The adhesion of baby hamster kidney 21C/13 fibroblasts to surfaces of passivated titanium, carbon fibers, bioactive glasses B5 and B6, fibronectin-precoated passivated titanium, and fibronectin-precoated B6 was quantified. The order of adhesive cell avidity for the uncoated surfaces was passivated t
Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
β Scribed by Eva Engvall; Erkki Ruoslahti
- Publisher
- John Wiley and Sons
- Year
- 1977
- Tongue
- French
- Weight
- 416 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0020-7136
No coin nor oath required. For personal study only.
β¦ Synopsis
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.
π SIMILAR VOLUMES
A scintillation proximity assay (SPA) has been developed to measure binding of alpha 5 beta 1 integrin, a heterodimeric cell-surface adhesion receptor, to fibronectin. This assay utilizes an anti-beta 1 integrin monoclonal antibody to simultaneously capture alpha 5 beta 1 from a cellular lysate and