Tumour necrosis factor‐α interacts with biglycan and decorin

FEBS Letters

Tufvesson, Ellen¹  Westergren-Thorsson, Gunilla¹ 

[1] Section for Cell and Matrix Biology, Department of Cell and Molecular Biology, BMC C13, Lund University, 221 84 Lund, Sweden

关键词: Biglycan;    Decorin;    Interaction;    Tumor necrosis factor-α;    CS;    chondroitin sulphate;    DS;    dermatan sulphate;    GAG;    glycosaminoglycan;    TGF-β;    transforming growth factor-β;    TNF-α;    tumour necrosis factor-α;   

DOI  :  10.1016/S0014-5793(02)03439-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 _ds 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 _ds, 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.

【 授权许可】

Unknown