Redox regulation of protein damage in plasma.
Identifieur interne : 000614 ( Main/Exploration ); précédent : 000613; suivant : 000615Redox regulation of protein damage in plasma.
Auteurs : Helen R. Griffiths [Royaume-Uni] ; Irundika H K. Dias [Royaume-Uni] ; Rachel S. Willetts [Royaume-Uni] ; Andrew Devitt [Royaume-Uni]Source :
- Redox biology [ 2213-2317 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules de Küpffer (physiologie), Espèces réactives de l'azote (métabolisme), Espèces réactives de l'oxygène (métabolisme), Glycosylation (MeSH), Humains (MeSH), Isoformes de protéines (métabolisme), Lipoxygenase (métabolisme), Maturation post-traductionnelle des protéines (MeSH), Myeloperoxidase (métabolisme), NADPH oxidase (MeSH), Nitric oxide synthase (métabolisme), Nitrosation (MeSH), Oxidoreductases (sang), Oxydoréduction (MeSH), Peroxirédoxines (métabolisme), Protéines du sang (métabolisme), Réticulum endoplasmique (MeSH), Stress oxydatif (MeSH), Thiorédoxines (métabolisme), Vieillissement (sang), Xanthine oxidase (métabolisme).
- MESH :
- métabolisme : Espèces réactives de l'azote, Espèces réactives de l'oxygène, Isoformes de protéines, Lipoxygenase, Myeloperoxidase, Nitric oxide synthase, Peroxirédoxines, Protéines du sang, Thiorédoxines, Xanthine oxidase.
- physiologie : Cellules de Küpffer.
- sang : Oxidoreductases, Vieillissement.
- Animaux, Glycosylation, Humains, Maturation post-traductionnelle des protéines, NADPH oxidase, Nitrosation, Oxydoréduction, Réticulum endoplasmique, Stress oxydatif.
English descriptors
- KwdEn :
- Aging (blood), Animals (MeSH), Blood Proteins (metabolism), Endoplasmic Reticulum (MeSH), Glycosylation (MeSH), Humans (MeSH), Kupffer Cells (physiology), Lipoxygenase (metabolism), NADPH Oxidases (MeSH), Nitric Oxide Synthase (metabolism), Nitrosation (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (blood), Peroxidase (metabolism), Peroxiredoxins (metabolism), Protein Isoforms (metabolism), Protein Processing, Post-Translational (MeSH), Reactive Nitrogen Species (metabolism), Reactive Oxygen Species (metabolism), Thioredoxins (metabolism), Xanthine Oxidase (metabolism).
- MESH :
- chemical , blood : Oxidoreductases.
- chemical , metabolism : Blood Proteins, Lipoxygenase, Nitric Oxide Synthase, Peroxidase, Peroxiredoxins, Protein Isoforms, Reactive Nitrogen Species, Reactive Oxygen Species, Thioredoxins, Xanthine Oxidase.
- blood : Aging.
- physiology : Kupffer Cells.
- Animals, Endoplasmic Reticulum, Glycosylation, Humans, NADPH Oxidases, Nitrosation, Oxidation-Reduction, Oxidative Stress, Protein Processing, Post-Translational.
Abstract
The presence and concentrations of modified proteins circulating in plasma depend on rates of protein synthesis, modification and clearance. In early studies, the proteins most frequently analysed for damage were those which were more abundant in plasma (e.g. albumin and immunoglobulins) which exist at up to 10 orders of magnitude higher concentrations than other plasma proteins e.g. cytokines. However, advances in analytical techniques using mass spectrometry and immuno-affinity purification methods, have facilitated analysis of less abundant, modified proteins and the nature of modifications at specific sites is now being characterised. The damaging reactive species that cause protein modifications in plasma principally arise from reactive oxygen species (ROS) produced by NADPH oxidases (NOX), nitric oxide synthases (NOS) and oxygenase activities; reactive nitrogen species (RNS) from myeloperoxidase (MPO) and NOS activities; and hypochlorous acid from MPO. Secondary damage to proteins may be caused by oxidized lipids and glucose autooxidation. In this review, we focus on redox regulatory control of those enzymes and processes which control protein maturation during synthesis, produce reactive species, repair and remove damaged plasma proteins. We have highlighted the potential for alterations in the extracellular redox compartment to regulate intracellular redox state and, conversely, for intracellular oxidative stress to alter the cellular secretome and composition of extracellular vesicles. Through secreted, redox-active regulatory molecules, changes in redox state may be transmitted to distant sites.
