Endogenous lectins (galectins-1 and -3) as probes to detect differentiation-dependent alterations in human squamous cell carcinomas of the oropharynx and larynx
Language English Country Greece Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10719052
DOI
10.3892/ijmm.5.4.369
Knihovny.cz E-resources
- MeSH
- Cell Differentiation MeSH
- Antigens, Differentiation metabolism MeSH
- Fluorescent Antibody Technique, Indirect MeSH
- Galactosides metabolism MeSH
- Galectin 1 MeSH
- Galectin 3 MeSH
- Hemagglutinins metabolism MeSH
- Keratins metabolism MeSH
- Lectins metabolism MeSH
- Humans MeSH
- Laryngeal Neoplasms metabolism pathology MeSH
- Oropharyngeal Neoplasms metabolism pathology MeSH
- Carcinoma, Squamous Cell metabolism pathology MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antigens, Differentiation MeSH
- Galactosides MeSH
- Galectin 1 MeSH
- Galectin 3 MeSH
- Hemagglutinins MeSH
- Keratins MeSH
- Lectins MeSH
Expression of glycan determinants for in situ binding is the prerequisite for a productive protein (lectin)-carbohydrate recognition. Labeled tissue lectins as tools are preferable to plant lectins to assess this parameter, because plant and animal lectins with identical saccharide specification can well differ in their profiles of oligosaccharide binding pattern. Due to their relevance in growth control and matrix adhesion the family of galectins (galactoside-binding metal ion independent animal lectins) is receiving increasing utilization in human biology. Employing biotinylated galectin-1 and galectin-3 we studied the expression of binding sites for these galectins in normal human squamous epithelium and human carcinomas from the oropharyngeal region and larynx in relation to the expression of LP-34+ cytokeratins by the procedure of double labeling. Tissue sites accessible for galectin-1 were located in all layers of normal epithelium and in tumor cells. In contrast, galectin-3 binding was suprabasal in the normal epithelium and in tumor cells exhibiting signs of keratinization. These results reveal differences in the localization of accessible sites for the two galectins. Relating to cell development galectin-3 appeared to display affinity to areas with increased extent of differentiation.
References provided by Crossref.org
Craniopharyngioma: a case report and comparative galectin histochemical analysis
