Laminin inhibits human keratinocyte migration.
A quantitative migration assay for human keratinocytes was developed to assess the influence of extracellular matrix molecules on cell motility independently from their effect on cell proliferation. Fibronectin and collagen types I and IV markedly promoted keratinocyte migration, but albumin, type V collagen, and heparan sulfate proteoglycan had little effect. In contrast, laminin inhibited keratinocyte motility and dramatically reduced type IV collagen-induced migration in a concentration-dependent manner. Laminin was not toxic, since it had no apparent effect on morphology, growth, or ability of cells to be passaged. Laminin, a major component of the lamina lucida, may inhibit motility of keratinocytes in vivo. Absence of contact with laminin, which accompanies wounding, may facilitate motility and healing in the epidermis.
Woodley
D T
DT
Department of Dermatology, University of North Carolina, School of Medicine, Chapel Hill 27514.
Bachmann
P M
PM
O'Keefe
E J
EJ
D002455:Cell Division / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects*; D002478:Cells, Cultured; D003094:Collagen / Q000494:pharmacology; D000078404:Epidermal Cells; D006493:Heparin / Q000031:analogs & derivatives / Q000494:pharmacology; D006801:Humans; D007633:Keratins; D007797:Laminin / Q000494:pharmacology*; D011509:Proteoglycans / Q000494:pharmacology
D007797:Laminin; D011509:Proteoglycans; C036090:heparin proteoglycan; D007633:Keratins; D006493:Heparin; D003094:Collagen