title: Differential regulation of galectin expression/reactivity during wound healing in porcine skin and in cultures of epidermal cells with functional impact on migration.
abstract: 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.
authors.affiliation: Institute of Animal Physiology and Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
authors.forename: J
authors.initials: J
authors.lastname: Klíma
authors.forename: L
authors.initials: L
authors.lastname: Lacina
authors.forename: B
authors.initials: B
authors.lastname: Dvořánková
authors.forename: D
authors.initials: D
authors.lastname: Herrmann
authors.forename: J W
authors.initials: JW
authors.lastname: Carnwath
authors.forename: H
authors.initials: H
authors.lastname: Niemann
authors.forename: H
authors.initials: H
authors.lastname: Kaltner
authors.forename: S
authors.initials: S
authors.lastname: André
authors.forename: J
authors.initials: J
authors.lastname: Motlík
authors.forename: H-J
authors.initials: HJ
authors.lastname: Gabius
authors.forename: K
authors.initials: K
authors.lastname: Smetana
mesh_terms: D000818:Animals; D001665:Binding Sites; D019921:Biotinylation; D015153:Blotting, Western; D002448:Cell Adhesion; D002465:Cell Movement; D002478:Cells, Cultured; D037483:Galectin 1 / Q000378:metabolism; D037502:Galectin 3 / Q000378:metabolism; D037161:Galectins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D015603:Keratinocytes / Q000378:metabolism* / Q000473:pathology; D012333:RNA, Messenger / Q000378:metabolism; D012867:Skin / Q000293:injuries / Q000378:metabolism* / Q000473:pathology; D013552:Swine; D013556:Swine, Miniature; D013997:Time Factors; D015854:Up-Regulation; D014945:Wound Healing
chemical_list: D037483:Galectin 1; D037502:Galectin 3; D037161:Galectins; C445499:LGALS1 protein, human; C092525:LGALS7 protein, human; D012333:RNA, Messenger