title: Collagen type I, III and V differently modulate synthesis and activation of matrix metalloproteinases by cultured rabbit periosteal fibroblasts.
abstract: In the present study we investigated whether the collagen types I, III and V affect the activity of fibroblasts obtained from rabbit periosteum. The cells were cultured on plates either or not coated with different amounts of collagen type I, III or V and analyzed for their attachment, DNA synthesis and the expression and activity of matrix metalloproteinases (MMPs). Our data show that the three collagen types promoted attachment and spreading of the cells and stimulated DNA synthesis when used in relatively low concentrations. High concentrations of type V-but not of type I or III-proved to inhibit thymidine incorporation. The expression and activity of matrix metalloproteinase 1 (MMP-1; interstitial collagenase) decreased under the influence of relatively low amounts of collagen (<40 microg/well), whereas higher levels increased its release. Matrix metalloproteinase 2 (MMP-2; gelatinase A) was up-regulated by the different types of collagen; the active fraction of stromelysin-1 (MMP-3) decreased. Accordingly, the mRNA expression of MMP-1 and -3 were reduced. The expression of MMP-2 mRNA, however, proved to be unaffected. Blocking antibodies to beta(1)-integrin or echistatin increased the level of MMP-1 but had no effect on MMP-2. All parameters tested were similarly affected by type I and III collagen, whereas the effect of type V was always less. We conclude that the collagen types I, III and V provide different sets of signals for fibroblasts that differently modulate their proliferation and MMP expression.
authors.affiliation: Department of Periodontology, Academic Center for Dentistry Amsterdam (ACTA), University of Amsterdam, Louwesweg 1, 1066 EA, Amsterdam, The Netherlands.
authors.forename: Erica H M
authors.initials: EH
authors.lastname: Kerkvliet
authors.forename: Ineke C
authors.initials: IC
authors.lastname: Jansen
authors.forename: Ton
authors.initials: T
authors.lastname: Schoenmaker
authors.forename: Wouter
authors.initials: W
authors.lastname: Beertsen
authors.forename: Vincent
authors.initials: V
authors.lastname: Everts
mesh_terms: D000818:Animals; D001483:Base Sequence; D002448:Cell Adhesion / Q000187:drug effects; D002455:Cell Division / Q000187:drug effects; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism / Q000494:pharmacology*; D024042:Collagen Type I / Q000378:metabolism / Q000494:pharmacology; D024043:Collagen Type II / Q000378:metabolism / Q000494:pharmacology; D024062:Collagen Type V / Q000378:metabolism / Q000494:pharmacology; D004247:DNA / Q000096:biosynthesis; D018076:DNA, Complementary / Q000235:genetics; D004789:Enzyme Activation / Q000187:drug effects; D005347:Fibroblasts / Q000187:drug effects / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic / Q000187:drug effects; D020781:Matrix Metalloproteinase 1 / Q000235:genetics / Q000378:metabolism; D020778:Matrix Metalloproteinase 2 / Q000235:genetics / Q000378:metabolism; D019278:Matrix Metalloproteinase 3 / Q000235:genetics / Q000378:metabolism; D020782:Matrix Metalloproteinases / Q000235:genetics / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D011817:Rabbits
chemical_list: D024042:Collagen Type I; D024043:Collagen Type II; D024062:Collagen Type V; D018076:DNA, Complementary; D012333:RNA, Messenger; D003094:Collagen; D004247:DNA; D020782:Matrix Metalloproteinases; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2; D020781:Matrix Metalloproteinase 1