Cereal Proteins: Immunostimulatory and Toxic Peptides

Autores
Chirdo, Fernando Gabriel; Arranz, Eduardo; Arranz, Eduardo; Fernández Bañares, Fernando; Rosell, Cristina M.; Amado, Luis Rodrigo; Peña, Salvador
Año de publicación
2015
Idioma
inglés
Tipo de recurso
parte de libro
Estado
versión publicada
Descripción
Storage proteins from wheat kernels are the base of a wide variety of homemade and industrial food products. Nonetheless, for a group of individuals (celiac disease (CD) patients), these proteins are toxic. Gliadins and glutenins from wheat, as well as their counterparts in barley and rye, also called prolamins, are evolutionary related, and present a high degree of homology. Polyclonal and monoclonal antibodies raised against prolamins have been a very useful tool to characterise structural and conformational features of prolamins, and particularly, for gluten analysis based on immunochemical techniques. Complete adherence to a gluten-free diet is required to recover the normal histology of the small intestine in CD patients. To this end, the use of certified gluten-free products is mandatory. Aqueous solvents such as 60-70% ethanol, have been used for extraction of prolamins from flours and food. This method is not selective and, therefore, results in complex mixtures of proteins which together with their low solubility in aqueous solutions, high degree of homology, and consequently crossreactivity, produce some drawbacks in gluten analysis by immunoassays. Prolamins drive an exacerbated immune response in intestinal mucosa of CD patients. T lymphocytes are a central piece in CD pathogenesis. However, new insights in the knowledge of innate immunity point out to some gliadin peptides which can also produce structural changes in the intestine as well as inflammatory reactions.
Instituto de Estudios Inmunológicos y Fisiopatológicos
Materia
Biología
Gliadins
glutenins
prolamins
toxic proteins
gluten analysis
immune response
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:10915/152536

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spelling Cereal Proteins: Immunostimulatory and Toxic PeptidesChirdo, Fernando GabrielArranz, EduardoArranz, EduardoFernández Bañares, FernandoRosell, Cristina M.Amado, Luis RodrigoPeña, SalvadorBiologíaGliadinsgluteninsprolaminstoxic proteinsgluten analysisimmune responseStorage proteins from wheat kernels are the base of a wide variety of homemade and industrial food products. Nonetheless, for a group of individuals (celiac disease (CD) patients), these proteins are toxic. Gliadins and glutenins from wheat, as well as their counterparts in barley and rye, also called prolamins, are evolutionary related, and present a high degree of homology. Polyclonal and monoclonal antibodies raised against prolamins have been a very useful tool to characterise structural and conformational features of prolamins, and particularly, for gluten analysis based on immunochemical techniques. Complete adherence to a gluten-free diet is required to recover the normal histology of the small intestine in CD patients. To this end, the use of certified gluten-free products is mandatory. Aqueous solvents such as 60-70% ethanol, have been used for extraction of prolamins from flours and food. This method is not selective and, therefore, results in complex mixtures of proteins which together with their low solubility in aqueous solutions, high degree of homology, and consequently crossreactivity, produce some drawbacks in gluten analysis by immunoassays. Prolamins drive an exacerbated immune response in intestinal mucosa of CD patients. T lymphocytes are a central piece in CD pathogenesis. However, new insights in the knowledge of innate immunity point out to some gliadin peptides which can also produce structural changes in the intestine as well as inflammatory reactions.Instituto de Estudios Inmunológicos y FisiopatológicosOmniaScience2015info:eu-repo/semantics/bookPartinfo:eu-repo/semantics/publishedVersionCapitulo de librohttp://purl.org/coar/resource_type/c_3248info:ar-repo/semantics/parteDeLibroapplication/pdf141-162http://sedici.unlp.edu.ar/handle/10915/152536enginfo:eu-repo/semantics/altIdentifier/isbn/978-84-943418-2-3info:eu-repo/semantics/altIdentifier/doi/10.3926/oms.251info: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:UNLP2025-09-29T11:39:28Zoai:sedici.unlp.edu.ar:10915/152536Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:39:28.549SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Cereal Proteins: Immunostimulatory and Toxic Peptides
title Cereal Proteins: Immunostimulatory and Toxic Peptides
spellingShingle Cereal Proteins: Immunostimulatory and Toxic Peptides
Chirdo, Fernando Gabriel
Biología
Gliadins
glutenins
prolamins
toxic proteins
gluten analysis
immune response
title_short Cereal Proteins: Immunostimulatory and Toxic Peptides
title_full Cereal Proteins: Immunostimulatory and Toxic Peptides
title_fullStr Cereal Proteins: Immunostimulatory and Toxic Peptides
title_full_unstemmed Cereal Proteins: Immunostimulatory and Toxic Peptides
title_sort Cereal Proteins: Immunostimulatory and Toxic Peptides
dc.creator.none.fl_str_mv Chirdo, Fernando Gabriel
Arranz, Eduardo
Arranz, Eduardo
Fernández Bañares, Fernando
Rosell, Cristina M.
