Contribution of the plasmin/matrix metalloproteinase cascade to the retraction of human fibroblast populated collagen lattices.
To assess the contribution of the plasmin/matrix metalloproteinase cascade in lattices retraction, human gingival fibroblast-populated collagen lattices were supplemented with plasminogen. The rate of lattice retraction was enhanced by addition of plasminogen. This effect was concomitant to plasmin generation, prostromelysin-1 and procollagenase activation. Plasminogen-mediated initiation of that proteolytic cascade was accompanied by conspicuous changes in cell morphology and collagen fibers organization. At day 1 of culture fibroblasts shifted from a rounded (control) to an elongated (in presence of plgn) shape. At the latest stage of retraction, intense vacuolization around fibroblasts was noticed in plgn-supplemented lattices which paralleled the increased collagen degradation. Plgn-enhancing influence on the initial phase of lattice retraction could be totally annihilated by either aprotinin or Batimastat. Those data emphasize the crucial importance of the plasmin-MMP proteolytic cascade in granulation tissue retraction in a healing wound.
Berton
A
A
Laboratory of Biochemistry and Molecular Biology, CNRS UPRESA 6021, Faculty of Medicine, University of Reims Champagne-Ardennes, Reims, France.
Lorimier
S
S
Emonard
H
H
Laurent-Maquin
D
D
Hornebeck
W
W
Bellon
G
G
D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism*; D004789:Enzyme Activation; D005341:Fibrinolysin / Q000378:metabolism*; D005347:Fibroblasts / Q000201:enzymology / Q000378:metabolism / Q000648:ultrastructure; D005881:Gingiva / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism*; D008855:Microscopy, Electron, Scanning
D003094:Collagen; D005341:Fibrinolysin; D020782:Matrix Metalloproteinases