Matrix metalloproteinase-11/stromelysin-3 exhibits collagenolytic function against collagen VI under normal and malignant conditions
| Autor: | Nadia Messaddeq, Elena Roza Motrescu, Marlène Rio, M. P. Chenard, Isabelle Stoll, Nicolas Etique, Sébastien Blaise, Catherine Tomasetto |
|---|---|
| Přispěvatelé: | Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-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), Maquart, François-Xavier, Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Service d'Anatomie Pathologique Générale, CHU Strasbourg-Hôpital de Hautepierre [Strasbourg], 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)-Université de Reims Champagne-Ardenne (URCA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
MESH: Extracellular Matrix Proteins
Cancer Research MESH: Osteosarcoma Extracellular matrix component Matrix metalloproteinase MESH: Silver Staining Collagen receptor MESH: Recombinant Proteins chemistry.chemical_compound Mice 0302 clinical medicine Collagen VI MESH: Matrix Metalloproteinase 11 Adipocyte MESH: Collagen Adipocytes Insulin MESH: Animals ComputingMilieux_MISCELLANEOUS Cells Cultured 0303 health sciences Extracellular Matrix Proteins Osteosarcoma MESH: Glioblastoma Cell Differentiation Recombinant Proteins Cell biology Extracellular Matrix Adipogenesis 030220 oncology & carcinogenesis Collagen MESH: Cells Cultured MESH: Cell Differentiation medicine.medical_specialty Silver Staining MESH: Cell Line Tumor MESH: Collagen Type VI Collagen Type VI MESH: Insulin Biology MESH: Extracellular Matrix 03 medical and health sciences Matrix Metalloproteinase 11 Internal medicine 3T3-L1 Cells Cell Line Tumor MESH: Hypoglycemic Agents Genetics medicine Extracellular Animals Humans Hypoglycemic Agents Molecular Biology MESH: Mice MESH: Adipocytes 030304 developmental biology MESH: Humans MESH: Embryo Mammalian Fibroblasts Embryo Mammalian [SDV.ETH] Life Sciences [q-bio]/Ethics MESH: 3T3-L1 Cells [SDV.ETH]Life Sciences [q-bio]/Ethics Collagen type I alpha 1 Endocrinology chemistry MESH: Fibroblasts Glioblastoma |
| Zdroj: | Oncogene Oncogene, 2008, 27 (49), pp.6347-6355. ⟨10.1038/onc.2008.218⟩ Oncogene, Nature Publishing Group, 2008, 27 (49), pp.6347-55. ⟨10.1038/onc.2008.218⟩ Oncogene, Nature Publishing Group, 2008, 27 (49), pp.6347-6355 HAL |
| ISSN: | 0950-9232 1476-5594 |
| Popis: | International audience; The substrate of matrix metalloproteinase 11 (MMP11) remains unknown. We have recently shown that MMP11 is a negative regulator of adipogenesis, able to reduce and even to revert mature adipocyte differentiation. Here, we have used mouse 3T3L1 cells and human U87MG and SaOS cells to show that MMP11 cleaves the native alpha3 chain of collagen VI, which is an adipocyte-related extracellular matrix component. It is known that extracellular proteolytic processing of this chain is required for correct collagen VI folding. Interestingly, MMP11-deficient fat tissue is less cohesive and exhibits collagen VI alteration, dramatic adipocyte plasma and basement membrane abnormalities and lipid leakage. MMP11 is thus required for correct collagen VI folding and therefore for fat tissue cohesion and adipocyte function. Both MMP11 and collagen VI favor tumor progression. Similar spatio-temporal overexpression at the adipocyte-cancer cell interface has been reported for the two proteins. MMP11-dependent collagen VI processing might therefore be expected to occur during malignancy. Accordingly, collagen VI no longer delineates adipocytes located at the invasive front of breast carcinomas. In conclusion, the native alpha3 chain of collagen VI constitutes a specific MMP11 substrate. This MMP11 collagenolytic activity is functional in fat tissue ontogenesis as well as during cancer invasive steps. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|