Beta 1 integrin-mediated collagen gel contraction is stimulated by PDGF
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1105496
- author
- Gullberg, Donald ; Tingström, Anders LU ; Thuresson, Ann-Charlotte ; Olsson, Lennart ; Terracio, Louis ; Borg, Thomas K and Rubin, Kristofer
- publishing date
- 1990
- 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
- 2016-04-01 12:25:10
- date last changed
- 2021-09-19 05:13:25
@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}},
doi = {{10.1016/0014-4827(90)90305-T}},
volume = {{186}},
year = {{1990}},
}