[HTML][HTML] Tumour necrosis factor-α interacts with biglycan and decorin
E Tufvesson, G Westergren-Thorsson - FEBS letters, 2002 - Elsevier
E Tufvesson, G Westergren-Thorsson
FEBS letters, 2002•ElsevierSeveral 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-α (TNF-α) binds to both biglycan and decorin with
Kds of 0.81 μM and 1.23 μM respectively, a binding that was confirmed by Scatchard plots
using a solid phase assay. Binding occurs preferentially via the core protein, shown by lower
Kds, 0.26 μM and 0.81 μM for biglycan and decorin respectively. There was also binding to …
proteoglycans, such as biglycan and decorin. Using surface plasmon resonance, we show
for the first time that tumour necrosis factor-α (TNF-α) binds to both biglycan and decorin with
Kds of 0.81 μM and 1.23 μM respectively, a binding that was confirmed by Scatchard plots
using a solid phase assay. Binding occurs preferentially via the core protein, shown by lower
Kds, 0.26 μM and 0.81 μM for biglycan and decorin respectively. There was also binding to …
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-α (TNF-α) binds to both biglycan and decorin with Kds of 0.81 μM and 1.23 μM respectively, a binding that was confirmed by Scatchard plots using a solid phase assay. Binding occurs preferentially via the core protein, shown by lower Kds, 0.26 μM and 0.81 μM for biglycan and decorin respectively. There was also binding to dermatan sulphate, with a Kd of 10.53 μM. The function of this interaction between TNF-α 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.
Elsevier