title: [Effect of elastin peptides on the production of matrix metalloproteinase 2 by human skin fibroblasts in culture].
abstract: Soluble elastin-derived peptides from alkaline or elastase hydrolysis of insoluble elastin, as well as tropoelastin, increase matrix metalloproteinase-2 (MMP-2) production by human skin fibroblasts in culture as determined by gelatin zymography and ELISA. Such an effect is time and concentration dependent; it can be reproduced by synthetic elastin: VGVAPG, PGAIPG, and laminin: LGTIPG, hexapeptides and inhibited by lactose and is therefore elastin receptor-mediated. The steady state levels of MMP-2 mRNAs are invariant following elastin-fibroblasts interaction. Inhibition of phospholipase C (D-609), ADP-ribosylation factor (brefeldin), protein kinase C (RO-318220) and phospholipase D (1-propanol) totally abolished the elastin-mediated increase of MMP-2 production. It suggested that the post-transcriptional mechanism controlling the elastin-mediated overproduction of MMP-2 involved a cascade leading to phospholipase D activation.
authors.affiliation: Signalisation Cellulaire et Matrice Extracellulaire, CNRS FRE 2260, IFR 53 Biomolécules, Facultés de Médecine et des Sciences, Université de Reims Champagne-Ardenne, Reims, France.
authors.forename: E
authors.initials: E
authors.lastname: Huet
authors.forename: B
authors.initials: B
authors.lastname: Brassart
authors.forename: J
authors.initials: J
authors.lastname: Wallach
authors.forename: L
authors.initials: L
authors.lastname: Debelle
authors.forename: B
authors.initials: B
authors.lastname: Haye
authors.forename: H
authors.initials: H
authors.lastname: Emonard
authors.forename: W
authors.initials: W
authors.lastname: Hornebeck
mesh_terms: D020727:ADP-Ribosylation Factors / Q000037:antagonists & inhibitors; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology; D001952:Bridged-Ring Compounds / Q000494:pharmacology; D002417:Cattle; D003609:Dactinomycin / Q000494:pharmacology; D004549:Elastin / Q000737:chemistry / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000187:drug effects; D004790:Enzyme Induction / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004797:Enzyme-Linked Immunosorbent Assay; D005347:Fibroblasts / Q000187:drug effects* / Q000201:enzymology; D006801:Humans; D007211:Indoles / Q000494:pharmacology; D007785:Lactose / Q000494:pharmacology; D007797:Laminin / Q000494:pharmacology; D020778:Matrix Metalloproteinase 2 / Q000096:biosynthesis* / Q000235:genetics; D019278:Matrix Metalloproteinase 3 / Q000096:biosynthesis / Q000235:genetics; D009636:Norbornanes; D019384:Nucleic Acid Synthesis Inhibitors / Q000494:pharmacology; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology*; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010739:Phospholipase D / Q000378:metabolism; D011493:Protein Kinase C / Q000037:antagonists & inhibitors; D011499:Protein Processing, Post-Translational / Q000187:drug effects; D015398:Signal Transduction; D012867:Skin / Q000166:cytology; D013859:Thiocarbamates; D013871:Thiones / Q000494:pharmacology; D014333:Tropoelastin / Q000737:chemistry / Q000494:pharmacology; D010738:Type C Phospholipases / Q000037:antagonists & inhibitors
chemical_list: D001952:Bridged-Ring Compounds; D004791:Enzyme Inhibitors; D007211:Indoles; D007797:Laminin; D009636:Norbornanes; D019384:Nucleic Acid Synthesis Inhibitors; D010446:Peptide Fragments; D013859:Thiocarbamates; D013871:Thiones; D014333:Tropoelastin; D003609:Dactinomycin; D020126:Brefeldin A; C046498:tricyclodecane-9-yl-xanthogenate; D004549:Elastin; D011493:Protein Kinase C; D010738:Type C Phospholipases; D010739:Phospholipase D; D019278:Matrix Metalloproteinase 3; D020778:Matrix Metalloproteinase 2; D020727:ADP-Ribosylation Factors; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D007785:Lactose; C064758:Ro 31-8220