Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress.
Identifieur interne : 000D10 ( Main/Exploration ); précédent : 000D09; suivant : 000D11Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress.
Auteurs : Paola Checconi [Royaume-Uni] ; Sonia Salzano [Royaume-Uni] ; Lucas Bowler [Royaume-Uni] ; Lisa Mullen [Royaume-Uni] ; Manuela Mengozzi [Royaume-Uni] ; Eva-Maria Hanschmann [Allemagne] ; Christopher Horst Lillig [Allemagne] ; Rossella Sgarbanti [Italie] ; Simona Panella [Italie] ; Lucia Nencioni [Italie] ; Anna Teresa Palamara [Italie] ; Pietro Ghezzi [Royaume-Uni]Source :
- PloS one [ 1932-6203 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux, Antioxydants (pharmacologie), Cellules RAW 264.7, Dexaméthasone (pharmacologie), Glutathion (métabolisme), Grippe humaine (), Grippe humaine (anatomopathologie), Grippe humaine (métabolisme), Humains, Inflammation (), Inflammation (anatomopathologie), Inflammation (métabolisme), Lignée cellulaire, Lipopolysaccharides (pharmacologie), Oxydoréduction (), Peroxirédoxines (métabolisme), Profilines (métabolisme), Protéines (métabolisme), Protéomique, Régulation négative (), Souris, Stress oxydatif (), Technique de Western, Thiols (pharmacologie), Thiorédoxines (métabolisme), Vimentine (métabolisme).
- MESH :
- anatomopathologie : Grippe humaine, Inflammation.
- métabolisme : Glutathion, Grippe humaine, Inflammation, Peroxirédoxines, Profilines, Protéines, Thiorédoxines, Vimentine.
- pharmacologie : Antioxydants, Dexaméthasone, Lipopolysaccharides, Thiols.
- Animaux, Cellules RAW 264.7, Grippe humaine, Humains, Inflammation, Lignée cellulaire, Oxydoréduction, Protéomique, Régulation négative, Souris, Stress oxydatif, Technique de Western.
English descriptors
- KwdEn :
- Animals, Antioxidants (pharmacology), Blotting, Western, Cell Line, Dexamethasone (pharmacology), Down-Regulation (drug effects), Glutathione (metabolism), Humans, Inflammation (complications), Inflammation (metabolism), Inflammation (pathology), Influenza, Human (complications), Influenza, Human (metabolism), Influenza, Human (pathology), Lipopolysaccharides (pharmacology), Mice, Oxidation-Reduction (drug effects), Oxidative Stress (drug effects), Peroxiredoxins (metabolism), Profilins (metabolism), Proteins (metabolism), Proteomics, RAW 264.7 Cells, Sulfhydryl Compounds (pharmacology), Thioredoxins (metabolism), Vimentin (metabolism).
- MESH :
- chemical , metabolism : Glutathione, Peroxiredoxins, Profilins, Proteins, Thioredoxins, Vimentin.
- chemical , pharmacology : Antioxidants, Dexamethasone, Lipopolysaccharides, Sulfhydryl Compounds.
- complications : Inflammation, Influenza, Human.
- drug effects : Down-Regulation, Oxidation-Reduction, Oxidative Stress.
- metabolism : Inflammation, Influenza, Human.
- pathology : Inflammation, Influenza, Human.
- Animals, Blotting, Western, Cell Line, Humans, Mice, Proteomics, RAW 264.7 Cells.