DOI: 10.1016/j.redox.2014.01.010
PubMed: 24624332
PubMed Central: PMC3949090
Affiliations:
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Le document en format XML
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Post-Translational (MeSH)</term><term>Reactive Nitrogen Species (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>Thioredoxins (metabolism)</term><term>Xanthine Oxidase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules de Küpffer (physiologie)</term><term>Espèces réactives de l'azote (métabolisme)</term><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Glycosylation (MeSH)</term><term>Humains (MeSH)</term><term>Isoformes de protéines (métabolisme)</term><term>Lipoxygenase (métabolisme)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Myeloperoxidase (métabolisme)</term><term>NADPH oxidase (MeSH)</term><term>Nitric oxide synthase (métabolisme)</term><term>Nitrosation (MeSH)</term><term>Oxidoreductases (sang)</term><term>Oxydoréduction (MeSH)</term><term>Peroxirédoxines (métabolisme)</term><term>Protéines du sang (métabolisme)</term><term>Réticulum endoplasmique (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Thiorédoxines (métabolisme)</term><term>Vieillissement (sang)</term><term>Xanthine oxidase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Blood Proteins</term><term>Lipoxygenase</term><term>Nitric Oxide Synthase</term><term>Peroxidase</term><term>Peroxiredoxins</term><term>Protein Isoforms</term><term>Reactive Nitrogen Species</term><term>Reactive Oxygen Species</term><term>Thioredoxins</term><term>Xanthine Oxidase</term></keywords><keywords scheme="MESH" qualifier="blood" xml:lang="en"><term>Aging</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'azote</term><term>Espèces réactives de l'oxygène</term><term>Isoformes de protéines</term><term>Lipoxygenase</term><term>Myeloperoxidase</term><term>Nitric oxide synthase</term><term>Peroxirédoxines</term><term>Protéines du sang</term><term>Thiorédoxines</term><term>Xanthine oxidase</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cellules de Küpffer</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Kupffer Cells</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Oxidoreductases</term><term>Vieillissement</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Endoplasmic Reticulum</term><term>Glycosylation</term><term>Humans</term><term>NADPH Oxidases</term><term>Nitrosation</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Glycosylation</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>NADPH oxidase</term><term>Nitrosation</term><term>Oxydoréduction</term><term>Réticulum endoplasmique</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The presence and concentrations of modified proteins circulating in plasma depend on rates of protein synthesis, modification and clearance. In early studies, the proteins most frequently analysed for damage were those which were more abundant in plasma (e.g. albumin and immunoglobulins) which exist at up to 10 orders of magnitude higher concentrations than other plasma proteins e.g. cytokines. However, advances in analytical techniques using mass spectrometry and immuno-affinity purification methods, have facilitated analysis of less abundant, modified proteins and the nature of modifications at specific sites is now being characterised. The damaging reactive species that cause protein modifications in plasma principally arise from reactive oxygen species (ROS) produced by NADPH oxidases (NOX), nitric oxide synthases (NOS) and oxygenase activities; reactive nitrogen species (RNS) from myeloperoxidase (MPO) and NOS activities; and hypochlorous acid from MPO. Secondary damage to proteins may be caused by oxidized lipids and glucose autooxidation. In this review, we focus on redox regulatory control of those enzymes and processes which control protein maturation during synthesis, produce reactive species, repair and remove damaged plasma proteins. We have highlighted the potential for alterations in the extracellular redox compartment to regulate intracellular redox state and, conversely, for intracellular oxidative stress to alter the cellular secretome and composition of extracellular vesicles. Through secreted, redox-active regulatory molecules, changes in redox state may be transmitted to distant sites. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24624332</PMID><DateCompleted><Year>2015</Year><Month>03</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2213-2317</ISSN><JournalIssue CitedMedium="Print"><Volume>2</Volume><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Redox biology</Title><ISOAbbreviation>Redox Biol</ISOAbbreviation></Journal><ArticleTitle>Redox regulation of protein damage in plasma.