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Beta 1 integrin-mediated collagen gel contraction is stimulated by PDGF

Gullberg, Donald; Tingström, Anders LU ; Thuresson, Ann-Charlotte; Olsson, Lennart; Terracio, Louis; Borg, Thomas K and Rubin, Kristofer (1990) In Experimental Cell Research 186(2). p.264-272
Abstract
The attachment of primary rat hepatocytes and fibroblasts to collagen type I is mediated by non-RGD-dependent beta 1 integrin matrix receptors. In this report we describe a novel 96-well microtiter plate assay for the quantification of fibroblast-mediated contraction of floating collagen type I gels. Fetal calf serum and platelet-derived growth factor (PDGF), but not transforming growth factor-beta 1, stimulated primary rat heart fibroblasts and normal human diploid fibroblasts (AG 1518) to contract collagen gels to less than 10% of the initial gel volume within a 24-h incubation period. Rabbit polyclonal antibodies directed to the rat hepatocyte integrin beta 1-chain inhibited the PDGF-stimulated collagen gel contraction. The inhibitory... (More)
The attachment of primary rat hepatocytes and fibroblasts to collagen type I is mediated by non-RGD-dependent beta 1 integrin matrix receptors. In this report we describe a novel 96-well microtiter plate assay for the quantification of fibroblast-mediated contraction of floating collagen type I gels. Fetal calf serum and platelet-derived growth factor (PDGF), but not transforming growth factor-beta 1, stimulated primary rat heart fibroblasts and normal human diploid fibroblasts (AG 1518) to contract collagen gels to less than 10% of the initial gel volume within a 24-h incubation period. Rabbit polyclonal antibodies directed to the rat hepatocyte integrin beta 1-chain inhibited the PDGF-stimulated collagen gel contraction. The inhibitory activity on contraction of the anti-beta 1 integrin IgG could be overcome by adding higher doses of PDGF. The contraction process was not blocked by anti-fibronectin IgG nor by synthetic peptides containing the tripeptide Arg-Gly-Asp (RGD), in concentrations that readily blocked fibroblast attachment to fibronectin-coated planar substrates. Autologous fibronectin or control peptides containing the tripeptide Arg-Gly-Glu were without effect. Immunofluorescence microscopy on fibroblasts grown within collagen gels revealed a punctate distribution of the beta 1 integrin and a lack of detectable levels of endogenously produced fibronectin. Collectively these data suggest a role for integrin collagen receptors with affinity for collagen fibers, distinct from the previously described RGD-dependent fibronectin receptors, in the fibronectin-independent PDGF-stimulated collagen gel contraction process. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Experimental Cell Research
volume
186
issue
2
pages
264 - 272
publisher
Academic Press
external identifiers
  • pmid:2298242
  • scopus:0025178575
ISSN
1090-2422
DOI
10.1016/0014-4827(90)90305-T
language
English
LU publication?
no
id
12289e12-5474-4694-b445-9bf8bc6bd92e (old id 1105496)
date added to LUP
2008-08-05 16:37:48
date last changed
2017-09-03 03:53:42
@article{12289e12-5474-4694-b445-9bf8bc6bd92e,
  abstract     = {The attachment of primary rat hepatocytes and fibroblasts to collagen type I is mediated by non-RGD-dependent beta 1 integrin matrix receptors. In this report we describe a novel 96-well microtiter plate assay for the quantification of fibroblast-mediated contraction of floating collagen type I gels. Fetal calf serum and platelet-derived growth factor (PDGF), but not transforming growth factor-beta 1, stimulated primary rat heart fibroblasts and normal human diploid fibroblasts (AG 1518) to contract collagen gels to less than 10% of the initial gel volume within a 24-h incubation period. Rabbit polyclonal antibodies directed to the rat hepatocyte integrin beta 1-chain inhibited the PDGF-stimulated collagen gel contraction. The inhibitory activity on contraction of the anti-beta 1 integrin IgG could be overcome by adding higher doses of PDGF. The contraction process was not blocked by anti-fibronectin IgG nor by synthetic peptides containing the tripeptide Arg-Gly-Asp (RGD), in concentrations that readily blocked fibroblast attachment to fibronectin-coated planar substrates. Autologous fibronectin or control peptides containing the tripeptide Arg-Gly-Glu were without effect. Immunofluorescence microscopy on fibroblasts grown within collagen gels revealed a punctate distribution of the beta 1 integrin and a lack of detectable levels of endogenously produced fibronectin. Collectively these data suggest a role for integrin collagen receptors with affinity for collagen fibers, distinct from the previously described RGD-dependent fibronectin receptors, in the fibronectin-independent PDGF-stimulated collagen gel contraction process.},
  author       = {Gullberg, Donald and Tingström, Anders and Thuresson, Ann-Charlotte and Olsson, Lennart and Terracio, Louis and Borg, Thomas K and Rubin, Kristofer},
  issn         = {1090-2422},
  language     = {eng},
  number       = {2},
  pages        = {264--272},
  publisher    = {Academic Press},
  series       = {Experimental Cell Research},
  title        = {Beta 1 integrin-mediated collagen gel contraction is stimulated by PDGF},
  url          = {http://dx.doi.org/10.1016/0014-4827(90)90305-T},
  volume       = {186},
  year         = {1990},
}