Abstract
Protein cysteines can form transient disulfides with glutathione (GSH), resulting in the production of glutathionylated proteins, and this process is regarded as a mechanism by which the redox state of the cell can regulate protein function. Most studies on redox regulation of immunity have focused on intracellular proteins. In this study we have used redox proteomics to identify those proteins released in glutathionylated form by macrophages stimulated with lipopolysaccharide (LPS) after pre-loading the cells with biotinylated GSH. Of the several proteins identified in the redox secretome, we have selected a number for validation. Proteomic analysis indicated that LPS stimulated the release of peroxiredoxin (PRDX) 1, PRDX2, vimentin (VIM), profilin1 (PFN1) and thioredoxin 1 (TXN1). For PRDX1 and TXN1, we were able to confirm that the released protein is glutathionylated. PRDX1, PRDX2 and TXN1 were also released by the human pulmonary epithelial cell line, A549, infected with influenza virus. The release of the proteins identified was inhibited by the anti-inflammatory glucocorticoid, dexamethasone (DEX), which also inhibited tumor necrosis factor (TNF)-α release, and by thiol antioxidants (N-butanoyl GSH derivative, GSH-C4, and N-acetylcysteine (NAC), which did not affect TNF-α production. The proteins identified could be useful as biomarkers of oxidative stress associated with inflammation, and further studies will be required to investigate if the extracellular forms of these proteins has immunoregulatory functions.
DOI: 10.1371/journal.pone.0127086
PubMed: 25985305
Affiliations:
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Le document en format XML
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Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome, Italy; Brighton & Sussex Medical School, Falmer, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute Pasteur, Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome, Italy; Brighton & Sussex Medical School, Falmer, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author><author><name sortKey="Salzano, Sonia" sort="Salzano, Sonia" uniqKey="Salzano S" first="Sonia" last="Salzano">Sonia Salzano</name><affiliation wicri:level="1"><nlm:affiliation>Brighton & Sussex Medical School, Falmer, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Brighton & Sussex Medical School, Falmer, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author><author><name sortKey="Bowler, Lucas" sort="Bowler, Lucas" uniqKey="Bowler L" first="Lucas" last="Bowler">Lucas Bowler</name><affiliation wicri:level="1"><nlm:affiliation>University of Brighton, Pharmacy and Biomolecular Sciences, Moulsecoomb, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>University of Brighton, Pharmacy and Biomolecular Sciences, Moulsecoomb, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author><author><name sortKey="Mullen, Lisa" sort="Mullen, Lisa" uniqKey="Mullen L" first="Lisa" last="Mullen">Lisa Mullen</name><affiliation wicri:level="1"><nlm:affiliation>Brighton & Sussex Medical School, Falmer, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Brighton & Sussex Medical School, Falmer, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author><author><name sortKey="Mengozzi, Manuela" sort="Mengozzi, Manuela" uniqKey="Mengozzi M" first="Manuela" last="Mengozzi">Manuela Mengozzi</name><affiliation wicri:level="1"><nlm:affiliation>Brighton & Sussex Medical School, Falmer, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Brighton & Sussex Medical School, Falmer, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author><author><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, Ernst-Moritz Arndt University, Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine, Ernst-Moritz Arndt University, Greifswald</wicri:regionArea><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Medical Biochemistry and Molecular Biology, University Medicine, Ernst-Moritz Arndt University, Greifswald, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Medical Biochemistry and Molecular Biology, University Medicine, Ernst-Moritz Arndt University, Greifswald</wicri:regionArea><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion></affiliation></author><author><name sortKey="Sgarbanti, Rossella" sort="Sgarbanti, Rossella" uniqKey="Sgarbanti