Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation
Language English Country Greece Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
11408923
Knihovny.cz E-resources
- MeSH
- Cell Differentiation MeSH
- Cytoskeletal Proteins metabolism MeSH
- Desmogleins MeSH
- Desmoplakins MeSH
- Antigens, Differentiation metabolism MeSH
- Epithelial Cells metabolism MeSH
- Fluorescent Dyes MeSH
- Fluorescent Antibody Technique, Indirect MeSH
- Galectin 3 MeSH
- Keratins metabolism MeSH
- Humans MeSH
- Ligands MeSH
- Lymphatic Metastasis pathology MeSH
- Membrane Glycoproteins metabolism MeSH
- Biomarkers, Tumor metabolism MeSH
- Neoplasm Proteins metabolism MeSH
- Head and Neck Neoplasms metabolism pathology MeSH
- Prognosis MeSH
- Carcinoma, Squamous Cell metabolism pathology MeSH
- Neoplasm Staging methods MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Cytoskeletal Proteins MeSH
- Desmogleins MeSH
- Desmoplakins MeSH
- Antigens, Differentiation MeSH
- DSP protein, human MeSH Browser
- Fluorescent Dyes MeSH
- Galectin 3 MeSH
- Keratins MeSH
- Ligands MeSH
- Membrane Glycoproteins MeSH
- Biomarkers, Tumor MeSH
- Neoplasm Proteins MeSH
The definition of biological markers for oropharynx and larynx cancer is essential to predict their clinical behavior. Since cellular glycans play an important role in biological information transfer, we have employed an endogenous lectin, galectin-3, to examine in primary squamous carcinomas, lymph node metastases, and physiological squamous epithelia whether glycans recognized by this lectin are altered in relation to the state of differentiation. The expression of galectin-3 was concomitantly evaluated by immunohistochemistry using the A1D6 monoclonal antibody. In addition, other antibodies were used for the detection of cytokeratins and desmosomal proteins (desmoplakin-1 and desmoglein). The results show the expression of galectin-3-reactive ligands in moderately/highly differentiated carcinomas only in areas exhibiting a high level of keratinization. Except for one patient out of 14, metastatic cells in lymph nodes expressed no accessible binding sites for galectin-3. No galectin-3-reactivity was detected in the basal cell layer of all studied normal epithelia (which contains the proliferating cells). The suprabasal layers were positive in epidermis and epithelium of tongue and cornea and negative in epithelium of palatine tonsil. The tumor cells expressed galectin-3 with an intensity positively correlated with tumor differentiation. The position of galectin-3-reactive sites colocalized with the two tested desmosomal proteins. However, presence of these proteins was also detected in areas of tumor and suprabasal layers of tonsil epithelium where no binding reactivity for galectin-3 was found. The present study showed that expression of galectin-3-reactive glycoligands is differentiation-dependent in normal as well as malignant squamous cells. Colocalization of galectin-3-reactive sites with desmosomal proteins (desmoplakin-1 and desmoglein) suggests an association of the galectin-3 ligand(s) with the cell surface, pointing to a potential participation of galectin-3 in mediation of intercellular contacts in these tumor types.
Craniopharyngioma: a case report and comparative galectin histochemical analysis