</ArticleTitle><Pagination><MedlinePgn>430-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.redox.2014.01.010</ELocationID><Abstract><AbstractText>The presence and concentrations of modified proteins circulating in plasma depend on rates of protein synthesis, modification and clearance. In early studies, the proteins most frequently analysed for damage were those which were more abundant in plasma (e.g. albumin and immunoglobulins) which exist at up to 10 orders of magnitude higher concentrations than other plasma proteins e.g. cytokines. However, advances in analytical techniques using mass spectrometry and immuno-affinity purification methods, have facilitated analysis of less abundant, modified proteins and the nature of modifications at specific sites is now being characterised. The damaging reactive species that cause protein modifications in plasma principally arise from reactive oxygen species (ROS) produced by NADPH oxidases (NOX), nitric oxide synthases (NOS) and oxygenase activities; reactive nitrogen species (RNS) from myeloperoxidase (MPO) and NOS activities; and hypochlorous acid from MPO. Secondary damage to proteins may be caused by oxidized lipids and glucose autooxidation. In this review, we focus on redox regulatory control of those enzymes and processes which control protein maturation during synthesis, produce reactive species, repair and remove damaged plasma proteins. We have highlighted the potential for alterations in the extracellular redox compartment to regulate intracellular redox state and, conversely, for intracellular oxidative stress to alter the cellular secretome and composition of extracellular vesicles. Through secreted, redox-active regulatory molecules, changes in redox state may be transmitted to distant sites. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Griffiths</LastName><ForeName>Helen R</ForeName><Initials>HR</Initials><AffiliationInfo><Affiliation>Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham B4 7ET, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dias</LastName><ForeName>Irundika H K</ForeName><Initials>IH</Initials><AffiliationInfo><Affiliation>Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham B4 7ET, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Willetts</LastName><ForeName>Rachel S</ForeName><Initials>RS</Initials><AffiliationInfo><Affiliation>Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham B4 7ET, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Devitt</LastName><ForeName>Andrew</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Life & Health Sciences and Aston Research Centre for Healthy Ageing, Aston University, Aston Triangle, Birmingham B4 7ET, UK.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>01</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Redox Biol</MedlineTA><NlmUniqueID>101605639</NlmUniqueID><ISSNLinking>2213-2317</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001798">Blood Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026361">Reactive Nitrogen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.11.12</RegistryNumber><NameOfSubstance UI="D008084">Lipoxygenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.13.39</RegistryNumber><NameOfSubstance UI="D019001">Nitric Oxide Synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.17.3.2</RegistryNumber><NameOfSubstance UI="D014969">Xanthine Oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.3.-</RegistryNumber><NameOfSubstance UI="D019255">NADPH Oxidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000375" MajorTopicYN="N">Aging</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001798" MajorTopicYN="N">Blood Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007728" MajorTopicYN="N">Kupffer Cells</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008084" MajorTopicYN="N">Lipoxygenase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019255" MajorTopicYN="N">NADPH Oxidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019001" MajorTopicYN="N">Nitric Oxide Synthase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015538" MajorTopicYN="N">Nitrosation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D026361" MajorTopicYN="N">Reactive Nitrogen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014969" MajorTopicYN="N">Xanthine Oxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Ageing</Keyword><Keyword MajorTopicYN="N">BH4, tetrahydrobiopterin</Keyword><Keyword MajorTopicYN="N">COX, cyclo-oxygenase</Keyword><Keyword MajorTopicYN="N">CRP, C-reactive protein</Keyword><Keyword MajorTopicYN="N">ER, endoplasmic reticulum</Keyword><Keyword MajorTopicYN="N">ERO1, endoplasmic reticulum oxidoreductin 1</Keyword><Keyword MajorTopicYN="N">EV, extracellular vesicles</Keyword><Keyword MajorTopicYN="N">FX1, factor XI</Keyword><Keyword MajorTopicYN="N">GPI, glycoprotein 1</Keyword><Keyword MajorTopicYN="N">GPX, glutathione peroxidase</Keyword><Keyword MajorTopicYN="N">GRX, glutaredoxin</Keyword><Keyword MajorTopicYN="N">GSH, glutathione</Keyword><Keyword MajorTopicYN="N">Glycosylation</Keyword><Keyword MajorTopicYN="N">MIRNA, microRNA</Keyword><Keyword MajorTopicYN="N">MPO, myeloperoxidase</Keyword><Keyword MajorTopicYN="N">NO, nitric oxide</Keyword><Keyword MajorTopicYN="N">NOS, nitric oxide synthase</Keyword><Keyword MajorTopicYN="N">NOX, NADPH oxidase</Keyword><Keyword MajorTopicYN="N">Nitration</Keyword><Keyword MajorTopicYN="N">O2•−, superoxide anion radical</Keyword><Keyword MajorTopicYN="N">ONOO-, peroxynitrite</Keyword><Keyword MajorTopicYN="N">Oxidation</Keyword><Keyword MajorTopicYN="N">PDI, protein disulphide isomerase</Keyword><Keyword MajorTopicYN="N">Peroxiredoxin</Keyword><Keyword MajorTopicYN="N">Prx, peroxiredoxin</Keyword><Keyword MajorTopicYN="N">RNS, reactive nitrogen species</Keyword><Keyword MajorTopicYN="N">ROS, reactive nitrogen species</Keyword><Keyword MajorTopicYN="N">Thioredoxin</Keyword><Keyword MajorTopicYN="N">Trx, thioredoxin</Keyword><Keyword MajorTopicYN="N">VWF, von Willebrand factor</Keyword><Keyword MajorTopicYN="N">XO, xanthine oxidase</Keyword></KeywordList><GeneralNote Owner="NLM">Original DateCompleted: 20140624</GeneralNote></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>12</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>01</Month><Day>11</Day></PubMedPubDate><PubMedPubDate 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