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J. Biol. Chem., Vol. 278, Issue 11, 9576-9584, March 14, 2003
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From the The ADAMs (a disintegrin
and metalloprotease) comprise a large family of
multidomain proteins with cell-binding and metalloprotease activities.
The ADAM12 cysteine-rich domain (rADAM12-cys) supports cell
attachment using syndecan-4 as a primary cell surface receptor that
subsequently triggers
ADAM12/Syndecan-4 Signaling Promotes
1
Integrin-dependent Cell Spreading through Protein Kinase
C
and RhoA*
,,,,
,
Institute of Molecular Pathology, University
of Copenhagen, Frederik V's vej 11, DK-2100, Copenhagen, Denmark, the
§ Division of Molecular Medicine, Lund University, SE-20502
Malmö, Sweden, the ¶ Department of Vascular Biology VB-1,
The Scripps Research Institute, La Jolla, California 92037, the
Department of Pathology, Beth Israel Deaconess Medical Center,
Harvard Medical School, Boston, Massachusetts 02215, and the
** Division of Biomedical Sciences, Imperial College London,
SW7 2AZ, London, United Kingdom
1
integrin-dependent cell spreading, stress fiber assembly,
and focal adhesion formation. This process contrasts with cell adhesion
on fibronectin, which is integrin-initiated but
syndecan-4-dependent. In the present study, we investigated ADAM12/syndecan-4 signaling leading to cell spreading and stress fiber
formation. We demonstrate that syndecan-4, when present in significant
amounts, promotes 1 integrin-dependent cell
spreading and stress fiber formation in response to rADAM12-cys. A
mutant form of syndecan-4 deficient in protein kinase C (PKC)
activation or a different member of the syndecan family, syndecan-2,
was unable to promote cell spreading. GF109203X and Gö6976,
inhibitors of PKC, completely inhibited ADAM12/syndecan-4-induced cell
spreading. Expression of syndecan-4, but not syn4
I, resulted in the
accumulation of activated 1 integrins at the cell
periphery in Chinese hamster ovary 1 cells as revealed by 12G10
staining. Further, expression of myristoylated, constitutively active
PKC resulted in 1 integrin-dependent cell
spreading, but additional activation of RhoA was required to induce
stress fiber formation. In summary, these data provide novel
insights into syndecan-4 signaling. Syndecan-4 can promote cell
spreading in a 1 integrin-dependent fashion
through PKC and RhoA, and PKC and RhoA likely function in
separate pathways.
*
This work was supported by grants from the Danish Cancer
Society, The Danish Medical Research Council, The Neye-Foundation, Novo
Nordisk, Haensch, Munksholm, Velux, and Dansk Kraeftforsknings Fond (to
U. W.), Wellcome Trust Program Grant 065940, and National Institutes
of Health Grants GM50194 (to J. R. C.) and CA80789 (to A. M. M.).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.
To whom correspondence should be addressed: Institute of
Molecular Pathology, University of Copenhagen, Frederik V's vej 11, DK-2100, Copenhagen, Denmark. Tel.: 45-3532-6056; Fax: 45-3532-6081; E-mail: ullaw@pai.ku.dk.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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