A matrix metalloproteinase inhibitor which prevents fibroblast‐mediated collagen lattice contraction

FEBS Letters

Wood, Edward J¹  Karran, Eric H²  Scott, Kate A¹ 

[1] School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK;Molecular Neurobiological Research, SmithKline Beecham Pharmaceuticals, Harlow CM19 5AW, UK

关键词: Lattice contraction;    Marimastat;    Interstitial collagenase activity;    MMP;    matrix metalloproteinase;    TIMP;    tissue inhibitor of matrix metalloproteinases;    ECM;    extracellular matrix;    DE;    dermal equivalent;    MMP-1;    interstitial collagenase;    APMA;    p-aminophenylmercuric acetate;    DMEM;    Dulbecco's modified Eagle's medium;    NBCS;    newborn calf serum;   

DOI  :  10.1016/S0014-5793(98)01542-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Matrix metalloproteinases (MMPs) and the specific tissue inhibitors of metalloproteinases (TIMPs) are involved in tissue turnover in normal and pathological processes including wound healing. Marimastat, a potent inhibitor of MMPs, was used to investigate the role of MMPs in an in vitro wound contraction model, the dermal equivalent, in which fibroblasts are grown in a collagen matrix. Marimastat inhibited fibroblast-mediated lattice contraction and this inhibition was reversible upon removal of the inhibitor, indicating that MMPs play an important role in fibroblast-mediated collagen lattice contraction, modelling what may happen when granulation tissue contracts in a healing wound.

【 授权许可】

Unknown