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J Biol Chem, Vol. 273, Issue 9, 5146-5154, February 27, 1998
From the We have shown previously that Rho plays a pivotal
role in 1-oleoyl-lysophosphatidic acid (LPA)-dependent
invasion of rat hepatoma cells (MM1). Herein we made stable
transfectants of MM1 expressing active and Botulinum
exoenzyme C3 (C3)-sensitive (Val14), or active and
C3-insensitive (Val14/Ile41) forms of human
RhoA. Both transfectants showed greatly promoted invasive ability
in vitro in the absence of LPA as well as in vivo, adherence to the dish with scattered shape, and enhanced phosphorylation level of 20-kDa myosin light chain (MLC20). A specific MLC kinase inhibitor (KT5926) could inhibit their
invasion and the phosphorylation level of MLC20. Stable active RhoA
transfectants of W1 cells (low invasive counterpart of MM1) also
demonstrated promoted invasive ability in vitro and
in vivo, and enhanced phosphorylation level of MLC20. C3
treatment inhibited the invasiveness of the Val14 RhoA
transfectant but not that of the Val14/Ile41
RhoA transfectant. LPA enhanced the invasiveness of both transfectants, and this enhancement was abolished by the C3 treatment. These results
suggested that 1) the Rho signaling pathway and actomyosin system were
linked in the transmigration of tumor cells, and 2) expressed active
RhoA enhanced LPA-induced tumor cell invasion via the activation of
endogenous RhoA pathway, indicating a positive feedback mechanism in
the activation of RhoA.
Small GTP-binding Protein Rho Stimulates the Actomyosin System,
Leading to Invasion of Tumor Cells
Department of Tumor Biochemistry, Osaka
Medical Center for Cancer and Cardiovascular Diseases, Osaka 537, Japan and the § Department of Molecular Biology and
Biochemistry, Rutgers University,
Piscataway, New Jersey 08854-1059
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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