Differentiation-dependent glycosylation of cells in squamous cell epithelia detected by a mammalian lectin
Language English Country Switzerland Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12097836
DOI
10.1159/000063707
PII: 63707
Knihovny.cz E-resources
- MeSH
- Ki-67 Antigen metabolism MeSH
- Integrin beta1 metabolism MeSH
- Carcinoma, Basal Cell metabolism MeSH
- Cell Differentiation physiology MeSH
- Cytoskeletal Proteins metabolism MeSH
- Desmogleins MeSH
- Desmoplakins MeSH
- Epithelium physiology MeSH
- Epithelial Cells cytology metabolism MeSH
- Galectin 3 metabolism MeSH
- Glycosylation MeSH
- Immunohistochemistry MeSH
- Keratinocytes cytology metabolism MeSH
- Keratins metabolism MeSH
- Cells, Cultured MeSH
- Humans MeSH
- Mice MeSH
- Skin Neoplasms metabolism MeSH
- Swine MeSH
- Plant Lectins metabolism MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Ki-67 Antigen MeSH
- Integrin beta1 MeSH
- Cytoskeletal Proteins MeSH
- Desmogleins MeSH
- Desmoplakins MeSH
- dolichos biflorus agglutinin MeSH Browser
- DSP protein, human MeSH Browser
- Dsp protein, mouse MeSH Browser
- Galectin 3 MeSH
- Keratins MeSH
- Plant Lectins MeSH
UNLABELLED: The squamous stratified epithelia contain a proliferative (harboring mitotic activity) and a differentiating compartment. Due to the potential of protein-carbohydrate interactions to regulate cellular activities we introduced a mammalian lectin to cyto- and histochemical analysis. We answer the questions of whether and to what extent this new probe can pinpoint differentiation-dependent glycosylation changes in sections and in culture of keratinocytes. MATERIAL AND METHODS: Purification and labeling enabled monitoring of galectin-3 reactivity in frozen sections of human and pig epidermis and basal cell carcinomas as well as in culture of keratinocytes. The staining pattern of the lectin was correlated with the staining profile of other cell markers including desmosomal proteins, beta(1) integrin, and the proliferation marker Ki-67. The Dolichos biflorus agglutinin (DBA) sharing binding reactivity of galectin-3 to the A type histoblood group epitope was used for comparison. RESULTS: Both lectins exhibit suprabasal binding. However, their profiles were not identical, substantiated by lack of coinhibition. Strong DBA reactivity was also observed in a limited number of basal layer cells, namely in cells without the expression of the proliferation marker Ki-67. Cultured mitotic epidermal cells have no reactivity for DBA. Presence of ligands for this plant lectin was connected with decreased positivity of nuclei for Ki-67 and the occurrence of ring-shaped nucleoli, micronucleoli or absence of nucleoli. Considering colocalization the pattern of galectin-3-binding sites coincided with the presence of desmosomal proteins such as desmoplakin-1 and desmoglein but not beta(1) integrin, a potential ligand. Interestingly, studied basal cell carcinomas expressed no binding sites for galectin-3, while a limited number of cells were DBA-reactive. CONCLUSION: The expression of galectin-3-binding sites and also DBA-reactive glycoligands correlates with an increased level of differentiation and/or cessation of proliferation in the examined squamous stratified epithelia. Further application of tissue lectins for characterizing ligand expression and its modulation is an important step to reveal functional relevance.
References provided by Crossref.org
Comparative phenotypic characterization of keratinocytes originating from hair follicles
Craniopharyngioma: a case report and comparative galectin histochemical analysis
