Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion
- Autores
- Chiatellino, Maria Clara; Fernandez Villamil, Silvia Hebe; Vilchez Larrea, Salomé Catalina
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- Chagas´ disease stands as one of the main public health problems in Latin America. T. cruzi, protozoan parasite responsible for this disease, has a complex life cycle comprising several stages that allow it to multiply and disseminate. During the cell invasion step, the parasite modulates several metabolic pathways in the host cell; therefore, drugs that operate on these pathways could be used with therapeutic aims. Signaling though PI3k/Akt elicited in the host cell during T. cruzi infection. Activation of this pathway is important since it has anti-apoptotic effects that operate in favor of the infection and is also crucial for the regulation of the lysosome dependent and independent invasion mechanisms. Recently, it has been reported that Poly(ADP-ribose)Glycohydrolase (PARG) participates in the regulation of the PI3k/Akt route by downregulating Akt phosphorylation in cancer cells. In our infection model, PARG inhibition by DEA 1 μM or silencing by iRNA (shPARG) in Vero cells, the % of phosphorylated Akt is not altered when compared to Wild Type infected cells, but the upregulation of Akt levels on Wild Type (35% at 15 min and 80% at 6 h PI) cells could not be observed in cells where PARG activity is absent. Lysosome formation in response to parasitic infection is also altered when Vero cell PARG is inhibited or silenced: at 1 h PI, LAMP-1 (lysosome marker) signaling diminishes in DEA 1 μM-treated or shPARG cells in comparison to Wild Type cells. The reduction in lysosome density can also been observed in the absence of infection, indicating that lysosome formation regulation by PARG might be operating also in physiological conditions. Previous results obtained by our group showed that PARG inhibition led to a marked decrease in T. cruzi infection in vitro. These new findings could indicate that the downregulation of the lysosome invasion pathway could partially account for the reduction in T. cruzi infection when PARG activity is absent.
Fil: Chiatellino, Maria Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Vilchez Larrea, Salomé Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Científica y Tecnológica; Argentina
LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio
Mar del Plata
Argentina
Sociedad Argentina de Investigación Clínica
Asociación Argentina de Farmacología Experimental
Sociedad Argentina de Biología
Sociedad Argentina de Protozoología
Asociación Argentina de Nanomedicinas
Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio
The Histochemical Society - Materia
-
TRYPANOSOMA CRUZI
PARG
INVASIÓN
LYSOSOMES - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/234137
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Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasionChiatellino, Maria ClaraFernandez Villamil, Silvia HebeVilchez Larrea, Salomé CatalinaTRYPANOSOMA CRUZIPARGINVASIÓNLYSOSOMEShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Chagas´ disease stands as one of the main public health problems in Latin America. T. cruzi, protozoan parasite responsible for this disease, has a complex life cycle comprising several stages that allow it to multiply and disseminate. During the cell invasion step, the parasite modulates several metabolic pathways in the host cell; therefore, drugs that operate on these pathways could be used with therapeutic aims. Signaling though PI3k/Akt elicited in the host cell during T. cruzi infection. Activation of this pathway is important since it has anti-apoptotic effects that operate in favor of the infection and is also crucial for the regulation of the lysosome dependent and independent invasion mechanisms. Recently, it has been reported that Poly(ADP-ribose)Glycohydrolase (PARG) participates in the regulation of the PI3k/Akt route by downregulating Akt phosphorylation in cancer cells. In our infection model, PARG inhibition by DEA 1 μM or silencing by iRNA (shPARG) in Vero cells, the % of phosphorylated Akt is not altered when compared to Wild Type infected cells, but the upregulation of Akt levels on Wild Type (35% at 15 min and 80% at 6 h PI) cells could not be observed in cells where PARG activity is absent. Lysosome formation in response to parasitic infection is also altered when Vero cell PARG is inhibited or silenced: at 1 h PI, LAMP-1 (lysosome marker) signaling diminishes in DEA 1 μM-treated or shPARG cells in comparison to Wild Type cells. The reduction in lysosome density can also been observed in the absence of infection, indicating that lysosome formation regulation by PARG might be operating also in physiological conditions. Previous results obtained by our group showed that PARG inhibition led to a marked decrease in T. cruzi infection in vitro. These new findings could indicate that the downregulation of the lysosome invasion pathway could partially account for the reduction in T. cruzi infection when PARG activity is absent.Fil: Chiatellino, Maria Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Vilchez Larrea, Salomé Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Científica y Tecnológica; ArgentinaLXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de LaboratorioMar del PlataArgentinaSociedad Argentina de Investigación ClínicaAsociación Argentina de Farmacología ExperimentalSociedad Argentina de BiologíaSociedad Argentina de ProtozoologíaAsociación Argentina de NanomedicinasAsociación Argentina de Ciencia y Tecnología de Animales de LaboratorioThe Histochemical SocietyFundación Revista Medicina2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/234137Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion; LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio; Mar del Plata; Argentina; 2019; 181-1810025-76801669-9106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://medicinabuenosaires.com/revistas/vol79-19/s4/vol79_s4.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:49:17Zoai:ri.conicet.gov.ar:11336/234137instacron: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:34982025-09-29 09:49:17.451CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
title |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
spellingShingle |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion Chiatellino, Maria Clara TRYPANOSOMA CRUZI PARG INVASIÓN LYSOSOMES |
title_short |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
title_full |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
title_fullStr |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
