Differential regulation of galectin expression/reactivity during wound healing in porcine skin and in cultures of epidermal cells with functional impact on migration
Jazyk angličtina Země Česko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
19093745
DOI
10.33549/physiolres.931624
PII: 1624
Knihovny.cz E-zdroje
- MeSH
- biotinylace MeSH
- buněčná adheze MeSH
- časové faktory MeSH
- galektin 1 metabolismus MeSH
- galektin 3 metabolismus MeSH
- galektiny genetika metabolismus MeSH
- hojení ran * MeSH
- imunohistochemie MeSH
- keratinocyty metabolismus patologie MeSH
- kultivované buňky MeSH
- kůže zranění metabolismus patologie MeSH
- lidé MeSH
- messenger RNA metabolismus MeSH
- miniaturní prasata MeSH
- pohyb buněk * MeSH
- prasata MeSH
- upregulace MeSH
- vazebná místa MeSH
- western blotting MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- galektin 1 MeSH
- galektin 3 MeSH
- galektiny MeSH
- LGALS1 protein, human MeSH Prohlížeč
- LGALS7 protein, human MeSH Prohlížeč
- messenger RNA MeSH
The glycophenotyping of mammalian cells with plant lectins maps aspects of the glycomic profile and disease-associated alterations. A salient step toward delineating their functional dimension is the detection of endogenous lectins. They can translate sugar-encoded changes into cellular responses. Among them, the members of the lectin family of galectins are emerging regulators of cell adhesion, migration and proliferation. Focusing on galectins-1, -3 and -7, we addressed the issue whether their expression is regulated during wound healing in porcine skin as model. A conspicuous upregulation is detected for galectin-1 in the dermis and a neoexpression in the epidermis, where an increased level of galectin-7 was also found. Applying biotinylated tissue lectins as probes, the signal intensities for accessible binding sites decreased, intimating an interaction of the cell lectin with reactive sites. In contrast, galectin-3 parameters remained rather constant. Of note, epidermal cells in culture also showed an increase in expression/presence of galectin-1, measured on the levels of mRNA and protein, in this case by Western blotting and quantitative immunocytochemistry. Used as matrix, galectin-1 conferred resistance to trypsin treatment to attached human keratinocytes and reduced migration into scratch-wound areas in vitro. This report thus presents new information on endogenous lectins in wound healing and differential regulation among the three tested cases.
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