Mycobacterium tuberculosis Up-Regulates Matrix Metalloproteinase-1 Secretion from Human Airway Epithelial Cells via a p38 MAPK Switch

Pulmonary cavitation is vital to the persistence and spread of Mycobacterium tuberculosis (MTb), but mechanisms underlying this lung destruction are poorly understood. Fibrillar type I collagen provides the lung's tensile strength, and only matrix metalloproteinases (MMPs) can degrade it at neu...

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Veröffentlicht in:	Journal of Immunology 2005-10, Vol.175 (8), p.5333-5340
Hauptverfasser:	Elkington, Paul T. G, Emerson, Jenny E, Lopez-Pascua, Laura D. C, O'Kane, Cecilia M, Horncastle, Donna E, Boyle, Joseph J, Friedland, Jon S
Format:	Artikel
Sprache:	eng
Schlagworte:	Bronchi - enzymology Bronchi - metabolism Bronchi - microbiology Cells, Cultured Culture Media, Conditioned Epithelial Cells - enzymology Epithelial Cells - metabolism Epithelial Cells - microbiology Humans Ligands MAP Kinase Signaling System - physiology Matrix Metalloproteinase 1 - metabolism Monocytes - physiology Mycobacterium tuberculosis Mycobacterium tuberculosis - physiology p38 Mitogen-Activated Protein Kinases - physiology Phosphorylation Receptors, G-Protein-Coupled - physiology Respiratory Mucosa - enzymology Respiratory Mucosa - metabolism Respiratory Mucosa - microbiology Tissue Inhibitor of Metalloproteinase-1 - metabolism Tuberculosis, Pulmonary - enzymology Tumor Necrosis Factor-alpha - physiology Up-Regulation - physiology
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