The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine
ABSTRACT: HSP90 is an abundant protein in Leishmania parasites that plays a major role in the parasite survival under stress conditions. Here we found that the HSP90 inhibitor 17- AAG (≥100 nM 17-AAG) induced cell cycle arrest at G0/G1 in L. infantum and L. panamensis promastigotes, and highly poten...
- Autores:
-
Varela Miranda, Rubén Eduardo
Mollinedo Gajate, Cristina
Muro, Antonio
Mollinedo, Faustino
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2014
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/33047
- Acceso en línea:
- https://hdl.handle.net/10495/33047
- Palabra clave:
- Proteínas HSP90 de Choque Térmico
HSP90 Heat-Shock Proteins
Puntos de Control del Ciclo Celular
Cell Cycle Checkpoints
Leishmania
Leishmania infantum
Apoptosis
Benzoquinonas
Benzoquinones
Relación Dosis-Respuesta a Droga
Dose-Response Relationship, Drug
Quimioterapia Combinada
Drug Therapy, Combination
Éteres Fosfolípidos
Phospholipid Ethers
Proteínas Protozoarias
Protozoan Proteins
Fase de Descanso del Ciclo Celular
Resting Phase, Cell Cycle
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by-nc-nd/2.5/co/
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The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| title |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| spellingShingle |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine Proteínas HSP90 de Choque Térmico HSP90 Heat-Shock Proteins Puntos de Control del Ciclo Celular Cell Cycle Checkpoints Leishmania Leishmania infantum Apoptosis Benzoquinonas Benzoquinones Relación Dosis-Respuesta a Droga Dose-Response Relationship, Drug Quimioterapia Combinada Drug Therapy, Combination Éteres Fosfolípidos Phospholipid Ethers Proteínas Protozoarias Protozoan Proteins Fase de Descanso del Ciclo Celular Resting Phase, Cell Cycle |
| title_short |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| title_full |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| title_fullStr |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| title_full_unstemmed |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| title_sort |
The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine |
| dc.creator.fl_str_mv |
Varela Miranda, Rubén Eduardo Mollinedo Gajate, Cristina Muro, Antonio Mollinedo, Faustino |
| dc.contributor.author.none.fl_str_mv |
Varela Miranda, Rubén Eduardo Mollinedo Gajate, Cristina Muro, Antonio Mollinedo, Faustino |
| dc.contributor.researchgroup.spa.fl_str_mv |
Programa de Estudio y Control de Enfermedades Tropicales (PECET) |
| dc.subject.decs.none.fl_str_mv |
Proteínas HSP90 de Choque Térmico HSP90 Heat-Shock Proteins Puntos de Control del Ciclo Celular Cell Cycle Checkpoints Leishmania Leishmania infantum Apoptosis Benzoquinonas Benzoquinones Relación Dosis-Respuesta a Droga Dose-Response Relationship, Drug Quimioterapia Combinada Drug Therapy, Combination Éteres Fosfolípidos Phospholipid Ethers Proteínas Protozoarias Protozoan Proteins Fase de Descanso del Ciclo Celular Resting Phase, Cell Cycle |
| topic |
Proteínas HSP90 de Choque Térmico HSP90 Heat-Shock Proteins Puntos de Control del Ciclo Celular Cell Cycle Checkpoints Leishmania Leishmania infantum Apoptosis Benzoquinonas Benzoquinones Relación Dosis-Respuesta a Droga Dose-Response Relationship, Drug Quimioterapia Combinada Drug Therapy, Combination Éteres Fosfolípidos Phospholipid Ethers Proteínas Protozoarias Protozoan Proteins Fase de Descanso del Ciclo Celular Resting Phase, Cell Cycle |
| description |
ABSTRACT: HSP90 is an abundant protein in Leishmania parasites that plays a major role in the parasite survival under stress conditions. Here we found that the HSP90 inhibitor 17- AAG (≥100 nM 17-AAG) induced cell cycle arrest at G0/G1 in L. infantum and L. panamensis promastigotes, and highly potentiated the induction of cell death by an apoptotic-like process mediated by the ether phospholipid edelfosine (5-20 μM). These data suggest that the combined treatment of 17-AAG and edelfosine might be a novel and effective approach of combination therapy in the treatment of leishmaniasis. |
| publishDate |
2014 |
| dc.date.issued.none.fl_str_mv |
2014 |
| dc.date.accessioned.none.fl_str_mv |
2022-12-27T12:42:46Z |
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2022-12-27T12:42:46Z |
| dc.type.spa.fl_str_mv |
Artículo de investigación |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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https://purl.org/redcol/resource_type/ART |
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http://purl.org/coar/resource_type/c_2df8fbb1 |
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acceptedVersion |
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Varela-M RE, Mollinedo-Gajate C, Muro A, Mollinedo F. The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine. Acta Trop. 2014 Mar;131:32-6. doi: 10.1016/j.actatropica.2013.11.018. |
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0001-706X |
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https://hdl.handle.net/10495/33047 |
| dc.identifier.doi.none.fl_str_mv |
10.1016/j.actatropica.2013.11.018 |
| dc.identifier.eissn.none.fl_str_mv |
1873-6254 |
| identifier_str_mv |