R" first="Rossella" last="Sgarbanti">Rossella Sgarbanti</name><affiliation wicri:level="3"><nlm:affiliation>IRCSS San Raffaele Pisana, Telematic University, Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>IRCSS San Raffaele Pisana, Telematic University, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Panella, Simona" sort="Panella, Simona" uniqKey="Panella S" first="Simona" last="Panella">Simona Panella</name><affiliation wicri:level="3"><nlm:affiliation>IRCSS San Raffaele Pisana, Telematic University, Rome, Italy; Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>IRCSS San Raffaele Pisana, Telematic University, Rome, Italy; Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Nencioni, Lucia" sort="Nencioni, Lucia" uniqKey="Nencioni L" first="Lucia" last="Nencioni">Lucia Nencioni</name><affiliation wicri:level="3"><nlm:affiliation>Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Palamara, Anna Teresa" sort="Palamara, Anna Teresa" uniqKey="Palamara A" first="Anna Teresa" last="Palamara">Anna Teresa Palamara</name><affiliation wicri:level="3"><nlm:affiliation>IRCSS San Raffaele Pisana, Telematic University, Rome, Italy; Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>IRCSS San Raffaele Pisana, Telematic University, Rome, Italy; Department of Public Health and Infectious Diseases, Institute Pasteur Cenci-Bolognetti Foundation, "Sapienza" University of Rome, Rome</wicri:regionArea><placeName><settlement type="city">Rome</settlement><region nuts="2">Latium</region></placeName></affiliation></author><author><name sortKey="Ghezzi, Pietro" sort="Ghezzi, Pietro" uniqKey="Ghezzi P" first="Pietro" last="Ghezzi">Pietro Ghezzi</name><affiliation wicri:level="1"><nlm:affiliation>Brighton & Sussex Medical School, Falmer, Brighton, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Brighton & Sussex Medical School, Falmer, Brighton</wicri:regionArea><wicri:noRegion>Brighton</wicri:noRegion></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antioxidants (pharmacology)</term><term>Blotting, Western</term><term>Cell Line</term><term>Dexamethasone (pharmacology)</term><term>Down-Regulation (drug effects)</term><term>Glutathione (metabolism)</term><term>Humans</term><term>Inflammation (complications)</term><term>Inflammation (metabolism)</term><term>Inflammation (pathology)</term><term>Influenza, Human (complications)</term><term>Influenza, Human (metabolism)</term><term>Influenza, Human (pathology)</term><term>Lipopolysaccharides (pharmacology)</term><term>Mice</term><term>Oxidation-Reduction (drug effects)</term><term>Oxidative Stress (drug effects)</term><term>Peroxiredoxins (metabolism)</term><term>Profilins (metabolism)</term><term>Proteins (metabolism)</term><term>Proteomics</term><term>RAW 264.7 Cells</term><term>Sulfhydryl Compounds (pharmacology)</term><term>Thioredoxins (metabolism)</term><term>Vimentin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antioxydants (pharmacologie)</term><term>Cellules RAW 264.7</term><term>Dexaméthasone (pharmacologie)</term><term>Glutathion (métabolisme)</term><term>Grippe humaine ()</term><term>Grippe humaine (anatomopathologie)</term><term>Grippe humaine (métabolisme)</term><term>Humains</term><term>Inflammation ()</term><term>Inflammation (anatomopathologie)</term><term>Inflammation (métabolisme)</term><term>Lignée cellulaire</term><term>Lipopolysaccharides (pharmacologie)</term><term>Oxydoréduction ()</term><term>Peroxirédoxines (métabolisme)</term><term>Profilines (métabolisme)</term><term>Protéines (métabolisme)</term><term>Protéomique</term><term>Régulation négative ()</term><term>Souris</term><term>Stress oxydatif ()</term><term>Technique de Western</term><term>Thiols (pharmacologie)</term><term>Thiorédoxines (métabolisme)</term><term>Vimentine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Peroxiredoxins</term><term>Profilins</term><term>Proteins</term><term>Thioredoxins</term><term>Vimentin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antioxidants</term><term>Dexamethasone</term><term>Lipopolysaccharides</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Grippe humaine</term><term>Inflammation</term></keywords><keywords scheme="MESH" qualifier="complications" xml:lang="en"><term>Inflammation</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Down-Regulation</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Inflammation</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Grippe