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dc.contributor.author
Herrera, Maria Georgina
dc.contributor.author
Pizzuto, Malvina
dc.contributor.author
Lonez, Caroline
dc.contributor.author
Rott, Karsten
dc.contributor.author
Hütten, Andreas
dc.contributor.author
Sewald, Norbert
dc.contributor.author
Ruysschaert, Jean-Marie
dc.contributor.author
Dodero, Veronica Isabel
dc.date.available
2019-12-27T16:09:25Z
dc.date.issued
2018-06
dc.identifier.citation
Herrera, Maria Georgina; Pizzuto, Malvina; Lonez, Caroline; Rott, Karsten; Hütten, Andreas; et al.; Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages; Elsevier Science; Nanomedicine-nanotechnology Biology And Medicine; 14; 4; 6-2018; 1417-1427
dc.identifier.issn
1549-9634
dc.identifier.uri
http://hdl.handle.net/11336/93096
dc.description.abstract
Gliadin, an immunogenic protein present in wheat, is not fully degraded by humans and after the normal gastric and pancreatic digestion, the immunodominant 33-mer gliadin peptide remains unprocessed. The 33-mer gliadin peptide is found in human faeces and urine, proving not only its proteolytic resistance in vivo but more importantly its transport through the entire human body. Here, we demonstrate that 33-mer supramolecular structures larger than 220 nm induce the overexpression of nuclear factor kappa B (NF-κB) via a specific Toll-like Receptor (TLR) 2 and (TLR) 4 dependent pathway and the secretion of pro-inflammatory cytokines such as IP-10/CXCL10 and TNF-α. Using helium ion microscopy, we elucidated the initial stages of oligomerisation of 33-mer gliadin peptide, showing that rod-like oligomers are nucleation sites for protofilament formation. The relevance of the 33-mer supramolecular structures in the early stages of the disease is paving new perspectives in the understanding of gluten-related disorders.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
CELIAC DISEASE
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GLUTEN-RELATED DISORDERS
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HELIUM ION MICROSCOPY
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INNATE IMMUNE RESPONSE
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OLIGOMERS
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Large supramolecular structures of 33-mer gliadin peptide activate toll-like receptors in macrophages
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-21T19:01:34Z
dc.journal.volume
14
dc.journal.number
4
dc.journal.pagination
1417-1427
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Herrera, Maria Georgina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Pizzuto, Malvina. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Lonez, Caroline. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Rott, Karsten. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Hütten, Andreas. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Sewald, Norbert. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Ruysschaert, Jean-Marie. Université Libre de Bruxelles; Bélgica
dc.description.fil
Fil: Dodero, Veronica Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universitat Bielefeld; Alemania
dc.journal.title
Nanomedicine-nanotechnology Biology And Medicine
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://linkinghub.elsevier.com/retrieve/pii/S1549963418300868
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.nano.2018.04.014
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