Varela-M RE, Mollinedo-Gajate C, Muro A, Mollinedo F. The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine. Acta Trop. 2014 Mar;131:32-6. doi: 10.1016/j.actatropica.2013.11.018. 0001-706X 10.1016/j.actatropica.2013.11.018 1873-6254 |
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https://hdl.handle.net/10495/33047 |
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eng |
| language |
eng |
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Acta. Trop. |
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21 |
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1 |
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131 |
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Acta Tropica |
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http://creativecommons.org/licenses/by-nc-nd/2.5/co/ |
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Elsevier |
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Ámsterdam, Países Bajos |
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Universidad de Antioquia |
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Varela Miranda, Rubén EduardoMollinedo Gajate, CristinaMuro, AntonioMollinedo, FaustinoPrograma de Estudio y Control de Enfermedades Tropicales (PECET)2022-12-27T12:42:46Z2022-12-27T12:42:46Z2014Varela-M RE, Mollinedo-Gajate C, Muro A, Mollinedo F. The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosine. Acta Trop. 2014 Mar;131:32-6. doi: 10.1016/j.actatropica.2013.11.018.0001-706Xhttps://hdl.handle.net/10495/3304710.1016/j.actatropica.2013.11.0181873-6254ABSTRACT: HSP90 is an abundant protein in Leishmania parasites that plays a major role in the parasite survival under stress conditions. Here we found that the HSP90 inhibitor 17- AAG (≥100 nM 17-AAG) induced cell cycle arrest at G0/G1 in L. infantum and L. panamensis promastigotes, and highly potentiated the induction of cell death by an apoptotic-like process mediated by the ether phospholipid edelfosine (5-20 μM). These data suggest that the combined treatment of 17-AAG and edelfosine might be a novel and effective approach of combination therapy in the treatment of leishmaniasis.COL001509921application/pdfengElsevierÁmsterdam, Países Bajoshttp://creativecommons.org/licenses/by-nc-nd/2.5/co/https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2The HSP90 inhibitor 17-AAG potentiates the antileishmanial activity of the ether lipid edelfosineArtículo de investigaciónhttp://purl.org/coar/resource_type/c_2df8fbb1https://purl.org/redcol/resource_type/ARTinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionProteínas HSP90 de Choque TérmicoHSP90 Heat-Shock ProteinsPuntos de Control del Ciclo CelularCell Cycle CheckpointsLeishmaniaLeishmania infantumApoptosisBenzoquinonasBenzoquinonesRelación Dosis-Respuesta a DrogaDose-Response Relationship, DrugQuimioterapia CombinadaDrug Therapy, CombinationÉteres FosfolípidosPhospholipid EthersProteínas ProtozoariasProtozoan ProteinsFase de Descanso del Ciclo CelularResting Phase, Cell CycleActa. Trop.211131Acta TropicaPublicationCC-LICENSElicense_rdflicense_rdfapplication/rdf+xml; charset=utf-8823https://bibliotecadigital.udea.edu.co/bitstreams/02240d3d-a339-44ca-b9c1-b257b37993cb/downloadb88b088d9957e670ce3b3fbe2eedbc13MD52falseAnonymousREADLICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://bibliotecadigital.udea.edu.co/bitstreams/be343d7f-32ae-495a-bd44-49e2ab2511db/download8a4605be74aa9ea9d79846c1fba20a33MD53falseAnonymousREADORIGINALVarelaRuben_2014_HSP90Inhibitor17-AAG.pdfVarelaRuben_2014_HSP90Inhibitor17-AAG.pdfArtículo de investigaciónapplication/pdf428060https://bibliotecadigital.udea.edu.co/bitstreams/6c58d94f-e41c-4354-804e-a37f08b2514b/download801452e1624f57041e0da35ae78112efMD51trueAnonymousREADTEXTVarelaRuben_2014_HSP90Inhibitor17-AAG.pdf.txtVarelaRuben_2014_HSP90Inhibitor17-AAG.pdf.txtExtracted texttext/plain29422https://bibliotecadigital.udea.edu.co/bitstreams/2f1f55f0-ba4f-474e-8579-30b6f7e6a2bf/download3ef4d60f923502c9fdeaa5d376f5e910MD54falseAnonymousREADTHUMBNAILVarelaRuben_2014_HSP90Inhibitor17-AAG.pdf.jpgVarelaRuben_2014_HSP90Inhibitor17-AAG.pdf.jpgGenerated Thumbnailimage/jpeg7974https://bibliotecadigital.udea.edu.co/bitstreams/4e0cc320-cbb1-45b6-990e-bda5e41c5fe8/downloadd2a11b1e35c4bf08576b7e3e937b15a7MD55falseAnonymousREAD10495/33047oai:bibliotecadigital.udea.edu.co:10495/330472025-03-26 19:40:12.054http://creativecommons.org/licenses/by-nc-nd/2.5/co/open.accesshttps://bibliotecadigital.udea.edu.coRepositorio Institucional de la Universidad de Antioquiaaplicacionbibliotecadigitalbiblioteca@udea.edu.coTk9URTogUExBQ0UgWU9VUiBPV04gTElDRU5TRSBIRVJFClRoaXMgc2FtcGxlIGxpY2Vuc2UgaXMgcHJvdmlkZWQgZm9yIGluZm9ybWF0aW9uYWwgcHVycG9zZXMgb25seS4KCk5PTi1FWENMVVNJVkUgRElTVFJJQlVUSU9OIExJQ0VOU0UKCkJ5IHNpZ25pbmcgYW5kIHN1Ym1pdHRpbmcgdGhpcyBsaWNlbnNlLCB5b3UgKHRoZSBhdXRob3Iocykgb3IgY29weXJpZ2h0Cm93bmVyKSBncmFudHMgdG8gRFNwYWNlIFVuaXZlcnNpdHkgKERTVSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBEU1UgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgRFNVIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgRFNVIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gRFNVLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpEU1Ugd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo= |