humaine</term><term>Inflammation</term><term>Peroxirédoxines</term><term>Profilines</term><term>Protéines</term><term>Thiorédoxines</term><term>Vimentine</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Inflammation</term><term>Influenza, Human</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antioxydants</term><term>Dexaméthasone</term><term>Lipopolysaccharides</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Cell Line</term><term>Humans</term><term>Mice</term><term>Proteomics</term><term>RAW 264.7 Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules RAW 264.7</term><term>Grippe humaine</term><term>Humains</term><term>Inflammation</term><term>Lignée cellulaire</term><term>Oxydoréduction</term><term>Protéomique</term><term>Régulation négative</term><term>Souris</term><term>Stress oxydatif</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein cysteines can form transient disulfides with glutathione (GSH), resulting in the production of glutathionylated proteins, and this process is regarded as a mechanism by which the redox state of the cell can regulate protein function. Most studies on redox regulation of immunity have focused on intracellular proteins. In this study we have used redox proteomics to identify those proteins released in glutathionylated form by macrophages stimulated with lipopolysaccharide (LPS) after pre-loading the cells with biotinylated GSH. Of the several proteins identified in the redox secretome, we have selected a number for validation. Proteomic analysis indicated that LPS stimulated the release of peroxiredoxin (PRDX) 1, PRDX2, vimentin (VIM), profilin1 (PFN1) and thioredoxin 1 (TXN1). For PRDX1 and TXN1, we were able to confirm that the released protein is glutathionylated. PRDX1, PRDX2 and TXN1 were also released by the human pulmonary epithelial cell line, A549, infected with influenza virus. The release of the proteins identified was inhibited by the anti-inflammatory glucocorticoid, dexamethasone (DEX), which also inhibited tumor necrosis factor (TNF)-α release, and by thiol antioxidants (N-butanoyl GSH derivative, GSH-C4, and N-acetylcysteine (NAC), which did not affect TNF-α production. The proteins identified could be useful as biomarkers of oxidative stress associated with inflammation, and further studies will be required to investigate if the extracellular forms of these proteins has immunoregulatory functions. </div></front></TEI><affiliations><list><country><li>Allemagne</li><li>Italie</li><li>Royaume-Uni</li></country><region><li>Latium</li></region><settlement><li>Rome</li></settlement></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Checconi, Paola" sort="Checconi, Paola" uniqKey="Checconi P" first="Paola" last="Checconi">Paola Checconi</name></noRegion><name sortKey="Bowler, Lucas" sort="Bowler, Lucas" uniqKey="Bowler L" first="Lucas" last="Bowler">Lucas Bowler</name><name sortKey="Ghezzi, Pietro" sort="Ghezzi, Pietro" uniqKey="Ghezzi P" first="Pietro" last="Ghezzi">Pietro Ghezzi</name><name sortKey="Mengozzi, Manuela" sort="Mengozzi, Manuela" uniqKey="Mengozzi M" first="Manuela" last="Mengozzi">Manuela Mengozzi</name><name sortKey="Mullen, Lisa" sort="Mullen, Lisa" uniqKey="Mullen L" first="Lisa" last="Mullen">Lisa Mullen</name><name sortKey="Salzano, Sonia" sort="Salzano, Sonia" uniqKey="Salzano S" first="Sonia" last="Salzano">Sonia Salzano</name></country><country name="Allemagne"><noRegion><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name></noRegion><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></country><country name="Italie"><region name="Latium"><name sortKey="Sgarbanti, Rossella" sort="Sgarbanti, Rossella" uniqKey="Sgarbanti R" first="Rossella" last="Sgarbanti">Rossella Sgarbanti</name></region><name sortKey="Nencioni, Lucia" sort="Nencioni, Lucia" uniqKey="Nencioni L" first="Lucia" last="Nencioni">Lucia Nencioni</name><name sortKey="Palamara, Anna Teresa" sort="Palamara, Anna Teresa" uniqKey="Palamara A" first="Anna Teresa" last="Palamara">Anna Teresa Palamara</name><name sortKey="Panella, Simona" sort="Panella, Simona" uniqKey="Panella S" first="Simona" last="Panella">Simona Panella</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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