Epidermal cell migration on laminin-coated substrates. Comparison with other extracellular matrix and non-matrix proteins.
Pieces of coverslip glass coated with various proteins were implanted under one edge of a fresh skin wound on adult newt hind limbs so that the implant served as wound bed for the migrating wound epithelium. Laminin, a protein that has been implicated as an epithelial-specific adhesin, was a moderately good migration substrate. Type-IV collagen, fibrinogen and fibronectin, however, were significantly better. Fetuin, myoglobin, and casein all proved to be very poor substrates, allowing practically no migration. The inability of fetuin, myoglobin, and casein to support migration is further evidence that the considerable migration that occurs on collagen (Donaldson et al. 1982) fibrinogen and fibronectin (Donaldson and Mahan 1983) and the moderate migration on laminin, is a relatively specific response to these proteins and is therefore of special significance. The fact that laminin is a poorer migration substrate than collagen, fibrinogen or fibronectin suggests that the absence of cell surface laminin that has been associated with epithelial movement in several studies (Stanley et al. 1981; Clark et al. 1982; Madri and Stenn 1982; Gulati et al. 1983) may promote motility by allowing epithelial cells to interact directly with other extracellular macromolecules.
D000818:Animals; D002465:Cell Movement / Q000187:drug effects; D003094:Collagen / Q000494:pharmacology; D005898:Glass; D007797:Laminin / Q000494:pharmacology*; D008297:Male; D008855:Microscopy, Electron, Scanning; D011506:Proteins / Q000494:pharmacology*; D012455:Salamandridae; D012867:Skin / Q000187:drug effects / Q000648:ultrastructure; D012879:Skin Physiological Phenomena
D007797:Laminin; D011506:Proteins; D003094:Collagen