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Tendon cells produce gelatinases in response to type I collagen attachment
Author(s) -
Ritty Timothy M.,
Herzog Jeremy
Publication year - 2003
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1016/s0736-0266(02)00200-0
Subject(s) - downregulation and upregulation , gelatinases , extracellular matrix , chemistry , type i collagen , matrix metalloproteinase , microbiology and biotechnology , tendon , wound healing , collagen, type i, alpha 1 , gelatinase , anatomy , immunology , biochemistry , biology , endocrinology , gene
Cells that carry out wound healing must be able to perform catabolic as well as anabolic functions. As the tendon is a tissue rich in extracellular matrix (ECM) proteins, we hypothesized that cells which participate in tendon healing should be able to produce proteases that would allow the remodeling of such a tissue. To this end, we assessed the ability of endotenon cells isolated from canine flexor digitorum profundus tendon and from surrounding parietal sheath to produce the gelatinases MMP‐2 and MMP‐9. Endotenon and sheath cells cultured in vitro on polystyrene produced small amounts of MMP‐2 and MMP‐9 was not detectable. When cultured on polystyrene coated with type I collagen, the cells upregulated MMP‐2 production and MMP‐9 production was induced. No other ECM protein elicited this response nor did other cell lines respond in this way after attachment to type I collagen. The two gelatinases were identified by immunological methods, ability to bind gelatin, size, metal ion requirement, serine protease inhibitor insensitivity, and APMA activation. For cells grown on collagen‐coated plastic, gelatinase upregulation was proportional to the amount of ligand present until saturation was reached. For any group of fresh tendon cells, MMP‐2 and MMP‐9 upregulation was greater in a three dimensional collagen gel than the highest response from the same group under two dimensional culture conditions. Attachment of the cells to type I collagen increased the ratio of active to inactive MMP‐2. Dexamethasone inhibited the upregulation of both MMP‐2 and MMP‐9. These results show that ECM proteins can influence both the production and the state of activation of these matrix metalloproteinases. © 2002 Orthopaedic Research Society. Published by Elsevier Science Ltd. All rights reserved.