Alteration of the serum N-glycome of mice ...
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Article dans une revue scientifique
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Title :
Alteration of the serum N-glycome of mice locally exposed to high doses of ionizing radiation
Author(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]
Journal title :
Molecular & cellular proteomics. MCP
Abbreviated title :
Mol. Cell Proteomics
Volume number :
12
Pages :
283-301
Publication date :
2013-02
ISSN :
1535-9484
English keyword(s) :
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
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
Mécanismes moléculaires de la N-glycosylation et pathologies associées
Submission date :
2020-02-12T15:12:10Z
2021-03-04T13:49:58Z
2021-03-04T13:49:58Z
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