Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways.

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways. / Whiteford, James; Behrends, Volker; Kirby, Hishani; Kusche-Gullberg, Marion; Muramatsu, Takashi; Couchman, John R.

In: Experimental Cell Research, Vol. 313, No. 18, 2007, p. 3902-13.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Whiteford, J, Behrends, V, Kirby, H, Kusche-Gullberg, M, Muramatsu, T & Couchman, JR 2007, 'Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways.', Experimental Cell Research, vol. 313, no. 18, pp. 3902-13. https://doi.org/10.1016/j.yexcr.2007.08.002

APA

Whiteford, J., Behrends, V., Kirby, H., Kusche-Gullberg, M., Muramatsu, T., & Couchman, J. R. (2007). Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways. Experimental Cell Research, 313(18), 3902-13. https://doi.org/10.1016/j.yexcr.2007.08.002

Vancouver

Whiteford J, Behrends V, Kirby H, Kusche-Gullberg M, Muramatsu T, Couchman JR. Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways. Experimental Cell Research. 2007;313(18):3902-13. https://doi.org/10.1016/j.yexcr.2007.08.002

Author

Whiteford, James ; Behrends, Volker ; Kirby, Hishani ; Kusche-Gullberg, Marion ; Muramatsu, Takashi ; Couchman, John R. / Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways. In: Experimental Cell Research. 2007 ; Vol. 313, No. 18. pp. 3902-13.

Bibtex

@article{d04072c0596011dd8d9f000ea68e967b,
title = "Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways.",
abstract = "Syndecans are transmembrane proteoglycans that support integrin-mediated adhesion. Well documented is the contribution of syndecan-4 that interacts through its heparan sulphate chains to promote focal adhesion formation in response to fibronectin domains. This process has requirements for integrin and signaling through the cytoplasmic domain of syndecan-4. Here an alternate pathway mediated by the extracellular domains of syndecans-2 and -4 is characterized that is independent of both heparan sulphate and syndecan signaling. This pathway is restricted to mesenchymal cells and was not seen in any epithelial cell line tested, apart from vascular endothelia. The syndecan ectodomains coated as substrates promoted integrin-dependent attachment, spreading and focal adhesion formation. Syndecan-4 null cells were competent, as were fibroblasts compromised in heparan sulphate synthesis that were unable to form focal adhesions in response to fibronectin. Consistent with actin cytoskeleton organization, the process required Rho-GTP and Rho kinase. While syndecan-2 and -4 ectodomains could both promote integrin-mediated adhesion, their pathways were distinct, as shown by competition assays. Evidence for an indirect interaction of beta1 integrin with both syndecan ectodomains was obtained, all of which suggests a distinct mechanism of integrin-mediated adhesion.",
author = "James Whiteford and Volker Behrends and Hishani Kirby and Marion Kusche-Gullberg and Takashi Muramatsu and Couchman, {John R}",
note = "Keywords: Animals; COS Cells; Cell Adhesion; Cell Line; Cercopithecus aethiops; Endothelial Cells; Fibroblasts; Focal Adhesions; Heparitin Sulfate; Humans; Integrins; Jurkat Cells; Mesoderm; Mice; Protein Structure, Tertiary; Rats; Syndecan-2; Syndecan-4; rho-Associated Kinases",
year = "2007",
doi = "10.1016/j.yexcr.2007.08.002",
language = "English",
volume = "313",
pages = "3902--13",
journal = "Experimental Cell Research",
issn = "0014-4827",
publisher = "Academic Press",
number = "18",

}

RIS

TY - JOUR

T1 - Syndecans promote integrin-mediated adhesion of mesenchymal cells in two distinct pathways.

AU - Whiteford, James

AU - Behrends, Volker

AU - Kirby, Hishani

AU - Kusche-Gullberg, Marion

AU - Muramatsu, Takashi

AU - Couchman, John R

N1 - Keywords: Animals; COS Cells; Cell Adhesion; Cell Line; Cercopithecus aethiops; Endothelial Cells; Fibroblasts; Focal Adhesions; Heparitin Sulfate; Humans; Integrins; Jurkat Cells; Mesoderm; Mice; Protein Structure, Tertiary; Rats; Syndecan-2; Syndecan-4; rho-Associated Kinases

PY - 2007

Y1 - 2007

N2 - Syndecans are transmembrane proteoglycans that support integrin-mediated adhesion. Well documented is the contribution of syndecan-4 that interacts through its heparan sulphate chains to promote focal adhesion formation in response to fibronectin domains. This process has requirements for integrin and signaling through the cytoplasmic domain of syndecan-4. Here an alternate pathway mediated by the extracellular domains of syndecans-2 and -4 is characterized that is independent of both heparan sulphate and syndecan signaling. This pathway is restricted to mesenchymal cells and was not seen in any epithelial cell line tested, apart from vascular endothelia. The syndecan ectodomains coated as substrates promoted integrin-dependent attachment, spreading and focal adhesion formation. Syndecan-4 null cells were competent, as were fibroblasts compromised in heparan sulphate synthesis that were unable to form focal adhesions in response to fibronectin. Consistent with actin cytoskeleton organization, the process required Rho-GTP and Rho kinase. While syndecan-2 and -4 ectodomains could both promote integrin-mediated adhesion, their pathways were distinct, as shown by competition assays. Evidence for an indirect interaction of beta1 integrin with both syndecan ectodomains was obtained, all of which suggests a distinct mechanism of integrin-mediated adhesion.

AB - Syndecans are transmembrane proteoglycans that support integrin-mediated adhesion. Well documented is the contribution of syndecan-4 that interacts through its heparan sulphate chains to promote focal adhesion formation in response to fibronectin domains. This process has requirements for integrin and signaling through the cytoplasmic domain of syndecan-4. Here an alternate pathway mediated by the extracellular domains of syndecans-2 and -4 is characterized that is independent of both heparan sulphate and syndecan signaling. This pathway is restricted to mesenchymal cells and was not seen in any epithelial cell line tested, apart from vascular endothelia. The syndecan ectodomains coated as substrates promoted integrin-dependent attachment, spreading and focal adhesion formation. Syndecan-4 null cells were competent, as were fibroblasts compromised in heparan sulphate synthesis that were unable to form focal adhesions in response to fibronectin. Consistent with actin cytoskeleton organization, the process required Rho-GTP and Rho kinase. While syndecan-2 and -4 ectodomains could both promote integrin-mediated adhesion, their pathways were distinct, as shown by competition assays. Evidence for an indirect interaction of beta1 integrin with both syndecan ectodomains was obtained, all of which suggests a distinct mechanism of integrin-mediated adhesion.

U2 - 10.1016/j.yexcr.2007.08.002

DO - 10.1016/j.yexcr.2007.08.002

M3 - Journal article

C2 - 17870067

VL - 313

SP - 3902

EP - 3913

JO - Experimental Cell Research

JF - Experimental Cell Research

SN - 0014-4827

IS - 18

ER -

ID: 5160709