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J. Biol. Chem., Vol. 278, Issue 15, 13039-13046, April 11, 2003
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From the Department of Physiology and
The rapid migration of intestinal epithelial cells is
important to the healing of mucosal ulcers and wounds. This cell
migration requires the presence of polyamines and the activation of
RhoA. RhoA activity, however, is not sufficient for migration
because polyamine depletion inhibited the migration of IEC-6 cells
expressing constitutively active RhoA. The current study examines
the role of Rac1 and Cdc42 in cell migration and whether their
activities are polyamine-dependent. Polyamine depletion
with
The Requirement for Polyamines for Intestinal Epithelial Cell
Migration Is Mediated through Rac1*
, and Department of Molecular Sciences, University of
Tennessee Health Science Center, Memphis, Tennessee 38163
-difluoromethylornithine inhibited the activities of RhoA,
Rac1, and Cdc42. This inhibition was prevented by supplying exogenous
putrescine in the presence of -difluoromethylornithine. IEC-6 cells
transfected with constitutively active Rac1 and Cdc42 migrated more
rapidly than vector-transfected cells, whereas cells expressing
dominant negative Rac1 and Cdc42 migrated more slowly. Polyamine
depletion had no effect on the migration of cells expressing Rac1 and
only partially inhibited the migration of those expressing Cdc42.
Although polyamine depletion caused the disappearance of actin stress
fibers in cells transfected with empty vector, it had no effect on
cells expressing Rac1. Constitutively active Rac1 increased RhoA and
Cdc42 activity in both normal and polyamine-depleted cells. These
results demonstrate that Rac1, RhoA, and Cdc42 are required for optimal
epithelial cell migration and that Rac1 activity is sufficient for cell
migration in the absence of polyamines due to its ability to activate
RhoA and Cdc42 as well as its own effects on the process of cell
migration. These data imply that the involvement of polyamines in cell
migration occurs either at Rac1 itself or upstream from Rac1.
*
This work was supported by National Institutes of Health
Grants DK 52784 (to L. R. J.) and GM 60523 (to Y. Z.) and by the Thomas A. Gerwin endowment (to L. R. J.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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