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 tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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