Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
Abstract
Fibronectin, a plasma protein immunologically identical with a major surface protein of normal fibroblasts, was found to bind to collagen and gelatin. A solid phase enzyme immunoassay was used for the binding tests. Collagen, gelatin or various control proteins were adsorbed to a plastic surface. Binding of fibronectin was detected using purified fibronectin antibodies conjugated to alkaline phosphatase. Circulating fibronectin and fibronectin obtained from fibroblast cultures both showed specific binding to collagen and gelatin. Preparative affinity chromatography of plasma on gelatin coupled to Sepharose gave electrophoretically and immunologically pure fibronectin in high yields. Malignantly transformed fibroblasts lack surface fibronectin. Our findings suggest the possibility that this results in a lack of anchorage to the surrounding intercellular matrix, which could contribute to the malignant growth behavior.
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Fibronectin and vitronectin are commonly isolated from bovine blood plasma.
“while fibronectin and vitronectin are commonly isolated from bovine blood plasma (Engvall and Ruoslahti, 1977).”
From Challenges and solutions in transitioning to animal-free standards: a comprehensive analysis of components in human cell-based developmental neurotoxicity assays (2026) · cites this paper as Engvall and Ruoslahti, 1977
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- Authors
- Engvall, E., & Ruoslahti, E.
- Venue
- International Journal of Cancer
- Publisher
- Wiley
- Published
- 1977-07-15
- Volume
- 20
- Issue
- 1
- Pages
- 1-5
- ISSN
- 0020-7136
- 1097-0215
- Cited by
- 1,433
- References
- 0
- Language
- en
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