Dimeric procyanidins are inhibitors of NF-κB–DNA binding

Autores
Mackenzie, Gerardo G.; Delfino, Jose Maria; Keen, Carl L.; Fraga, César Guillermo; Oteiza, Patricia Isabel
Año de publicación
2009
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Given the central role of the transcription factor NF-kB in inflammation, molecules that can inhibit NFkB are being actively investigated. The present work characterize potential interactions between dimeric procyanidins [B-type (B1 and B2) and A-type (A1 and A2)] and NF-kB proteins. B1 and B2, inhibited tumor necrosis factor a (TNFa)- and phorbol 12-myristate 13-acetate (PMA)-induced transactivation of NF-kB-driven genes and the increase of NF-kB–DNA nuclear binding in Jurkat T cells. B1 and B2, added in vitro to nuclear fractions, inhibited NF-kB binding to its DNA consensus sequence. B1 and B2 prevented the binding of RelA and p50 recombinant proteins to its DNA consensus sequence. All these effects were not observed with A1 and A2. Putative molecular models for possible interactions of B1, B2, A1 and A2, with NF-kB proteins were constructed, indicating that B-type dimeric procyanidins have higher possibilities of chemical interactions with NF-kB than A-type dimeric procyanidins. The results support the concept that B-type dimeric procyanidins can provide anti-inflammatory benefits due to their ability to reduce NF-kB binding to the DNA.
Fil: Mackenzie, Gerardo G.. University of California; Estados Unidos
Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Keen, Carl L.. University of California; Estados Unidos
Fil: Fraga, César Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of California; Estados Unidos
Fil: Oteiza, Patricia Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina
Materia
Procyanidins
Flavonoids
NF-kB
Immune response
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/102476
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/102476
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Dimeric procyanidins are inhibitors of NF-κB–DNA bindingMackenzie, Gerardo G.Delfino, Jose MariaKeen, Carl L.Fraga, César GuillermoOteiza, Patricia IsabelProcyanidinsFlavonoidsNF-kBImmune responsehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Given the central role of the transcription factor NF-kB in inflammation, molecules that can inhibit NFkB are being actively investigated. The present work characterize potential interactions between dimeric procyanidins [B-type (B1 and B2) and A-type (A1 and A2)] and NF-kB proteins. B1 and B2, inhibited tumor necrosis factor a (TNFa)- and phorbol 12-myristate 13-acetate (PMA)-induced transactivation of NF-kB-driven genes and the increase of NF-kB–DNA nuclear binding in Jurkat T cells. B1 and B2, added in vitro to nuclear fractions, inhibited NF-kB binding to its DNA consensus sequence. B1 and B2 prevented the binding of RelA and p50 recombinant proteins to its DNA consensus sequence. All these effects were not observed with A1 and A2. Putative molecular models for possible interactions of B1, B2, A1 and A2, with NF-kB proteins were constructed, indicating that B-type dimeric procyanidins have higher possibilities of chemical interactions with NF-kB than A-type dimeric procyanidins. The results support the concept that B-type dimeric procyanidins can provide anti-inflammatory benefits due to their ability to reduce NF-kB binding to the DNA.Fil: Mackenzie, Gerardo G.. University of California; Estados UnidosFil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Keen, Carl L.. University of California; Estados UnidosFil: Fraga, César Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of California; Estados UnidosFil: Oteiza, Patricia Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; ArgentinaPergamon-Elsevier Science Ltd2009-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102476Mackenzie, Gerardo G.; Delfino, Jose Maria; Keen, Carl L.; Fraga, César Guillermo; Oteiza, Patricia Isabel; Dimeric procyanidins are inhibitors of NF-κB–DNA binding; Pergamon-Elsevier Science Ltd; Biochemical Pharmacology; 78; 9; 11-2009; 1252-12620006-2952CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcp.2009.06.111info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0006295209005966info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:59:45Zoai:ri.conicet.gov.ar:11336/102476instacron: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:34982025-09-03 09:59:45.876CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Dimeric procyanidins are inhibitors of NF-κB–DNA binding
title Dimeric procyanidins are inhibitors of NF-κB–DNA binding
spellingShingle Dimeric procyanidins are inhibitors of NF-κB–DNA binding
Mackenzie, Gerardo G.
Procyanidins
Flavonoids
NF-kB
Immune response
title_short Dimeric procyanidins are inhibitors of NF-κB–DNA binding
title_full Dimeric procyanidins are inhibitors of NF-κB–DNA binding
title_fullStr Dimeric procyanidins are inhibitors of NF-κB–DNA binding
title_full_unstemmed Dimeric procyanidins are inhibitors of NF-κB–DNA binding
title_sort Dimeric procyanidins are inhibitors of NF-κB–DNA binding
dc.creator.none.fl_str_mv Mackenzie, Gerardo G.
