Friedenreich) blood group antigen behaves as an onco-foetal carcinoma-associated antigen, showing increased expression in malignancies and its detection and quantification can be used in serologic diagnosis mainly in adenocarcinomas. This study was undertaken to analyze the sera and tissue level detectable mucin-type glycoprotein (TF-antigen) by Peanut agglutinin (PNA) and its diagnostic index in serum as well tissues of human esophageal squamous cell carcinoma as marker.
resultsWe examined 100 patients for serological analysis by Enzyme Linked Lectin Assay (ELISA) and demonstrated a sensitivity of 87.5%, specificity of 90% and a positive predictive value of 95%. The immuno-histochemical localization of TF antigen by Fluorescence Antigen Technique (FAT) in 25 specimens of normal esophageal squamous epithelium specimens and 92 specimens with different grades of, allowed a quicker and more precise identification of its increased expression and this did not correlate with gender and tumor size. There was a positive correlation between membrane bound TF antigen expression with different histological progression, from well differentiated to poorly differentiated, determined by PNA binding. Specimens showed morphological changes and a pronounced increase in PNA binding in Golgi apparatus, secretory granules of the cytosol of well differentiated and an increased cell membrane labeling in moderately and poorly differentiated, when compared with ESCC and normal tissues.
conclusionThe authors propose that the expression of TF-antigen in human may play an important role during tumorigenesis establishing it as a chemically well-defined carcinoma-associated antigen. Identification of the circulating TF-antigen as a reactive form and as a cryptic form in the healthy individuals, using PNA-ELLA and Immunohistochemical analysis of TF antigen by FAT is positively correlated with the different histological grades as a simple and cost-effective method for the early diagnosis of ESCC. The present study reveals that, during tumorigenesis, an aberrant glycosylation takes place in Golgi apparatus leading to over secretion of TF antigen into the cytoplasm along with mucin granules and later into cell membrane. We suggest that the further characterization of TF antigen may unravel pathogenetic aspects of this silent disease.
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