Premium
Tumour necrosis factor‐α interacts with biglycan and decorin
Author(s) -
Tufvesson Ellen,
Westergren-Thorsson Gunilla
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03439-7
Subject(s) - decorin , biglycan , chemistry , proteoglycan , extracellular matrix , tumor necrosis factor alpha , microbiology and biotechnology , proinflammatory cytokine , biophysics , biochemistry , biology , immunology , inflammation
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 K d s 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 K d s, 0.26 μM and 0.81 μM for biglycan and decorin respectively. There was also binding to dermatan sulphate, with a K d 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.