Detection of rat Pneumocystis carinii proteinases and elastase and antipneumocystis activity of proteinase inhibitors in vitro
Identifieur interne : 002678 ( Main/Exploration ); précédent : 002677; suivant : 002679Detection of rat Pneumocystis carinii proteinases and elastase and antipneumocystis activity of proteinase inhibitors in vitro
Auteurs : C. Atzori [Italie] ; A. Mainini [Italie] ; F. Agostoni [Italie] ; E. Angeli [Italie] ; M. Bartlett [États-Unis] ; A. Bruno [Italie] ; M. Scaglia [Italie] ; A. Cargnel [Italie]Source :
- Parasite [ 1252-607X ] ; 2014-09-15.
Abstract
Proteinases play an important role in survival of microorganisms and in pathogenicity of diseases. By using a modified SDS-gelatin-polyacrylamide gel system, proteinases of rat-P. carinii were detected as bands of proteolytic digestion after electrophoresis. P.carinii organisms obtained from dexamethazone immuno-suppressed transtracheally infected rats were cultured in spinner flask suspension cultures to minimize host cell contamination. At pH 8.3, seven Pc-specific proteolytic bands were detected in three clusters of different molecular weights clearly different from host cell patterns. By using a range of pH, various preparations of organisms and both infected and uninfected culture media, proteolytic activities have been partially characterized. Elastase secretion has been assessed based on elastin digestion model. Proteinase inhibitors have been tested for their ability to inhibit P.carinii growth in HEL299 short-term monolayer cultures. Results indicate that proteolytic activities are involved in the proliferation of microorganisms since leupeptin exerted in vitro antipneumocystis activity while aprotinin enhanced P.carinii growth.
Les protéases jouent un rôle important pour la survie des microorganismes et pour la pathogénie des maladies. Par un système de gel en SDS-gélatine-polyacrylamide modifié, on a mis en évidence des bandes de digestion protéolytique qui sont dues à des protéases de P. carinii. Les organismes de P. carinii, obtenus à partir de rats immunodéprimés par la dexaméthasone et infectés par voie trans-trachéale, ont été cultivés en suspension dans des flacons "spinner flasks" pour réduir au maximum (< 1 %) la contamination par les cellules-hôtes. A pH 8,3, on a compté sept bandes protéolytiques spécifiques de P. carinii qui peuvent être rassemblées en trois groupes de poids moléculaires clairement différents de ceux des cellules-hôtes. De plus, en employant des pH variés, on a partiellement caractérisé les activités protéolytiques de différentes préparations d'organismes et de milieux de culture aussi bien infectés que non infectés, la sécrétion d'élastase a été démontrée avec un modèle de digestion de l'élastine. Des inhibiteurs des protéases ont été expérimentés pour leur aptitude à inhiber le développement de P. carinii dans une monocouche de cellules HEL299 en cultures à court terme. Les résultats démontrent que les activités protéolytiques sont impliquées dans la prolifération des micro-organismes, puisque la leupeptine exerçait une activité antipneumocystis in vitro, alors que l'aprotinine stimulait le développement de P.carinii.
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DOI: 10.1051/parasite/1999061009
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By using a modified SDS-gelatin-polyacrylamide gel system, proteinases of rat-P. carinii were detected as bands of proteolytic digestion after electrophoresis. P.carinii organisms obtained from dexamethazone immuno-suppressed transtracheally infected rats were cultured in spinner flask suspension cultures to minimize host cell contamination. At pH 8.3, seven Pc-specific proteolytic bands were detected in three clusters of different molecular weights clearly different from host cell patterns. By using a range of pH, various preparations of organisms and both infected and uninfected culture media, proteolytic activities have been partially characterized. Elastase secretion has been assessed based on elastin digestion model. Proteinase inhibitors have been tested for their ability to inhibit P.carinii growth in HEL299 short-term monolayer cultures. Results indicate that proteolytic activities are involved in the proliferation of microorganisms since leupeptin exerted in vitro antipneumocystis activity while aprotinin enhanced P.carinii growth.</div><div type="abstract" xml:lang="fr">Les protéases jouent un rôle important pour la survie des microorganismes et pour la pathogénie des maladies. Par un système de gel en SDS-gélatine-polyacrylamide modifié, on a mis en évidence des bandes de digestion protéolytique qui sont dues à des protéases de P. carinii. Les organismes de P. carinii, obtenus à partir de rats immunodéprimés par la dexaméthasone et infectés par voie trans-trachéale, ont été cultivés en suspension dans des flacons "spinner flasks" pour réduir au maximum (< 1 %) la contamination par les cellules-hôtes. A pH 8,3, on a compté sept bandes protéolytiques spécifiques de P. carinii qui peuvent être rassemblées en trois groupes de poids moléculaires clairement différents de ceux des cellules-hôtes. De plus, en employant des pH variés, on a partiellement caractérisé les activités protéolytiques de différentes préparations d'organismes et de milieux de culture aussi bien infectés que non infectés, la sécrétion d'élastase a été démontrée avec un modèle de digestion de l'élastine. Des inhibiteurs des protéases ont été expérimentés pour leur aptitude à inhiber le développement de P. carinii dans une monocouche de cellules HEL299 en cultures à court terme. Les résultats démontrent que les activités protéolytiques sont impliquées dans la prolifération des micro-organismes, puisque la leupeptine exerçait une activité antipneumocystis in vitro, alors que l'aprotinine stimulait le développement de P.carinii.</div></front></TEI><affiliations><list><country><li>Italie</li><li>États-Unis</li></country><region><li>Lombardie</li></region><settlement><li>Milan</li></settlement></list><tree><country name="Italie"><region name="Lombardie"><name sortKey="Atzori, C" sort="Atzori, C" uniqKey="Atzori C" first="C." last="Atzori">C. Atzori</name></region><name sortKey="Agostoni, F" sort="Agostoni, F" uniqKey="Agostoni F" first="F." last="Agostoni">F. Agostoni</name><name sortKey="Agostoni, F" sort="Agostoni, F" uniqKey="Agostoni F" first="F." last="Agostoni">F. Agostoni</name><name sortKey="Angeli, E" sort="Angeli, E" uniqKey="Angeli E" first="E." last="Angeli">E. Angeli</name><name sortKey="Atzori, C" sort="Atzori, C" uniqKey="Atzori C" first="C." last="Atzori">C. Atzori</name><name sortKey="Bruno, A" sort="Bruno, A" uniqKey="Bruno A" first="A." last="Bruno">A. Bruno</name><name sortKey="Cargnel, A" sort="Cargnel, A" uniqKey="Cargnel A" first="A." last="Cargnel">A. Cargnel</name><name sortKey="Mainini, A" sort="Mainini, A" uniqKey="Mainini A" first="A." last="Mainini">A. Mainini</name><name sortKey="Scaglia, M" sort="Scaglia, M" uniqKey="Scaglia M" first="M." last="Scaglia">M. Scaglia</name></country><country name="États-Unis"><noRegion><name sortKey="Bartlett, M" sort="Bartlett, M" uniqKey="Bartlett M" first="M." last="Bartlett">M. Bartlett</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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