Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages
- Autores
- Paraje, María Gabriela; Correa, Silvia Graciela; Albesa, Inés; Sotomayor, Claudia Elena
- Año de publicación
- 2009
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Candida albicans secretes various hydrolytic enzymes which are considered to be an integral part in the pathogenesis. However, the role of lipases is far from being completely understood and the direct effects of these fungal enzymes during the host-pathogen interaction remain to be established. We recently isolated and characterized an extracellular C. albicans lipase (CaLIP), and demonstrated the ability of this fungal enzyme to interact directly with macrophages (Mvarphi) and hepatocytes and to operate as a virulence factor. Herein, we explored the effects of CaLIP on Mvarphi functions such as oxidative burst and l-arginine metabolism. The study was performed in cells with different activation status: normal-resting Mvarphis and Mvarphis primed in vivo or in vitro with C. albicans. The ability of this fungal factor to modulate the above-mentioned parameters was dependent on cells status, dose, and microenvironment, where the interaction took place. These results constitute a new finding in the biology of candidiasis and could illustrate an additional evolutive advantage for the fungus in the framework of the bidirectional host-pathogen interaction.
Fil: Paraje, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Correa, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Albesa, Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
Fil: Sotomayor, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina - Materia
-
Macrophages
Candida Albicans
Virulence Factor
Ros - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/24226
Ver los metadatos del registro completo
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Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophagesParaje, María GabrielaCorrea, Silvia GracielaAlbesa, InésSotomayor, Claudia ElenaMacrophagesCandida AlbicansVirulence FactorRoshttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Candida albicans secretes various hydrolytic enzymes which are considered to be an integral part in the pathogenesis. However, the role of lipases is far from being completely understood and the direct effects of these fungal enzymes during the host-pathogen interaction remain to be established. We recently isolated and characterized an extracellular C. albicans lipase (CaLIP), and demonstrated the ability of this fungal enzyme to interact directly with macrophages (Mvarphi) and hepatocytes and to operate as a virulence factor. Herein, we explored the effects of CaLIP on Mvarphi functions such as oxidative burst and l-arginine metabolism. The study was performed in cells with different activation status: normal-resting Mvarphis and Mvarphis primed in vivo or in vitro with C. albicans. The ability of this fungal factor to modulate the above-mentioned parameters was dependent on cells status, dose, and microenvironment, where the interaction took place. These results constitute a new finding in the biology of candidiasis and could illustrate an additional evolutive advantage for the fungus in the framework of the bidirectional host-pathogen interaction.Fil: Paraje, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Correa, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Albesa, Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaFil: Sotomayor, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; ArgentinaElsevier Inc2009-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/24226Paraje, María Gabriela; Correa, Silvia Graciela; Albesa, Inés; Sotomayor, Claudia Elena; Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages; Elsevier Inc; Biochemical and Biophysical Research Communications; 390; 2; 9-2009; 263-2680006-291XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006291X09019214info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbrc.2009.09.104info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-11-05T10:13:25Zoai:ri.conicet.gov.ar:11336/24226instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-11-05 10:13:25.954CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| title |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| spellingShingle |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages Paraje, María Gabriela Macrophages Candida Albicans Virulence Factor Ros |
| title_short |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| title_full |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| title_fullStr |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| title_full_unstemmed |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| title_sort |
Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages |
| dc.creator.none.fl_str_mv |
Paraje, María Gabriela Correa, Silvia Graciela Albesa, Inés Sotomayor, Claudia Elena |
| author |
Paraje, María Gabriela |
| author_facet |
Paraje, María Gabriela Correa, Silvia Graciela Albesa, Inés Sotomayor, Claudia Elena |
| author_role |
author |
| author2 |
Correa, Silvia Graciela Albesa, Inés Sotomayor, Claudia Elena |
| author2_role |
author author author |
| dc.subject.none.fl_str_mv |
Macrophages Candida Albicans Virulence Factor Ros |
| topic |
Macrophages Candida Albicans Virulence Factor Ros |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.3 https://purl.org/becyt/ford/3 |
| dc.description.none.fl_txt_mv |
Candida albicans secretes various hydrolytic enzymes which are considered to be an integral part in the pathogenesis. However, the role of lipases is far from being completely understood and the direct effects of these fungal enzymes during the host-pathogen interaction remain to be established. We recently isolated and characterized an extracellular C. albicans lipase (CaLIP), and demonstrated the ability of this fungal enzyme to interact directly with macrophages (Mvarphi) and hepatocytes and to operate as a virulence factor. Herein, we explored the effects of CaLIP on Mvarphi functions such as oxidative burst and l-arginine metabolism. The study was performed in cells with different activation status: normal-resting Mvarphis and Mvarphis primed in vivo or in vitro with C. albicans. The ability of this fungal factor to modulate the above-mentioned parameters was dependent on cells status, dose, and microenvironment, where the interaction took place. These results constitute a new finding in the biology of candidiasis and could illustrate an additional evolutive advantage for the fungus in the framework of the bidirectional host-pathogen interaction. Fil: Paraje, María Gabriela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina Fil: Correa, Silvia Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina Fil: Albesa, Inés. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina Fil: Sotomayor, Claudia Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina |
| description |
Candida albicans secretes various hydrolytic enzymes which are considered to be an integral part in the pathogenesis. However, the role of lipases is far from being completely understood and the direct effects of these fungal enzymes during the host-pathogen interaction remain to be established. We recently isolated and characterized an extracellular C. albicans lipase (CaLIP), and demonstrated the ability of this fungal enzyme to interact directly with macrophages (Mvarphi) and hepatocytes and to operate as a virulence factor. Herein, we explored the effects of CaLIP on Mvarphi functions such as oxidative burst and l-arginine metabolism. The study was performed in cells with different activation status: normal-resting Mvarphis and Mvarphis primed in vivo or in vitro with C. albicans. The ability of this fungal factor to modulate the above-mentioned parameters was dependent on cells status, dose, and microenvironment, where the interaction took place. These results constitute a new finding in the biology of candidiasis and could illustrate an additional evolutive advantage for the fungus in the framework of the bidirectional host-pathogen interaction. |
| publishDate |
2009 |
| dc.date.none.fl_str_mv |
2009-09 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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publishedVersion |
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http://hdl.handle.net/11336/24226 Paraje, María Gabriela; Correa, Silvia Graciela; Albesa, Inés; Sotomayor, Claudia Elena; Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages; Elsevier Inc; Biochemical and Biophysical Research Communications; 390; 2; 9-2009; 263-268 0006-291X CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/24226 |
| identifier_str_mv |
Paraje, María Gabriela; Correa, Silvia Graciela; Albesa, Inés; Sotomayor, Claudia Elena; Lipase of Candida albicans induces activation of NADPH oxidase and L-arginine pathways on resting and activated macrophages; Elsevier Inc; Biochemical and Biophysical Research Communications; 390; 2; 9-2009; 263-268 0006-291X CONICET Digital CONICET |
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eng |
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eng |
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openAccess |
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Elsevier Inc |
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Elsevier Inc |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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