title: Cumulative influence of elastin peptides and plasminogen on matrix metalloproteinase activation and type I collagen invasion by HT-1080 fibrosarcoma cells.
abstract: HT-1080 fibrosarcoma cells express at their plasma membrane the elastin-binding protein (EBP). Occupancy of EBP by elastin fragments, tropoelastin or XGVAPG peptides was found to trigger procollagenase-1 (proMMP-1) overproduction by HT-1080 cells at the protein and enzyme levels. RT-PCR analysis indicated that elastin peptides did not modify the MMP-1 mRNA steady state levels, suggesting the involvement of a post-transcriptional mechanism. We previously reported that binding of elastin peptides to EBP induced other matrix metalloproteinases (MMP-2 and MT1-MMP) expression. Since those peptides were here found to also accelerate the secretion of urokinase from HT-1080 cells, culture medium was supplemented with plasminogen together with elastin peptides at aims to induce or potentiate MMPs activation cascades. In such conditions, plasmin activity was generated and exacerbate proMMP-1 and proMMP-2 activation. As a consequence, elastin peptides and plasminogen-treated HT-1080 cells displayed a significant type I collagen matrix invasive capacity.
authors.affiliation: FRE 2260 CNRS, Université de Reims (URCA), France.
authors.forename: Eric
authors.initials: E
authors.lastname: Huet
authors.forename: Bertrand
authors.initials: B
authors.lastname: Brassart
authors.forename: Jean-Hubert
authors.initials: JH
authors.lastname: Cauchard
authors.forename: Laurent
authors.initials: L
authors.lastname: Debelle
authors.forename: Philippe
authors.initials: P
authors.lastname: Birembaut
authors.forename: Jean
authors.initials: J
authors.lastname: Wallach
authors.forename: Herve
authors.initials: H
authors.lastname: Emonard
authors.forename: Myriam
authors.initials: M
authors.lastname: Polette
authors.forename: William
authors.initials: W
authors.lastname: Hornebeck
mesh_terms: D024042:Collagen Type I / Q000378:metabolism*; D017364:Collagenases / Q000378:metabolism*; D017931:DNA Primers / Q000737:chemistry; D004549:Elastin / Q000494:pharmacology*; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D005341:Fibrinolysin / Q000378:metabolism; D005354:Fibrosarcoma / Q000201:enzymology*; D005780:Gelatin / Q000378:metabolism; D018093:Gelatinases / Q000378:metabolism*; D006801:Humans; D020781:Matrix Metalloproteinase 1; D020778:Matrix Metalloproteinase 2 / Q000378:metabolism; D008666:Metalloendopeptidases / Q000378:metabolism*; D009361:Neoplasm Invasiveness; D010446:Peptide Fragments / Q000494:pharmacology*; D010958:Plasminogen / Q000494:pharmacology*; D011956:Receptors, Cell Surface / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D019716:Tissue Inhibitor of Metalloproteinase-2 / Q000378:metabolism; D014407:Tumor Cells, Cultured / Q000187:drug effects; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism
chemical_list: D024042:Collagen Type I; D017931:DNA Primers; D004792:Enzyme Precursors; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; C054901:elastin-binding proteins; D019716:Tissue Inhibitor of Metalloproteinase-2; D005780:Gelatin; D010958:Plasminogen; D004549:Elastin; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator; D017364:Collagenases; D018093:Gelatinases; D008666:Metalloendopeptidases; C069860:progelatinase; D020778:Matrix Metalloproteinase 2; D020781:Matrix Metalloproteinase 1