ACandida albicansmetallopeptidase degrades constitutive proteins of extracellular matrix
| Autor: | Marie-Hélène Rodier, J. L. Jacquemin, Catherine Kauffmann-Lacroix, Brahim El Moudni, Gyslaine Daniault |
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| Rok vydání: | 1999 |
| Předmět: |
Extracellular Matrix Proteins
biology Metallopeptidase Matrix metallopeptidase 12 Proteolytic enzymes Metalloendopeptidases biology.organism_classification Microbiology Fibronectins Fibronectin Extracellular matrix Type IV collagen Biochemistry Cell Wall Laminin Candida albicans Genetics biology.protein Collagen Molecular Biology |
| Zdroj: | FEMS Microbiology Letters. 177:205-210 |
| ISSN: | 1574-6968 0378-1097 |
| Popis: | Among potential virulence factors of Candida albicans, enzymes seem to play an important role. Many studies concern the secreted aspartic proteinases (saps), and the degradation of some components of the subendothelial extracellular matrix by the isoenzyme sap2 has been proved. Nevertheless, other proteolytic enzymes could be involved in the pathogenicity of the yeast. We studied the degradation of four constitutive proteins of the extracellular matrix: type I and IV collagens, laminin and fibronectin, by a 95-kDa metallopeptidase, localised in the cell wall of C. albicans. Each of these constituents was incubated with the purified enzyme and its degradation products analysed by an electrophoretic method. We observed that type I collagen and fibronectin were totally degraded by the enzyme whereas type IV collagen and laminin were only partially degraded. The C. albicans metallopeptidase may play a role in the degradation of the subendothelial extracellular matrix components. This enzyme could facilitate the migration of the yeast in the tissues after crossing the endothelial layer, allowing the fungal invasion of target organs. |
| Databáze: | OpenAIRE |
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