Proteomic Analysis of Pig (Sus scrofa) ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Proteomic Analysis of Pig (Sus scrofa) Olfactory Soluble Proteome Reveals O-Linked-N-Acetylglucosaminylation of Secreted Odorant-Binding Proteins
Auteur(s) :
Nagnan, Patricia [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Edouart (vercoutter), Anne-Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Hilliou, Frédérique [Auteur]
Institut Sophia Agrobiotech [ISA]
Le Danvic, Chrystelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lévy, Frédéric [Auteur]
Physiologie de la reproduction et des comportements [Nouzilly] [PRC]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Edouart (vercoutter), Anne-Sophie [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Hilliou, Frédérique [Auteur]
Institut Sophia Agrobiotech [ISA]
Le Danvic, Chrystelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lévy, Frédéric [Auteur]
Physiologie de la reproduction et des comportements [Nouzilly] [PRC]
Titre de la revue :
Frontiers in endocrinology
Numéro :
5
Date de publication :
2014-12-05
ISSN :
1664-2392
Mot(s)-clé(s) en anglais :
odorant-binding protein
olfaction
extracellular O-linked-N-acetylglucosaminylation
olfactory secretome
O-GlcNAc transferase
olfaction
extracellular O-linked-N-acetylglucosaminylation
olfactory secretome
O-GlcNAc transferase
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
The diversity of olfactory binding proteins (OBPs) is a key point to understand their role in molecular olfaction. Since only few different sequences were characterized in each mammalian species, they have been considered ...
Lire la suite >The diversity of olfactory binding proteins (OBPs) is a key point to understand their role in molecular olfaction. Since only few different sequences were characterized in each mammalian species, they have been considered as passive carriers of odors and pheromones. We have explored the soluble proteome of pig nasal mucus, taking benefit of the powerful tools of proteomics. Combining two-dimensional electrophoresis, mass spectrometry, and western-blot with specific antibodies, our analyses revealed for the first time that the pig nasal mucus is mainly composed of secreted OBP isoforms, some of them being potentially modified by O-GlcNAcylation. An ortholog gene of the glycosyltransferase responsible of the O-GlcNAc linking on extracellular proteins in Drosophila and Mouse (EOGT) was amplified from tissues of pigs of different ages and sex. The sequence was used in a phylogenetic analysis, which evidenced conservation of EOGT in insect and mammalian models studied in molecular olfaction. Extracellular O-GlcNAcylation of secreted OBPs could finely modulate their binding specificities to odors and pheromones. This constitutes a new mechanism for extracellular signaling by OBPs, suggesting that they act as the first step of odor discrimination.Lire moins >
Lire la suite >The diversity of olfactory binding proteins (OBPs) is a key point to understand their role in molecular olfaction. Since only few different sequences were characterized in each mammalian species, they have been considered as passive carriers of odors and pheromones. We have explored the soluble proteome of pig nasal mucus, taking benefit of the powerful tools of proteomics. Combining two-dimensional electrophoresis, mass spectrometry, and western-blot with specific antibodies, our analyses revealed for the first time that the pig nasal mucus is mainly composed of secreted OBP isoforms, some of them being potentially modified by O-GlcNAcylation. An ortholog gene of the glycosyltransferase responsible of the O-GlcNAc linking on extracellular proteins in Drosophila and Mouse (EOGT) was amplified from tissues of pigs of different ages and sex. The sequence was used in a phylogenetic analysis, which evidenced conservation of EOGT in insect and mammalian models studied in molecular olfaction. Extracellular O-GlcNAcylation of secreted OBPs could finely modulate their binding specificities to odors and pheromones. This constitutes a new mechanism for extracellular signaling by OBPs, suggesting that they act as the first step of odor discrimination.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Glycobiologie de l’olfaction
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
O-GlcNAcylation, signalisation cellulaire et cycle cellulaire
Date de dépôt :
2020-02-12T15:12:36Z
2021-03-18T14:53:30Z
2021-03-18T14:53:30Z
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