Delfino, Jose Maria
Keen, Carl L.
Fraga, César Guillermo
Oteiza, Patricia Isabel
author Mackenzie, Gerardo G.
author_facet Mackenzie, Gerardo G.
Delfino, Jose Maria
Keen, Carl L.
Fraga, César Guillermo
Oteiza, Patricia Isabel
author_role author
author2 Delfino, Jose Maria
Keen, Carl L.
Fraga, César Guillermo
Oteiza, Patricia Isabel
author2_role author
author
author
author
dc.subject.none.fl_str_mv Procyanidins
Flavonoids
NF-kB
Immune response
topic Procyanidins
Flavonoids
NF-kB
Immune response
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Given the central role of the transcription factor NF-kB in inflammation, molecules that can inhibit NFkB are being actively investigated. The present work characterize potential interactions between dimeric procyanidins [B-type (B1 and B2) and A-type (A1 and A2)] and NF-kB proteins. B1 and B2, inhibited tumor necrosis factor a (TNFa)- and phorbol 12-myristate 13-acetate (PMA)-induced transactivation of NF-kB-driven genes and the increase of NF-kB–DNA nuclear binding in Jurkat T cells. B1 and B2, added in vitro to nuclear fractions, inhibited NF-kB binding to its DNA consensus sequence. B1 and B2 prevented the binding of RelA and p50 recombinant proteins to its DNA consensus sequence. All these effects were not observed with A1 and A2. Putative molecular models for possible interactions of B1, B2, A1 and A2, with NF-kB proteins were constructed, indicating that B-type dimeric procyanidins have higher possibilities of chemical interactions with NF-kB than A-type dimeric procyanidins. The results support the concept that B-type dimeric procyanidins can provide anti-inflammatory benefits due to their ability to reduce NF-kB binding to the DNA.
Fil: Mackenzie, Gerardo G.. University of California; Estados Unidos
Fil: Delfino, Jose Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Keen, Carl L.. University of California; Estados Unidos
Fil: Fraga, César Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. University of California; Estados Unidos
Fil: Oteiza, Patricia Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Programa de Radicales Libres; Argentina. University of California; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentina
description Given the central role of the transcription factor NF-kB in inflammation, molecules that can inhibit NFkB are being actively investigated. The present work characterize potential interactions between dimeric procyanidins [B-type (B1 and B2) and A-type (A1 and A2)] and NF-kB proteins. B1 and B2, inhibited tumor necrosis factor a (TNFa)- and phorbol 12-myristate 13-acetate (PMA)-induced transactivation of NF-kB-driven genes and the increase of NF-kB–DNA nuclear binding in Jurkat T cells. B1 and B2, added in vitro to nuclear fractions, inhibited NF-kB binding to its DNA consensus sequence. B1 and B2 prevented the binding of RelA and p50 recombinant proteins to its DNA consensus sequence. All these effects were not observed with A1 and A2. Putative molecular models for possible interactions of B1, B2, A1 and A2, with NF-kB proteins were constructed, indicating that B-type dimeric procyanidins have higher possibilities of chemical interactions with NF-kB than A-type dimeric procyanidins. The results support the concept that B-type dimeric procyanidins can provide anti-inflammatory benefits due to their ability to reduce NF-kB binding to the DNA.
publishDate 2009
dc.date.none.fl_str_mv 2009-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/102476
Mackenzie, Gerardo G.; Delfino, Jose Maria; Keen, Carl L.; Fraga, César Guillermo; Oteiza, Patricia Isabel; Dimeric procyanidins are inhibitors of NF-κB–DNA binding; Pergamon-Elsevier Science Ltd; Biochemical Pharmacology; 78; 9; 11-2009; 1252-1262
0006-2952
CONICET Digital
CONICET
url http://hdl.handle.net/11336/102476
identifier_str_mv Mackenzie, Gerardo G.; Delfino, Jose Maria; Keen, Carl L.; Fraga, César Guillermo; Oteiza, Patricia Isabel; Dimeric procyanidins are inhibitors of NF-κB–DNA binding; Pergamon-Elsevier Science Ltd; Biochemical Pharmacology; 78; 9; 11-2009; 1252-1262
0006-2952
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bcp.2009.06.111
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0006295209005966
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
publisher.none.fl_str_mv Pergamon-Elsevier Science Ltd
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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