Induction of eryptosis by low concentrations of E. coli alpha-hemolysin
- Autores
- Carrizo Velásquez, Fernanda; Maté, Sabina María; Bakás, Laura Susana; Herlax, Vanesa Silvana
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Uropathogenic strains of Escherichia coli deliver the toxin alpha-hemolysin (HlyA) to optimize the host environment for the spread of infection. It was reported that at high concentrations, the toxin forms pores in eukaryotic membranes, leading to cell lysis, while lower concentrations have appeared to interfere with host-cell-signaling pathways causing cell death by apoptosis. Nevertheless, what is not clear is how often HlyA reaches levels that are high enough to lyse host target cells during the course of an infection. In the present investigation, we demonstrate that a low toxin concentration induces the suicidal death of erythrocytes (eryptosis), the major cell type present in blood. Eryptosis is triggered both by an increment in intracellular calcium and by ceramide. Since we have previously demonstrated that a low concentration of HlyA induces an increase in intraerythrocyte calcium, in the present experiments we have shown that this ion activates calpains, which hydrolyze skeleton proteins such as spectrin, ankyrin, protein 4.1 and the electrophoretic Band-3 species, thus resulting in morphologic changes in the erythrocytes. We furthermore observed that a low toxin concentration induced the activation of endogenous sphingomyelinases that in turn increased the amount of ceramide in erythrocyte membranes. Both spectrin proteolysis and ceramide formation may cause the exposure of phosphatidylserine on the membrane so as to trigger a macrophage engulfment of the erythrocyte. By this means eryptosis may be an advantageous mechanism for removing defective erythrocytes before hemolysis.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Exactas - Materia
-
Bioquímica
Abbreviations HlyA alpha hemolysin
PC phosphatidylcholine
PS phosphatidylserine
SM sphingomyelin
SMase sphingomyelinase - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/86388
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Induction of eryptosis by low concentrations of E. coli alpha-hemolysinCarrizo Velásquez, FernandaMaté, Sabina MaríaBakás, Laura SusanaHerlax, Vanesa SilvanaBioquímicaAbbreviations HlyA alpha hemolysinPC phosphatidylcholinePS phosphatidylserineSM sphingomyelinSMase sphingomyelinaseUropathogenic strains of Escherichia coli deliver the toxin alpha-hemolysin (HlyA) to optimize the host environment for the spread of infection. It was reported that at high concentrations, the toxin forms pores in eukaryotic membranes, leading to cell lysis, while lower concentrations have appeared to interfere with host-cell-signaling pathways causing cell death by apoptosis. Nevertheless, what is not clear is how often HlyA reaches levels that are high enough to lyse host target cells during the course of an infection. In the present investigation, we demonstrate that a low toxin concentration induces the suicidal death of erythrocytes (eryptosis), the major cell type present in blood. Eryptosis is triggered both by an increment in intracellular calcium and by ceramide. Since we have previously demonstrated that a low concentration of HlyA induces an increase in intraerythrocyte calcium, in the present experiments we have shown that this ion activates calpains, which hydrolyze skeleton proteins such as spectrin, ankyrin, protein 4.1 and the electrophoretic Band-3 species, thus resulting in morphologic changes in the erythrocytes. We furthermore observed that a low toxin concentration induced the activation of endogenous sphingomyelinases that in turn increased the amount of ceramide in erythrocyte membranes. Both spectrin proteolysis and ceramide formation may cause the exposure of phosphatidylserine on the membrane so as to trigger a macrophage engulfment of the erythrocyte. By this means eryptosis may be an advantageous mechanism for removing defective erythrocytes before hemolysis.Instituto de Investigaciones Bioquímicas de La PlataFacultad de Ciencias Exactas2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf2779-2788http://sedici.unlp.edu.ar/handle/10915/86388enginfo:eu-repo/semantics/altIdentifier/issn/0005-2736info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2015.08.012info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:16:54Zoai:sedici.unlp.edu.ar:10915/86388Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:54.445SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
title |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
spellingShingle |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin Carrizo Velásquez, Fernanda Bioquímica Abbreviations HlyA alpha hemolysin PC phosphatidylcholine PS phosphatidylserine SM sphingomyelin SMase sphingomyelinase |
