A matrix metalloproteinase inhibitor which prevents fibroblast-mediated collagen lattice contraction.
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.
Scott
K A
KA
School of Biochemistry and Molecular Biology, University of Leeds, UK.
Wood
E J
EJ
Karran
E H
EH
D000328:Adult; D002478:Cells, Cultured; D003094:Collagen / Q000187:drug effects / Q000502:physiology*; D017364:Collagenases / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006877:Hydroxamic Acids / Q000494:pharmacology*; D020781:Matrix Metalloproteinase 1; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D012867:Skin / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*
D006877:Hydroxamic Acids; D003094:Collagen; C100342:marimastat; D017364:Collagenases; D008666:Metalloendopeptidases; D020781:Matrix Metalloproteinase 1