Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect

Autores
Henning, María Florencia; Herlax, Vanesa Silvana; Bakás, Laura Susana
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
It is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that interaction. The presented data indicate that LPS does not lead to major changes in the structure of apoAI, judging from Trp fluorescence spectra. However, analysis of denaturation behavior and binding of ANS show that LPS induces a loosened protein conformation. Further evidence for an apoAI-LPS specific interaction was obtained by incubation of the protein with 125I-ASD- LPS. The results show that multiple regions of the protein were able to interact with LPS, according to its amphiphatic nature. Finally, the contribution of the purified C-terminal fragment of the protein in the endotoxin neutralization was evaluated in comparison with the effect of apoAI. In both cases, the same decrease in tumor necrosis factor-α released was observed. This result suggests that the C-terminal half of apoAI is the main domain responsible of the neutralization effect of this protein. Our data may provide innovative pharmacological tools in endotoxin neutralization therapies.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/83921
Acceder
id SEDICI_9f62046915a3d3352c6e6e09bbb3bd9f
oai_identifier_str oai:sedici.unlp.edu.ar:10915/83921
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effectHenning, María FlorenciaHerlax, Vanesa SilvanaBakás, Laura SusanaBiologíaANSASD-LPSGdnHCl denaturationlipoproteinTNF-alphaIt is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that interaction. The presented data indicate that LPS does not lead to major changes in the structure of apoAI, judging from Trp fluorescence spectra. However, analysis of denaturation behavior and binding of ANS show that LPS induces a loosened protein conformation. Further evidence for an apoAI-LPS specific interaction was obtained by incubation of the protein with 125I-ASD- LPS. The results show that multiple regions of the protein were able to interact with LPS, according to its amphiphatic nature. Finally, the contribution of the purified C-terminal fragment of the protein in the endotoxin neutralization was evaluated in comparison with the effect of apoAI. In both cases, the same decrease in tumor necrosis factor-α released was observed. This result suggests that the C-terminal half of apoAI is the main domain responsible of the neutralization effect of this protein. Our data may provide innovative pharmacological tools in endotoxin neutralization therapies.Instituto de Investigaciones Bioquímicas de La Plata2011info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf327-337http://sedici.unlp.edu.ar/handle/10915/83921enginfo:eu-repo/semantics/altIdentifier/issn/1753-4259info:eu-repo/semantics/altIdentifier/doi/10.1177/1753425910370709info: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:UNLP2025-09-29T11:16:06Zoai:sedici.unlp.edu.ar:10915/83921Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:16:06.57SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
spellingShingle Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
Henning, María Florencia
Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
title_short Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_full Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_fullStr Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_full_unstemmed Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
title_sort Contribution of the C-terminal end of apolipoprotein AI to neutralization of lipopolysaccharide endotoxic effect
dc.creator.none.fl_str_mv Henning, María Florencia
Herlax, Vanesa Silvana
Bakás, Laura Susana
author Henning, María Florencia
author_facet Henning, María Florencia
Herlax, Vanesa Silvana
Bakás, Laura Susana
author_role author
author2 Herlax, Vanesa Silvana
Bakás, Laura Susana
author2_role author
author
dc.subject.none.fl_str_mv Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
topic Biología
ANS
ASD-LPS
GdnHCl denaturation
lipoprotein
TNF-alpha
dc.description.none.fl_txt_mv It is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that interaction. The presented data indicate that LPS does not lead to major changes in the structure of apoAI, judging from Trp fluorescence spectra. However, analysis of denaturation behavior and binding of ANS show that LPS induces a loosened protein conformation. Further evidence for an apoAI-LPS specific interaction was obtained by incubation of the protein with 125I-ASD- LPS. The results show that multiple regions of the protein were able to interact with LPS, according to its amphiphatic nature. Finally, the contribution of the purified C-terminal fragment of the protein in the endotoxin neutralization was evaluated in comparison with the effect of apoAI. In both cases, the same decrease in tumor necrosis factor-α released was observed. This result suggests that the C-terminal half of apoAI is the main domain responsible of the neutralization effect of this protein. Our data may provide innovative pharmacological tools in endotoxin neutralization therapies.
Instituto de Investigaciones Bioquímicas de La Plata
description It is well known that high density lipoprotein (HDL) binds bacterial lipopolysaccharide (LPS) and neutralizes its toxicity. The aim of this work was to study changes in the apolipoprotein (apo) AI structure after its interaction with LPS as well as to determine the protein domain involved in that interaction. The presented data indicate that LPS does not lead to major changes in the structure of apoAI, judging from Trp fluorescence spectra. However, analysis of denaturation behavior and binding of ANS show that LPS induces a loosened protein conformation. Further evidence for an apoAI-LPS specific interaction was obtained by incubation of the protein with 125I-ASD- LPS. The results show that multiple regions of the protein were able to interact with LPS, according to its amphiphatic nature. Finally, the contribution of the purified C-terminal fragment of the protein in the endotoxin neutralization was evaluated in comparison with the effect of apoAI. In both cases, the same decrease in tumor necrosis factor-α released was observed. This result suggests that the C-terminal half of apoAI is the main domain responsible of the neutralization effect of this protein. Our data may provide innovative pharmacological tools in endotoxin neutralization therapies.
publishDate 2011
dc.date.none.fl_str_mv 2011
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/83921
url http://sedici.unlp.edu.ar/handle/10915/83921
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1753-4259
info:eu-repo/semantics/altIdentifier/doi/10.1177/1753425910370709
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
327-337
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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