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Vol. 9, Issue 5, 993-1006, May 1998
and
Department of Molecular Biology and Biochemistry, Rutgers
University, Busch Campus, Piscataway, New Jersey 08855
Fascin is an actin-bundling protein that is found in membrane
ruffles, microspikes, and stress fibers. The expression of fascin is
greatly increased in many transformed cells, as well as in specialized
normal cells including neuronal cells and antigen-presenting dendritic
cells. A morphological characteristic common to these cells expressing
high levels of fascin is the development of many membrane protrusions
in which fascin is predominantly present. To examine whether fascin
contributes to the alterations in microfilament organization at the
cell periphery, we have expressed fascin in LLC-PK1 epithelial cells to
levels as high as those found in transformed cells and in specialized
normal cells. Expression of fascin results in large changes in
morphology, the actin cytoskeleton, and cell motility:
fascin-transfected cells form an increased number of longer and thicker
microvilli on apical surfaces, extend lamellipodia-like structures at
basolateral surfaces, and show disorganization of cell-cell contacts.
Cell migration activity is increased by 8-17 times when assayed by
modified Boyden chamber. Microinjection of a fascin protein into
LLC-PK1 cells causes similar morphological alterations including the
induction of lamellipodia at basolateral surfaces and formation of an
increased number of microvilli on apical surfaces. Furthermore,
microinjection of fascin into REF-52 cells, normal fibroblasts, induces
the formation of many lamellipodia at all regions of cell periphery.
These results together suggest that fascin is directly responsible for
membrane protrusions through reorganization of the microfilament
cytoskeleton at the cell periphery.
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