title_full_unstemmed |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
title_sort |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion |
dc.creator.none.fl_str_mv |
Chiatellino, Maria Clara Fernandez Villamil, Silvia Hebe Vilchez Larrea, Salomé Catalina |
author |
Chiatellino, Maria Clara |
author_facet |
Chiatellino, Maria Clara Fernandez Villamil, Silvia Hebe Vilchez Larrea, Salomé Catalina |
author_role |
author |
author2 |
Fernandez Villamil, Silvia Hebe Vilchez Larrea, Salomé Catalina |
author2_role |
author author |
dc.subject.none.fl_str_mv |
TRYPANOSOMA CRUZI PARG INVASIÓN LYSOSOMES |
topic |
TRYPANOSOMA CRUZI PARG INVASIÓN LYSOSOMES |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Chagas´ disease stands as one of the main public health problems in Latin America. T. cruzi, protozoan parasite responsible for this disease, has a complex life cycle comprising several stages that allow it to multiply and disseminate. During the cell invasion step, the parasite modulates several metabolic pathways in the host cell; therefore, drugs that operate on these pathways could be used with therapeutic aims. Signaling though PI3k/Akt elicited in the host cell during T. cruzi infection. Activation of this pathway is important since it has anti-apoptotic effects that operate in favor of the infection and is also crucial for the regulation of the lysosome dependent and independent invasion mechanisms. Recently, it has been reported that Poly(ADP-ribose)Glycohydrolase (PARG) participates in the regulation of the PI3k/Akt route by downregulating Akt phosphorylation in cancer cells. In our infection model, PARG inhibition by DEA 1 μM or silencing by iRNA (shPARG) in Vero cells, the % of phosphorylated Akt is not altered when compared to Wild Type infected cells, but the upregulation of Akt levels on Wild Type (35% at 15 min and 80% at 6 h PI) cells could not be observed in cells where PARG activity is absent. Lysosome formation in response to parasitic infection is also altered when Vero cell PARG is inhibited or silenced: at 1 h PI, LAMP-1 (lysosome marker) signaling diminishes in DEA 1 μM-treated or shPARG cells in comparison to Wild Type cells. The reduction in lysosome density can also been observed in the absence of infection, indicating that lysosome formation regulation by PARG might be operating also in physiological conditions. Previous results obtained by our group showed that PARG inhibition led to a marked decrease in T. cruzi infection in vitro. These new findings could indicate that the downregulation of the lysosome invasion pathway could partially account for the reduction in T. cruzi infection when PARG activity is absent. Fil: Chiatellino, Maria Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina Fil: Vilchez Larrea, Salomé Catalina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Científica y Tecnológica; Argentina LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio Mar del Plata Argentina Sociedad Argentina de Investigación Clínica Asociación Argentina de Farmacología Experimental Sociedad Argentina de Biología Sociedad Argentina de Protozoología Asociación Argentina de Nanomedicinas Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio The Histochemical Society |
description |
Chagas´ disease stands as one of the main public health problems in Latin America. T. cruzi, protozoan parasite responsible for this disease, has a complex life cycle comprising several stages that allow it to multiply and disseminate. During the cell invasion step, the parasite modulates several metabolic pathways in the host cell; therefore, drugs that operate on these pathways could be used with therapeutic aims. Signaling though PI3k/Akt elicited in the host cell during T. cruzi infection. Activation of this pathway is important since it has anti-apoptotic effects that operate in favor of the infection and is also crucial for the regulation of the lysosome dependent and independent invasion mechanisms. Recently, it has been reported that Poly(ADP-ribose)Glycohydrolase (PARG) participates in the regulation of the PI3k/Akt route by downregulating Akt phosphorylation in cancer cells. In our infection model, PARG inhibition by DEA 1 μM or silencing by iRNA (shPARG) in Vero cells, the % of phosphorylated Akt is not altered when compared to Wild Type infected cells, but the upregulation of Akt levels on Wild Type (35% at 15 min and 80% at 6 h PI) cells could not be observed in cells where PARG activity is absent. Lysosome formation in response to parasitic infection is also altered when Vero cell PARG is inhibited or silenced: at 1 h PI, LAMP-1 (lysosome marker) signaling diminishes in DEA 1 μM-treated or shPARG cells in comparison to Wild Type cells. The reduction in lysosome density can also been observed in the absence of infection, indicating that lysosome formation regulation by PARG might be operating also in physiological conditions. Previous results obtained by our group showed that PARG inhibition led to a marked decrease in T. cruzi infection in vitro. These new findings could indicate that the downregulation of the lysosome invasion pathway could partially account for the reduction in T. cruzi infection when PARG activity is absent. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión Journal http://purl.org/coar/resource_type/c_5794 info:ar-repo/semantics/documentoDeConferencia |
status_str |
publishedVersion |
format |
conferenceObject |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/234137 Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion; LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio; Mar del Plata; Argentina; 2019; 181-181 0025-7680 1669-9106 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/234137 |
identifier_str_mv |
Poly(ADP-ribose)Glycohydrolase activity is important for lysosome formation during Trypanosoma cruzi invasion; LXIV Reunión Anual de la Sociedad Argentina de Investigación Clínica; LI Reunión Anual de la Asociación Argentina de Farmacología Experimental; XXI Reunión Anual de la Sociedad Argentina de Biología; XXXI Reunión Anual de la Sociedad Argentina de Protozoología; IX Reunión Anual de la Asociación Argentina de Nanomedicinas; VI Reunión Científica Regional de la Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio; Mar del Plata; Argentina; 2019; 181-181 0025-7680 1669-9106 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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Fundación Revista Medicina |
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Fundación Revista Medicina |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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