Cumulative influence of elastin peptides and plasminogen on matrix metalloproteinase activation and type I collagen invasion by HT-1080 fibrosarcoma cells

Autor: Eric HUET, Bertrand Brassart, Jean-Hubert Cauchard, Laurent Debelle, Birembaut, Philippe L., Jean Wallach, Herve Emonard, Polette, Myriam C., William Hornebeck
Přispěvatelé: Université de Reims Champagne-Ardenne (URCA), Dynamique cellulaire et moléculaire de la muqueuse respiratoire, Université de Reims Champagne-Ardenne (URCA)-IFR53-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de Biochimie Analytique et Synthèse Bioorganique (LBASB), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Croissance cellulaire, réparation et régénération tissulaires (CRRET), Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Matrice extracellulaire et dynamique cellulaire - UMR 7369 (MEDyC), Université de Reims Champagne-Ardenne (URCA)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre National de la Recherche Scientifique (CNRS), Plasticité de l'épithélium respiratoire dans les conditions normales et pathologiques - UMR-S 903 (PERPMP), SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Centre Hospitalier Universitaire de Reims (CHU Reims)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Reims Champagne-Ardenne (URCA), Laboratory of Biochemistry and Molecular Biology (LBMB), Faculty of Medicine-UPRESA 6021, Laboratoire de Biochimie et Biologie Moléculaire (LBBM), Faculté de Médecine-IFR 53 Biomolécules-UPRESA 6021, Université de Reims Champagne-Ardenne (URCA)-Centre Hospitalier Universitaire de Reims (CHU Reims)-Institut National de la Santé et de la Recherche Médicale (INSERM)-SFR CAP Santé (Champagne-Ardenne Picardie Santé), Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV)-Université de Reims Champagne-Ardenne (URCA)-Université de Picardie Jules Verne (UPJV), Birembaut, Philippe
Jazyk: angličtina
Rok vydání: 2002
Předmět:
MESH: DNA Primers
MESH: Enzyme Activation
Fibrosarcoma
[SDV]Life Sciences [q-bio]
MESH: Collagenases
MESH: Elastin
MESH: Collagen Type I
MESH: Metalloendopeptidases
Enzyme-Linked Immunosorbent Assay
Receptors
Cell Surface
[SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract
Collagen Type I
MESH: Enzyme Precursors
MESH: Neopla
Tumor Cells
Cultured
Humans
Neoplasm Invasiveness
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH: Gelatinases
Collagenases
Fibrinolysin
ComputingMilieux_MISCELLANEOUS
DNA Primers
Enzyme Precursors
Tissue Inhibitor of Metalloproteinase-2
MESH: Humans
integumentary system
MESH: Fibrosarcoma
Reverse Transcriptase Polymerase Chain Reaction
Metalloendopeptidases
MESH: Enzyme-Linked Immunosorbent Assay
Plasminogen
Urokinase-Type Plasminogen Activator
Peptide Fragments
Elastin
Enzyme Activation
MESH: Matrix Metalloproteinase 2
MESH: Matrix Metalloproteinase 1
Gelatinases
[SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract
Gelatin
Matrix Metalloproteinase 2
Matrix Metalloproteinase 1
MESH: Gelatin
Zdroj: Clinical and Experimental Metastasis
Clinical and Experimental Metastasis, Springer Verlag, 2002, 19 (2), pp.107-17
Clinical and Experimental Metastasis, Springer Verlag, 2002, 19 (2), pp.107-117. ⟨10.1023/A:1014547324918⟩
HAL
ISSN: 0262-0898
1573-7276
DOI: 10.1023/A:1014547324918⟩
Popis: 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.
Databáze: OpenAIRE
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