Amado, Luis Rodrigo
Peña, Salvador
author Chirdo, Fernando Gabriel
author_facet Chirdo, Fernando Gabriel
Arranz, Eduardo
Fernández Bañares, Fernando
Rosell, Cristina M.
Amado, Luis Rodrigo
Peña, Salvador
author_role author
author2 Arranz, Eduardo
Fernández Bañares, Fernando
Rosell, Cristina M.
Amado, Luis Rodrigo
Peña, Salvador
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Biología
Gliadins
glutenins
prolamins
toxic proteins
gluten analysis
immune response
topic Biología
Gliadins
glutenins
prolamins
toxic proteins
gluten analysis
immune response
dc.description.none.fl_txt_mv Storage proteins from wheat kernels are the base of a wide variety of homemade and industrial food products. Nonetheless, for a group of individuals (celiac disease (CD) patients), these proteins are toxic. Gliadins and glutenins from wheat, as well as their counterparts in barley and rye, also called prolamins, are evolutionary related, and present a high degree of homology. Polyclonal and monoclonal antibodies raised against prolamins have been a very useful tool to characterise structural and conformational features of prolamins, and particularly, for gluten analysis based on immunochemical techniques. Complete adherence to a gluten-free diet is required to recover the normal histology of the small intestine in CD patients. To this end, the use of certified gluten-free products is mandatory. Aqueous solvents such as 60-70% ethanol, have been used for extraction of prolamins from flours and food. This method is not selective and, therefore, results in complex mixtures of proteins which together with their low solubility in aqueous solutions, high degree of homology, and consequently crossreactivity, produce some drawbacks in gluten analysis by immunoassays. Prolamins drive an exacerbated immune response in intestinal mucosa of CD patients. T lymphocytes are a central piece in CD pathogenesis. However, new insights in the knowledge of innate immunity point out to some gliadin peptides which can also produce structural changes in the intestine as well as inflammatory reactions.
Instituto de Estudios Inmunológicos y Fisiopatológicos
description Storage proteins from wheat kernels are the base of a wide variety of homemade and industrial food products. Nonetheless, for a group of individuals (celiac disease (CD) patients), these proteins are toxic. Gliadins and glutenins from wheat, as well as their counterparts in barley and rye, also called prolamins, are evolutionary related, and present a high degree of homology. Polyclonal and monoclonal antibodies raised against prolamins have been a very useful tool to characterise structural and conformational features of prolamins, and particularly, for gluten analysis based on immunochemical techniques. Complete adherence to a gluten-free diet is required to recover the normal histology of the small intestine in CD patients. To this end, the use of certified gluten-free products is mandatory. Aqueous solvents such as 60-70% ethanol, have been used for extraction of prolamins from flours and food. This method is not selective and, therefore, results in complex mixtures of proteins which together with their low solubility in aqueous solutions, high degree of homology, and consequently crossreactivity, produce some drawbacks in gluten analysis by immunoassays. Prolamins drive an exacerbated immune response in intestinal mucosa of CD patients. T lymphocytes are a central piece in CD pathogenesis. However, new insights in the knowledge of innate immunity point out to some gliadin peptides which can also produce structural changes in the intestine as well as inflammatory reactions.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/bookPart
info:eu-repo/semantics/publishedVersion
Capitulo de libro
http://purl.org/coar/resource_type/c_3248
info:ar-repo/semantics/parteDeLibro
format bookPart
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/152536
url http://sedici.unlp.edu.ar/handle/10915/152536
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/isbn/978-84-943418-2-3
info:eu-repo/semantics/altIdentifier/doi/10.3926/oms.251
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
141-162
dc.publisher.none.fl_str_mv OmniaScience
publisher.none.fl_str_mv OmniaScience
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
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