Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts.

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. / Woods, A; Longley, R L; Tumova, S; Couchman, J R.

In: Archives of Biochemistry and Biophysics, Vol. 374, No. 1, 2000, p. 66-72.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Woods, A, Longley, RL, Tumova, S & Couchman, JR 2000, 'Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts.', Archives of Biochemistry and Biophysics, vol. 374, no. 1, pp. 66-72. https://doi.org/10.1006/abbi.1999.1607

APA

Woods, A., Longley, R. L., Tumova, S., & Couchman, J. R. (2000). Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Archives of Biochemistry and Biophysics, 374(1), 66-72. https://doi.org/10.1006/abbi.1999.1607

Vancouver

Woods A, Longley RL, Tumova S, Couchman JR. Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Archives of Biochemistry and Biophysics. 2000;374(1):66-72. https://doi.org/10.1006/abbi.1999.1607

Author

Woods, A ; Longley, R L ; Tumova, S ; Couchman, J R. / Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. In: Archives of Biochemistry and Biophysics. 2000 ; Vol. 374, No. 1. pp. 66-72.

Bibtex

@article{ca102d90597011dd8d9f000ea68e967b,

title = "Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts.",

abstract = "Cell adhesion to extracellular matrix involves signaling mechanisms which control attachment, spreading and the formation of focal adhesions and stress fibers. Fibronectin can provide sufficient signals for all three processes, even when protein synthesis is prevented by cycloheximide. Primary fibroblasts attach and spread following integrin ligation, but do not form focal adhesions unless treated with a heparin-binding fragment of fibronectin (HepII), a peptide from this domain, or phorbol esters to activate protein kinase C. Syndecan-4 heparan sulfate proteoglycan is a transmembrane component present together with integrins in focal adhesions. Syndecan-4 binds and activates protein kinase Calpha, whose activity is needed for focal adhesion formation. We now report that the glycosaminoglycan chains of syndecan-4 bind recombinant HepII and it is incorporated into forming focal adhesions.",

author = "A Woods and Longley, {R L} and S Tumova and Couchman, {J R}",

note = "Keywords: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Cell Adhesion; Cells, Cultured; Fibroblasts; Fibronectins; Heparin; Membrane Glycoproteins; Oligopeptides; Protein Binding; Proteoglycans; Rats; Syndecan-4; Tetradecanoylphorbol Acetate",

year = "2000",

doi = "10.1006/abbi.1999.1607",

language = "English",

volume = "374",

pages = "66--72",

journal = "Archives of Biochemistry and Biophysics",

issn = "0003-9861",

publisher = "Academic Press",

number = "1",

}

RIS

TY - JOUR

T1 - Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts.

AU - Woods, A

AU - Longley, R L

AU - Tumova, S

AU - Couchman, J R

N1 - Keywords: Amino Acid Sequence; Animals; Binding Sites; Binding, Competitive; Cell Adhesion; Cells, Cultured; Fibroblasts; Fibronectins; Heparin; Membrane Glycoproteins; Oligopeptides; Protein Binding; Proteoglycans; Rats; Syndecan-4; Tetradecanoylphorbol Acetate

PY - 2000

Y1 - 2000

N2 - Cell adhesion to extracellular matrix involves signaling mechanisms which control attachment, spreading and the formation of focal adhesions and stress fibers. Fibronectin can provide sufficient signals for all three processes, even when protein synthesis is prevented by cycloheximide. Primary fibroblasts attach and spread following integrin ligation, but do not form focal adhesions unless treated with a heparin-binding fragment of fibronectin (HepII), a peptide from this domain, or phorbol esters to activate protein kinase C. Syndecan-4 heparan sulfate proteoglycan is a transmembrane component present together with integrins in focal adhesions. Syndecan-4 binds and activates protein kinase Calpha, whose activity is needed for focal adhesion formation. We now report that the glycosaminoglycan chains of syndecan-4 bind recombinant HepII and it is incorporated into forming focal adhesions.

AB - Cell adhesion to extracellular matrix involves signaling mechanisms which control attachment, spreading and the formation of focal adhesions and stress fibers. Fibronectin can provide sufficient signals for all three processes, even when protein synthesis is prevented by cycloheximide. Primary fibroblasts attach and spread following integrin ligation, but do not form focal adhesions unless treated with a heparin-binding fragment of fibronectin (HepII), a peptide from this domain, or phorbol esters to activate protein kinase C. Syndecan-4 heparan sulfate proteoglycan is a transmembrane component present together with integrins in focal adhesions. Syndecan-4 binds and activates protein kinase Calpha, whose activity is needed for focal adhesion formation. We now report that the glycosaminoglycan chains of syndecan-4 bind recombinant HepII and it is incorporated into forming focal adhesions.

U2 - 10.1006/abbi.1999.1607

DO - 10.1006/abbi.1999.1607

M3 - Journal article

C2 - 10640397

VL - 374

SP - 66

EP - 72

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -

ID: 5163755