Tumour necrosis factor-alpha interacts with biglycan and decorin.
Author
Summary, in English
Several interactions of cytokines with extracellular matrix molecules are mediated by proteoglycans, such as biglycan and decorin. Using surface plasmon resonance, we show for the first time that tumour necrosis factor-alpha (TNF-alpha) binds to both biglycan and decorin with K(d)s of 0.81 microM and 1.23 microM respectively, a binding that was confirmed by Scatchard plots using a solid phase assay. Binding occurs preferentially via the core protein, shown by lower K(d)s, 0.26 microM and 0.81 microM for biglycan and decorin respectively. There was also binding to dermatan sulphate, with a K(d) of 10.53 microM. The function of this interaction between TNF-alpha and biglycan and decorin is not known, but we suggest that the differential localisation of the proteoglycans enables the cytokines to be immobilised in different environments.
Department/s
Publishing year
2002
Language
English
Pages
124-128
Publication/Series
FEBS Letters
Volume
530
Issue
1-3
Links
Document type
Journal article
Publisher
Wiley-Blackwell
Topic
- Biological Sciences
Status
Published
Research group
- Lung physiology and biomarkers
ISBN/ISSN/Other
- ISSN: 1873-3468