Control of morphology, cytoskeleton and migration by syndecan-4.
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Control of morphology, cytoskeleton and migration by syndecan-4. / Longley, R L; Woods, A; Fleetwood, A; Cowling, G J; Gallagher, J T; Couchman, J R.
In: Journal of Cell Science, Vol. 112 ( Pt 20), 1999, p. 3421-31.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Control of morphology, cytoskeleton and migration by syndecan-4.
AU - Longley, R L
AU - Woods, A
AU - Fleetwood, A
AU - Cowling, G J
AU - Gallagher, J T
AU - Couchman, J R
N1 - Keywords: Amino Acid Sequence; Animals; CHO Cells; Cell Adhesion; Cell Division; Cell Size; Chemotaxis; Cricetinae; Cytoskeleton; Epithelial Cells; Flow Cytometry; Liver; Membrane Glycoproteins; Molecular Sequence Data; Mutagenesis; Protein Kinase C; Proteoglycans; Rats; Recombinant Proteins; Sequence Deletion; Sequence Homology, Amino Acid; Syndecan-2; Syndecan-4; Transfection
PY - 1999
Y1 - 1999
N2 - Syndecan-4 is a widely expressed transmembrane heparan sulfate proteoglycan which localizes to focal adhesions. Previous studies showed that the syndecan-4 cytoplasmic domain can associate with and potentiate the activity of protein kinase C, which is required for focal adhesion formation. To examine further the role of syndecan-4 in cell adhesion, we expressed syndecan-4 cDNA constructs in CHO-K1 cells. Syndecan-2 transfection was used to confirm effects seen were specific for syndecan-4. Cells overexpressing full length syndecan-4 core protein exhibited a more flattened, fibroblastic morphology, with increased focal adhesion formation and decreased cell motility. Expression of a syndecan-4 core protein with either a partial or complete deletion of the cytoplasmic domain or of an antisense construct led to markedly decreased spreading and focal adhesion formation, a more epithelioid morphology, and decreased motility. Overexpression of syndecan-2 changed the adhesive phenotype, but did not markedly alter focal adhesion and microfilament bundle formation. The data suggest that syndecan-4 is a regulator of focal adhesion and stress fiber formation, and influences both morphology and migration.
AB - Syndecan-4 is a widely expressed transmembrane heparan sulfate proteoglycan which localizes to focal adhesions. Previous studies showed that the syndecan-4 cytoplasmic domain can associate with and potentiate the activity of protein kinase C, which is required for focal adhesion formation. To examine further the role of syndecan-4 in cell adhesion, we expressed syndecan-4 cDNA constructs in CHO-K1 cells. Syndecan-2 transfection was used to confirm effects seen were specific for syndecan-4. Cells overexpressing full length syndecan-4 core protein exhibited a more flattened, fibroblastic morphology, with increased focal adhesion formation and decreased cell motility. Expression of a syndecan-4 core protein with either a partial or complete deletion of the cytoplasmic domain or of an antisense construct led to markedly decreased spreading and focal adhesion formation, a more epithelioid morphology, and decreased motility. Overexpression of syndecan-2 changed the adhesive phenotype, but did not markedly alter focal adhesion and microfilament bundle formation. The data suggest that syndecan-4 is a regulator of focal adhesion and stress fiber formation, and influences both morphology and migration.
M3 - Journal article
C2 - 10504291
VL - 112 ( Pt 20)
SP - 3421
EP - 3431
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
ER -
ID: 5164352