Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments.

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Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. / Woods, A; Couchman, J R; Johansson, S; Höök, M.

I: EMBO Journal, Bind 5, Nr. 4, 1986, s. 665-70.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Woods, A, Couchman, JR, Johansson, S & Höök, M 1986, 'Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments.', EMBO Journal, bind 5, nr. 4, s. 665-70.

APA

Woods, A., Couchman, J. R., Johansson, S., & Höök, M. (1986). Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. EMBO Journal, 5(4), 665-70.

Vancouver

Woods A, Couchman JR, Johansson S, Höök M. Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. EMBO Journal. 1986;5(4):665-70.

Author

Woods, A ; Couchman, J R ; Johansson, S ; Höök, M. / Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. I: EMBO Journal. 1986 ; Bind 5, Nr. 4. s. 665-70.

Bibtex

@article{be8fe780598411dd8d9f000ea68e967b,
title = "Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments.",
abstract = "Fibronectin has been shown previously to promote complete cell adhesion in the absence of other serum components or de novo protein synthesis. Recently a sequence of four amino acids from the cell-binding domain of fibronectin has been termed the 'cell recognition site' of this multidomain molecule since it mediates cell attachment and inhibits cell adhesion to intact fibronectin. We show here, however, that substrata coated with an isolated cell-binding domain of fibronectin are not sufficient for complete cell adhesion; cells attach and spread but, unlike those adhering to intact fibronectin, they do not form stress fibres terminating in focal adhesions. An additional external stimulus is needed for this cytoskeletal reorganisation and may be provided by one of two heparin-binding fragments of fibronectin. The two 'signals' required for complete adhesion need not be provided simultaneously since focal adhesion formation can be promoted by stimulating cells pre-spread on a cell-binding fragment of fibronectin with a soluble heparin-binding fragment. This second stimulation may involve cell membrane heparan sulphate proteoglycans.",
author = "A Woods and Couchman, {J R} and S Johansson and M H{\"o}{\"o}k",
note = "Keywords: Antibodies; Cell Adhesion; Cytoskeleton; Embryo, Mammalian; Female; Fibroblasts; Fibronectins; Humans; Peptide Fragments; Pregnancy",
year = "1986",
language = "English",
volume = "5",
pages = "665--70",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "4",

}

RIS

TY - JOUR

T1 - Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments.

AU - Woods, A

AU - Couchman, J R

AU - Johansson, S

AU - Höök, M

N1 - Keywords: Antibodies; Cell Adhesion; Cytoskeleton; Embryo, Mammalian; Female; Fibroblasts; Fibronectins; Humans; Peptide Fragments; Pregnancy

PY - 1986

Y1 - 1986

N2 - Fibronectin has been shown previously to promote complete cell adhesion in the absence of other serum components or de novo protein synthesis. Recently a sequence of four amino acids from the cell-binding domain of fibronectin has been termed the 'cell recognition site' of this multidomain molecule since it mediates cell attachment and inhibits cell adhesion to intact fibronectin. We show here, however, that substrata coated with an isolated cell-binding domain of fibronectin are not sufficient for complete cell adhesion; cells attach and spread but, unlike those adhering to intact fibronectin, they do not form stress fibres terminating in focal adhesions. An additional external stimulus is needed for this cytoskeletal reorganisation and may be provided by one of two heparin-binding fragments of fibronectin. The two 'signals' required for complete adhesion need not be provided simultaneously since focal adhesion formation can be promoted by stimulating cells pre-spread on a cell-binding fragment of fibronectin with a soluble heparin-binding fragment. This second stimulation may involve cell membrane heparan sulphate proteoglycans.

AB - Fibronectin has been shown previously to promote complete cell adhesion in the absence of other serum components or de novo protein synthesis. Recently a sequence of four amino acids from the cell-binding domain of fibronectin has been termed the 'cell recognition site' of this multidomain molecule since it mediates cell attachment and inhibits cell adhesion to intact fibronectin. We show here, however, that substrata coated with an isolated cell-binding domain of fibronectin are not sufficient for complete cell adhesion; cells attach and spread but, unlike those adhering to intact fibronectin, they do not form stress fibres terminating in focal adhesions. An additional external stimulus is needed for this cytoskeletal reorganisation and may be provided by one of two heparin-binding fragments of fibronectin. The two 'signals' required for complete adhesion need not be provided simultaneously since focal adhesion formation can be promoted by stimulating cells pre-spread on a cell-binding fragment of fibronectin with a soluble heparin-binding fragment. This second stimulation may involve cell membrane heparan sulphate proteoglycans.

M3 - Journal article

C2 - 3709521

VL - 5

SP - 665

EP - 670

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 4

ER -

ID: 5167495