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Gelatinase A Activation Is Regulated by the Organization of the Polymerized Actin Cytoskeleton

The Journal of biological chemistry, 1997-03, Vol.272 (11), p.7482-7487 [Peer Reviewed Journal]

1997 © 1997 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.272.11.7482 ;PMID: 9054450

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  • Title:
    Gelatinase A Activation Is Regulated by the Organization of the Polymerized Actin Cytoskeleton
  • Author: Tomasek, James J. ; Halliday, Nancy L. ; Updike, Dawn L. ; Ahern-Moore, Joan S. ; Vu, Thien-Khai H. ; Liu, Rose W. ; Howard, Eric W.
  • Subjects: Actins - metabolism ; Actins - ultrastructure ; Cells, Cultured ; Cytoskeleton - metabolism ; Cytoskeleton - ultrastructure ; Enzyme Activation ; Fibroblasts - metabolism ; Fibroblasts - ultrastructure ; Gelatinases - metabolism ; Humans ; Matrix Metalloproteinase 2 ; Metalloendopeptidases - metabolism
  • Is Part Of: The Journal of biological chemistry, 1997-03, Vol.272 (11), p.7482-7487
  • Description: Gelatinase A (GL-A) is a matrix metalloproteinase (MMP) involved in both connective tissue remodeling and tumor invasion. GL-A activation is mediated by a membrane-type MMP (MT-MMP) that cleaves the GL-A propeptide. In this study, we examined the role of the actin cytoskeleton in regulating GL-A activation and MT-MMP-1 expression. Human palmar fascia fibroblasts and human fetal lung fibroblasts were cultured on a planar substratum or within different types of collagen lattices. Fibroblasts that formed stress fibers, either on a planar substratum or within an attached collagen lattice, showed reduced GL-A activation compared with fibroblasts lacking stress fibers, within either floating or stress-released collagen lattices. To determine whether changes in the organization of the actin cytoskeleton could promote GL-A activation, fibroblasts with stress fibers were treated with cytochalasin D. Within 24 h after treatment, GL-A activation was dramatically increased. Associated with this GL-A activation was an increase in MT-MMP-1 mRNA as determined by Northern blot analysis. Treatment with nocodazole, which induced microtubule depolymerization and cell shape changes without affecting stress fibers, did not promote GL-A activation. These results suggest that the extracellular matrix and the actin cytoskeleton transduce signals that modulate GL-A activation and regulate tissue remodeling.
  • Publisher: United States: Elsevier Inc
  • Language: English
  • Identifier: ISSN: 0021-9258
    EISSN: 1083-351X
    DOI: 10.1074/jbc.272.11.7482
    PMID: 9054450
  • Source: MEDLINE
    Alma/SFX Local Collection
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