Expression of galectin-3-reactive ligands in squamous cancer and normal epithelial cells as a marker of differentiation
Jazyk angličtina Země Řecko Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
PubMed
11408923
Knihovny.cz E-zdroje
- MeSH
- buněčná diferenciace MeSH
- cytoskeletální proteiny metabolismus MeSH
- desmogleiny MeSH
- desmoplakiny MeSH
- diferenciační antigeny metabolismus MeSH
- epitelové buňky metabolismus MeSH
- fluorescenční barviva MeSH
- fluorescenční protilátková technika nepřímá MeSH
- galektin 3 MeSH
- keratiny metabolismus MeSH
- lidé MeSH
- ligandy MeSH
- lymfatické metastázy patologie MeSH
- membránové glykoproteiny metabolismus MeSH
- nádorové biomarkery metabolismus MeSH
- nádorové proteiny metabolismus MeSH
- nádory hlavy a krku metabolismus patologie MeSH
- prognóza MeSH
- spinocelulární karcinom metabolismus patologie MeSH
- staging nádorů metody MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- cytoskeletální proteiny MeSH
- desmogleiny MeSH
- desmoplakiny MeSH
- diferenciační antigeny MeSH
- DSP protein, human MeSH Prohlížeč
- fluorescenční barviva MeSH
- galektin 3 MeSH
- keratiny MeSH
- ligandy MeSH
- membránové glykoproteiny MeSH
- nádorové biomarkery MeSH
- nádorové proteiny 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
