Differential regulation of galectin expression/reactivity during wound healing in porcine skin and in cultures of epidermal cells with functional impact on migration.
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.
Klíma
J
J
Institute of Animal Physiology and Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
Lacina
L
L
Dvořánková
B
B
Herrmann
D
D
Carnwath
J W
JW
Niemann
H
H
Kaltner
H
H
André
S
S
Motlík
J
J
Gabius
H-J
HJ
Smetana
K
K
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
D037483:Galectin 1; D037502:Galectin 3; D037161:Galectins; C445499:LGALS1 protein, human; C092525:LGALS7 protein, human; D012333:RNA, Messenger