Members of the galectin family of endogenous lectins are involved in diverse cellular activities such as cell-cell and cell-matrix interactions, growth control or mediator release by virtue of the recognition of appropriate glycoligands. To delineate the physiological significance of individual galectins expressed at distinct sites, their localization is an essential step. In this study we focused on galectin-3. We employed the A1D6 monoclonal antibody as well as a polyclonal antibody for the immunohistochemical detection of galectin-3, biotinylated galectin-3 to visualize presence of accessible binding sites and labeled (neo)glycoconjugates with Gal/GalNAc-termini to reveal presence of accessible receptor sites for such carbohydrate structures. As a marker for suprabasal keratinocytes the anti-cytokeratin 10 monoclonal antibody was applied. The resulting staining reactions showed strong suprabasal coexpression of galectin-3 with cytokeratin 10. In addition to this cell type, basal keratinocytes were also reactive to the carbohydrate ligand-exposing neoglycoconjugates, a cytochemical stratification being apparent for carbohydrate-binding sites recognizing alpha-GalNAc. This observation argues in favor of the presence of further members of the galectin family in human epidermis. Since no evidence for accessible binding sites for galectin-3 could be provided, epidermal keratinocytes thus apparently have a restricted expression of respective glycoligands which can be saturated in suprabasal keratinocytes by the cellular lectin. In conclusion, galectin-3 expression in human epidermis is restricted to the suprabasal keratinocytes lacking proliferative activity.
|Original language||English (US)|
|Number of pages||10|
|Journal||Electronic Journal of Pathology and Histology|
|State||Published - 1999|
- Cytokeratin 10
- Langerhans cell
ASJC Scopus subject areas