title_short |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
title_full |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
title_fullStr |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
title_full_unstemmed |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
title_sort |
Induction of eryptosis by low concentrations of E. coli alpha-hemolysin |
dc.creator.none.fl_str_mv |
Carrizo Velásquez, Fernanda Maté, Sabina María Bakás, Laura Susana Herlax, Vanesa Silvana |
author |
Carrizo Velásquez, Fernanda |
author_facet |
Carrizo Velásquez, Fernanda Maté, Sabina María Bakás, Laura Susana Herlax, Vanesa Silvana |
author_role |
author |
author2 |
Maté, Sabina María Bakás, Laura Susana Herlax, Vanesa Silvana |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Bioquímica Abbreviations HlyA alpha hemolysin PC phosphatidylcholine PS phosphatidylserine SM sphingomyelin SMase sphingomyelinase |
topic |
Bioquímica Abbreviations HlyA alpha hemolysin PC phosphatidylcholine PS phosphatidylserine SM sphingomyelin SMase sphingomyelinase |
dc.description.none.fl_txt_mv |
Uropathogenic strains of Escherichia coli deliver the toxin alpha-hemolysin (HlyA) to optimize the host environment for the spread of infection. It was reported that at high concentrations, the toxin forms pores in eukaryotic membranes, leading to cell lysis, while lower concentrations have appeared to interfere with host-cell-signaling pathways causing cell death by apoptosis. Nevertheless, what is not clear is how often HlyA reaches levels that are high enough to lyse host target cells during the course of an infection. In the present investigation, we demonstrate that a low toxin concentration induces the suicidal death of erythrocytes (eryptosis), the major cell type present in blood. Eryptosis is triggered both by an increment in intracellular calcium and by ceramide. Since we have previously demonstrated that a low concentration of HlyA induces an increase in intraerythrocyte calcium, in the present experiments we have shown that this ion activates calpains, which hydrolyze skeleton proteins such as spectrin, ankyrin, protein 4.1 and the electrophoretic Band-3 species, thus resulting in morphologic changes in the erythrocytes. We furthermore observed that a low toxin concentration induced the activation of endogenous sphingomyelinases that in turn increased the amount of ceramide in erythrocyte membranes. Both spectrin proteolysis and ceramide formation may cause the exposure of phosphatidylserine on the membrane so as to trigger a macrophage engulfment of the erythrocyte. By this means eryptosis may be an advantageous mechanism for removing defective erythrocytes before hemolysis. Instituto de Investigaciones Bioquímicas de La Plata Facultad de Ciencias Exactas |
description |
Uropathogenic strains of Escherichia coli deliver the toxin alpha-hemolysin (HlyA) to optimize the host environment for the spread of infection. It was reported that at high concentrations, the toxin forms pores in eukaryotic membranes, leading to cell lysis, while lower concentrations have appeared to interfere with host-cell-signaling pathways causing cell death by apoptosis. Nevertheless, what is not clear is how often HlyA reaches levels that are high enough to lyse host target cells during the course of an infection. In the present investigation, we demonstrate that a low toxin concentration induces the suicidal death of erythrocytes (eryptosis), the major cell type present in blood. Eryptosis is triggered both by an increment in intracellular calcium and by ceramide. Since we have previously demonstrated that a low concentration of HlyA induces an increase in intraerythrocyte calcium, in the present experiments we have shown that this ion activates calpains, which hydrolyze skeleton proteins such as spectrin, ankyrin, protein 4.1 and the electrophoretic Band-3 species, thus resulting in morphologic changes in the erythrocytes. We furthermore observed that a low toxin concentration induced the activation of endogenous sphingomyelinases that in turn increased the amount of ceramide in erythrocyte membranes. Both spectrin proteolysis and ceramide formation may cause the exposure of phosphatidylserine on the membrane so as to trigger a macrophage engulfment of the erythrocyte. By this means eryptosis may be an advantageous mechanism for removing defective erythrocytes before hemolysis. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Articulo 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://sedici.unlp.edu.ar/handle/10915/86388 |
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http://sedici.unlp.edu.ar/handle/10915/86388 |
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eng |
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eng |
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