Forward transport of glycoproteins on leading lamellipodia in locomoting cells.
In several types of locomoting cells, active rearward transport of particles on the cell surface has been observed and correlated with motility. No forward transport of particles has previously been reported, however. Here we report rapid forward transport of concanavalin A-coated gold particles on the dorsal surfaces of lamellipodia of fish epidermal keratocytes. These movements are active, not diffusive, and more rapid than either rearward particle transport or the rate of cell locomotion. We observed forward transport in migrating, but not in stationary cells, and could block the movement by treatment with cytochalasin D. These studies demonstrate for the first time that small numbers of glycoproteins can be actively transported on the surface of the cell to the front of the lamellipodium. We suggest that this mechanism transports proteins involved in cell locomotion, such as proteins necessary for adhesion, and could also produce an extensile force.
Kucik
D F
DF
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.
Elson
E L
EL
Sheetz
M P
MP
D000818:Animals; D001692:Biological Transport / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects; D003208:Concanavalin A; D015638:Cytochalasin D; D003572:Cytochalasins / Q000494:pharmacology; D003593:Cytoplasm / Q000378:metabolism / Q000502:physiology; D004058:Diffusion; D000078404:Epidermal Cells; D006046:Gold; D006054:Goldfish; D066298:In Vitro Techniques; D007633:Keratins; D008562:Membrane Glycoproteins / Q000378:metabolism*; D011336:Probability
D003572:Cytochalasins; D008562:Membrane Glycoproteins; D003208:Concanavalin A; D015638:Cytochalasin D; D007633:Keratins; D006046:Gold