Defining the glycophenotype of squamous epithelia using plant and mammalian lectins. Differentiation-dependent expression of alpha2,6- and alpha2,3-linked N-acetylneuraminic acid in squamous epithelia and carcinomas, and its differential effect on binding of the endogenous lectins galectins-1 and -3
Jazyk angličtina Země Dánsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- barvení a značení MeSH
- beta-D-galaktosid-alfa-2,6-sialyltransferasa MeSH
- beta-galaktosid-alfa-2,3-sialyltransferasa MeSH
- biologické markery MeSH
- buněčná diferenciace MeSH
- epidermální buňky MeSH
- epitelové buňky chemie cytologie MeSH
- fenotyp MeSH
- galektin 1 metabolismus MeSH
- galektin 3 metabolismus MeSH
- glykokonjugáty analýza biosyntéza MeSH
- glykosylace MeSH
- kultivované buňky MeSH
- kuřecí embryo MeSH
- kyselina N-acetylneuraminová analýza metabolismus MeSH
- lektiny metabolismus MeSH
- lidé MeSH
- myši inbrední BALB C MeSH
- myši inbrední C57BL MeSH
- myši MeSH
- nádorové proteiny biosyntéza chemie MeSH
- nádory hrtanu chemie patologie MeSH
- nádory jazyka chemie patologie MeSH
- orgánová specificita MeSH
- posttranslační úpravy proteinů MeSH
- prasata MeSH
- rostlinné lektiny metabolismus MeSH
- sialyltransferasy metabolismus MeSH
- spinocelulární karcinom chemie patologie MeSH
- zvířata MeSH
- Check Tag
- kuřecí embryo MeSH
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- beta-D-galaktosid-alfa-2,6-sialyltransferasa MeSH
- beta-galaktosid-alfa-2,3-sialyltransferasa MeSH
- biologické markery MeSH
- galektin 1 MeSH
- galektin 3 MeSH
- glykokonjugáty MeSH
- kyselina N-acetylneuraminová MeSH
- lektiny MeSH
- nádorové proteiny MeSH
- rostlinné lektiny MeSH
- sialyltransferasy MeSH
A thorough characterization of the properties of squamous epithelial cells is necessary in order to improve our understanding of the functional aspects of normal development and malignant aberrations. Up to now, studies have focused almost exclusively on monitoring distinct protein markers. With our growing awareness of the coding function of glycan chains of cellular glycoconjugates and their interaction with receptors (lectins) in situ, defining the glycophenotype of these cells has become an important issue. Whereas the commonly applied plant lectins are tools used to map the presence and localization of biochemically defined saccharide epitopes, the introduction of endogenous (mammalian) lectins to this analysis enables us to take the step from monitoring the presence of glycan to understanding the functional implications by revealing ligand properties of the detected epitope for tissue lectin. Thus, in this study we investigated a distinct aspect of glycosylation using plant and mammalian lectins, i.e. the linkage type of sialylation. We first mapped the expression profile of the type of sialylation (alpha2,3- or alpha2,6-linked) by plant lectins. Based on the hypothesis that this factor regulates accessibility of ligands for endogenous lectins we introduced two labeled galectins to this study. Galectin-3 (but not galectin-1) binding was related to cell differentiation in normal adult and developing epithelia, cultured epidermal cells, and carcinomas derived from these epithelia. The presented data suggest that alpha2,6-linked N-acetyl-D-neuraminic acid moieties could serve to mask galectin-3-reactive glycoepitopes. As a consequence, monitoring of the linkage type of sialic acid in glycans by plant lectins therefore has implications for the extent of glycan reactivity with endogenous lectins, pointing to a potential function of changes in sialylation type beyond these cell and lectin systems.
Citace poskytuje Crossref.org
Comparative phenotypic characterization of keratinocytes originating from hair follicles
