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Tissue origin and extracellular matrix control neutral proteinase activity in human fibroblast three-dimensional cultures

1996; Wiley; Volume: 168; Issue: 1 Linguagem: Inglês

10.1002/(sici)1097-4652(199607)168

1097-4652

Sandrine Lorimier, Philippe Gillery, William Hornebeck, F. Chastang, D. Laurent‐Maquin, Sylvie Bouthors, C Droullé, G Potron, François‐Xavier Maquart,

Cellular transport and secretion

Journal of Cellular PhysiologyVolume 168, Issue 1 p. 188-198 Tissue origin and extracellular matrix control neutral proteinase activity in human fibroblast three-dimensional cultures Sandrine Lorimier, Sandrine Lorimier Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, France Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorPhilippe Gillery, Philippe Gillery Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorWilliam Hornebeck, William Hornebeck Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorFrançois Chastang, François Chastang Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorDominique Laurent-Maquin, Dominique Laurent-Maquin Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorSylvie Bouthors, Sylvie Bouthors Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorChantal Droulle, Chantal Droulle Laboratoire Central d'Hématologie, Centre Hospitalier Universitaire, 51092 Reims, FranceSearch for more papers by this authorGérard Potron, Gérard Potron Laboratoire Central d'Hématologie, Centre Hospitalier Universitaire, 51092 Reims, FranceSearch for more papers by this authorFrançois-Xavier Maquart, Corresponding Author François-Xavier Maquart Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceLaboratoire de Biochimie, Faculté de Médecine, 51, rue Cognacq-Jay, 51095 Reims Cedex, FranceSearch for more papers by this author Sandrine Lorimier, Sandrine Lorimier Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, France Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorPhilippe Gillery, Philippe Gillery Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorWilliam Hornebeck, William Hornebeck Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorFrançois Chastang, François Chastang Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceSearch for more papers by this authorDominique Laurent-Maquin, Dominique Laurent-Maquin Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorSylvie Bouthors, Sylvie Bouthors Laboratoire de Recherche en Odontologie, Faculté d'Odontologie, 51100 Reims, FranceSearch for more papers by this authorChantal Droulle, Chantal Droulle Laboratoire Central d'Hématologie, Centre Hospitalier Universitaire, 51092 Reims, FranceSearch for more papers by this authorGérard Potron, Gérard Potron Laboratoire Central d'Hématologie, Centre Hospitalier Universitaire, 51092 Reims, FranceSearch for more papers by this authorFrançois-Xavier Maquart, Corresponding Author François-Xavier Maquart Laboratoire de Biochimie-CNRS EP 89, Faculté de Médecine, 51095 Reims, FranceLaboratoire de Biochimie, Faculté de Médecine, 51, rue Cognacq-Jay, 51095 Reims Cedex, FranceSearch for more papers by this author First published: July 1996 https://doi.org/10.1002/(SICI)1097-4652(199607)168:1 3.0.CO;2-2Citations: 20AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Remodeling of the extracellular matrix by fibroblasts is an important step in the process of wound healing and tissue repair. We compared the behavior of fibroblasts from two different tissues, dermis and gingiva, in three-dimensional lattices made of two different extracellular matrix macromolecules, collagen and fibrin. Cells were grown in monolayer cultures from normal skin or gingiva and seeded in three-dimensional lattices made of either collagen or fibrin. Photonic and scanning electron microscopy did not reveal any morphological differences between the two types of fibroblasts in both sets of lattices. Both types of fibroblasts retracted collagen lattices similarly and caused only a slight degradation of the collagen substratum. By contrast, when seeded in fibrin lattices, gingival fibroblasts completely digested their substratum in less than 8 days, whereas only a slight fibrin degradation was observed with dermal fibroblasts. The ability of gingival but not dermal fibroblasts to express high levels of tissue plasminogen activators (tPA) when cultured in fibrin lattices was assessed on an immunological basis. Also, deprivation of plasminogen-contaminating fibrinogen preparations or use of tPA inhibitors markedly inhibited both fibrinolysis and retraction rates of fibrin lattices by gingival fibroblasts. Casein-zymography confirmed the intense proteolytic activity induced by fibrin in gingival fibroblasts. It was inhibited by aprotinin and phenyl methylsulfonyl fluoride (PMSF), two non-specific inhibitors of serine proteinases, and by η-amino-caproic acid (ηACA), an inhibitor of plasminogen activators. Monolayer cultures exhibited only trace amounts of caseinolytic activity. 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