Alteration of the serum N-glycome of mice ...
Type de document :
Article dans une revue scientifique
DOI :
PMID :
URL permanente :
Titre :
Alteration of the serum N-glycome of mice locally exposed to high doses of ionizing radiation
Auteur(s) :
Chaze, Thibault [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Slomianny, Marie-Christine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Milliat, Fabien [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Tarlet, Georges [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Gourmelon, Patrick [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Bey, Eric [Auteur]
Benderitter, Marc [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Guipaud, Olivier [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Slomianny, Marie-Christine [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Milliat, Fabien [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Tarlet, Georges [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Lefebvre, Tony [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Gourmelon, Patrick [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Bey, Eric [Auteur]
Benderitter, Marc [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Michalski, Jean-Claude [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Guipaud, Olivier [Auteur]
Institut de Radioprotection et de Sûreté Nucléaire [IRSN]
Titre de la revue :
Molecular & cellular proteomics. MCP
Nom court de la revue :
Mol. Cell Proteomics
Numéro :
12
Pagination :
283-301
Date de publication :
2013-02
ISSN :
1535-9484
Mot(s)-clé(s) en anglais :
Gamma Rays
Humans
Liver
Glycomics
Molecular Sequence Data
Male
Electrophoresis, Gel, Two-Dimensional
Interleukin-6
Adult
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Principal Component Analysis
Carbohydrate Sequence
Gene Expression Regulation
Glycosylation
Interleukin-1beta
Tumor Necrosis Factor-alpha
Animals
Blood Proteins
Mice
Protein Processing, Post-Translational
Mice, Inbred BALB C
Skin
Burns
Polysaccharide
Radiation Injuries, Experimental
Humans
Liver
Glycomics
Molecular Sequence Data
Male
Electrophoresis, Gel, Two-Dimensional
Interleukin-6
Adult
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Principal Component Analysis
Carbohydrate Sequence
Gene Expression Regulation
Glycosylation
Interleukin-1beta
Tumor Necrosis Factor-alpha
Animals
Blood Proteins
Mice
Protein Processing, Post-Translational
Mice, Inbred BALB C
Skin
Burns
Polysaccharide
Radiation Injuries, Experimental
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Exposure of the skin to ionizing radiation leads to characteristic reactions that will often turn into a pathophysiological process called the cutaneous radiation syndrome. The study of this disorder is crucial to finding ...
Lire la suite >Exposure of the skin to ionizing radiation leads to characteristic reactions that will often turn into a pathophysiological process called the cutaneous radiation syndrome. The study of this disorder is crucial to finding diagnostic and prognostic bioindicators of local radiation exposure or radiation effects. It is known that irradiation alters the serum proteome content and potentially post-translationally modifies serum proteins. In this study, we investigated whether localized irradiation of the skin alters the serum glycome. Two-dimensional differential in-gel electrophoresis of serum proteins from a man and from mice exposed to ionizing radiation showed that potential post-translational modification changes occurred following irradiation. Using a large-scale quantitative mass-spectrometry-based glycomic approach, we performed a global analysis of glycan structures of serum proteins from non-irradiated and locally irradiated mice exposed to high doses of γ-rays (20, 40, and 80 Gy). Non-supervised descriptive statistical analyses (principal component analysis) using quantitative glycan structure data allowed us to discriminate between uninjured/slightly injured animals and animals that developed severe lesions. Decisional statistics showed that several glycan families were down-regulated whereas others increased, and that particular structures were statistically significantly changed in the serum of locally irradiated mice. The observed increases in multiantennary N-glycans and in outer branch fucosylation and sialylation were associated with the up-regulation of genes involved in glycosylation in the liver, which is the main producer of serum proteins, and with an increase in the key proinflammatory serum cytokines IL-1β, IL-6, and TNFα, which can regulate the expression of glycosylation genes. Our results suggest for the first time a role of serum protein glycosylation in response to irradiation. These protein-associated glycan structure changes might signal radiation exposure or effects.Lire moins >
Lire la suite >Exposure of the skin to ionizing radiation leads to characteristic reactions that will often turn into a pathophysiological process called the cutaneous radiation syndrome. The study of this disorder is crucial to finding diagnostic and prognostic bioindicators of local radiation exposure or radiation effects. It is known that irradiation alters the serum proteome content and potentially post-translationally modifies serum proteins. In this study, we investigated whether localized irradiation of the skin alters the serum glycome. Two-dimensional differential in-gel electrophoresis of serum proteins from a man and from mice exposed to ionizing radiation showed that potential post-translational modification changes occurred following irradiation. Using a large-scale quantitative mass-spectrometry-based glycomic approach, we performed a global analysis of glycan structures of serum proteins from non-irradiated and locally irradiated mice exposed to high doses of γ-rays (20, 40, and 80 Gy). Non-supervised descriptive statistical analyses (principal component analysis) using quantitative glycan structure data allowed us to discriminate between uninjured/slightly injured animals and animals that developed severe lesions. Decisional statistics showed that several glycan families were down-regulated whereas others increased, and that particular structures were statistically significantly changed in the serum of locally irradiated mice. The observed increases in multiantennary N-glycans and in outer branch fucosylation and sialylation were associated with the up-regulation of genes involved in glycosylation in the liver, which is the main producer of serum proteins, and with an increase in the key proinflammatory serum cytokines IL-1β, IL-6, and TNFα, which can regulate the expression of glycosylation genes. Our results suggest for the first time a role of serum protein glycosylation in response to irradiation. These protein-associated glycan structure changes might signal radiation exposure or effects.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Date de dépôt :
2020-02-12T15:12:10Z
2021-03-04T13:49:58Z
2021-03-04T13:49:58Z
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