|Alteration of the serum N-glycome of mice locally exposed to high doses of ionizing radiation.|
|PMID: 23146835 Owner: NLM Status: MEDLINE|
|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.|
|Thibault Chaze; Marie-Christine Slomianny; Fabien Milliat; Georges Tarlet; Tony Lefebvre-Darroman; Patrick Gourmelon; Eric Bey; Marc Benderitter; Jean-Claude Michalski; Olivier Guipaud|
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|Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-11-12|
|Title: Molecular & cellular proteomics : MCP Volume: 12 ISSN: 1535-9484 ISO Abbreviation: Mol. Cell Proteomics Publication Date: 2013 Feb|
|Created Date: 2013-02-06 Completed Date: 2013-07-11 Revised Date: 2014-02-04|
Medline Journal Info:
|Nlm Unique ID: 101125647 Medline TA: Mol Cell Proteomics Country: United States|
|Languages: eng Pagination: 283-301 Citation Subset: IM|
|APA/MLA Format Download EndNote Download BibTex|
Blood Proteins / chemistry, genetics, metabolism*
Burns / blood*, etiology, genetics
Electrophoresis, Gel, Two-Dimensional
Gamma Rays / adverse effects
Gene Expression Regulation
Interleukin-1beta / blood
Interleukin-6 / blood
Liver / metabolism, radiation effects*
Mice, Inbred BALB C
Molecular Sequence Data
Polysaccharides / blood*, chemistry
Principal Component Analysis
Protein Processing, Post-Translational*
Radiation Injuries, Experimental / blood*, etiology, genetics
Skin / metabolism, radiation effects*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tumor Necrosis Factor-alpha / blood
|0/Blood Proteins; 0/Interleukin-1beta; 0/Interleukin-6; 0/Polysaccharides; 0/Tumor Necrosis Factor-alpha|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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