Premium
A matrix metalloproteinase inhibitor which prevents fibroblast‐mediated collagen lattice contraction
Author(s) -
Scott Kate A,
Wood Edward J,
Karran Eric H
Publication year - 1998
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(98)01542-7
Subject(s) - matrix metalloproteinase , fibroblast , contraction (grammar) , wound healing , type i collagen , microbiology and biotechnology , granulation tissue , chemistry , tissue inhibitor of metalloproteinase , extracellular matrix , matrix metalloproteinase inhibitor , in vitro , pathology , biochemistry , immunology , medicine , biology , endocrinology
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.