Redox and antioxidant systems of the malaria parasite Plasmodium falciparum.
Identifieur interne : 000E58 ( Main/Exploration ); précédent : 000E57; suivant : 000E59Redox and antioxidant systems of the malaria parasite Plasmodium falciparum.
Auteurs : Sylke Müller [Royaume-Uni]Source :
- Molecular microbiology [ 0950-382X ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Antioxydants (métabolisme), Espèces réactives de l'oxygène (métabolisme), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Humains (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Plasmodium falciparum (composition chimique), Plasmodium falciparum (métabolisme), Plasmodium falciparum (physiologie), Protéines de protozoaire (composition chimique), Protéines de protozoaire (génétique), Protéines de protozoaire (métabolisme), Stress oxydatif (MeSH), Superoxide dismutase (métabolisme), Thioredoxin-disulfide reductase (composition chimique), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme), Érythrocytes (composition chimique), Érythrocytes (microbiologie), Érythrocytes (métabolisme).
- MESH :
- composition chimique : Glutathion, Oxidoreductases, Peroxidases, Plasmodium falciparum, Protéines de protozoaire, Thioredoxin-disulfide reductase, Thiorédoxines, Érythrocytes.
- génétique : Protéines de protozoaire.
- microbiologie : Érythrocytes.
- métabolisme : Antioxydants, Espèces réactives de l'oxygène, Glutathion, Oxidoreductases, Peroxidases, Plasmodium falciparum, Protéines de protozoaire, Superoxide dismutase, Thioredoxin-disulfide reductase, Thiorédoxines, Érythrocytes.
- physiologie : Plasmodium falciparum.
- Animaux, Glutarédoxines, Humains, Oxydoréduction, Peroxirédoxines, Stress oxydatif.
English descriptors
- KwdEn :
- Animals (MeSH), Antioxidants (metabolism), Erythrocytes (chemistry), Erythrocytes (metabolism), Erythrocytes (microbiology), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione (metabolism), Humans (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Peroxidases (chemistry), Peroxidases (metabolism), Peroxiredoxins (MeSH), Plasmodium falciparum (chemistry), Plasmodium falciparum (metabolism), Plasmodium falciparum (physiology), Protozoan Proteins (chemistry), Protozoan Proteins (genetics), Protozoan Proteins (metabolism), Reactive Oxygen Species (metabolism), Superoxide Dismutase (metabolism), Thioredoxin-Disulfide Reductase (chemistry), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Glutathione, Oxidoreductases, Peroxidases, Protozoan Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , genetics : Protozoan Proteins.
- chemical , metabolism : Antioxidants, Glutathione, Oxidoreductases, Peroxidases, Protozoan Proteins, Reactive Oxygen Species, Superoxide Dismutase, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemistry : Erythrocytes, Plasmodium falciparum.
- metabolism : Erythrocytes, Plasmodium falciparum.
- microbiology : Erythrocytes.
- physiology : Plasmodium falciparum.
- Animals, Glutaredoxins, Humans, Oxidation-Reduction, Oxidative Stress, Peroxiredoxins.
Abstract
The malaria parasite Plasmodium falciparum is highly adapted to cope with the oxidative stress to which it is exposed during the erythrocytic stages of its life cycle. This includes the defence against oxidative insults arising from the parasite's metabolism of haemoglobin which results in the formation of reactive oxygen species and the release of toxic ferriprotoporphyrin IX. Central to the parasite's defences are superoxide dismutases and thioredoxin-dependent peroxidases; however, they lack catalase and glutathione peroxidases. The vital importance of the thioredoxin redox cycle (comprising NADPH, thioredoxin reductase and thioredoxin) is emphasized by the confirmation that thioredoxin reductase is essential for the survival of intraerythrocytic P. falciparum. The parasites also contain a fully functional glutathione redox system and the low-molecular-weight thiol glutathione is not only an important intracellular thiol redox buffer but also a cofactor for several redox active enzymes such as glutathione S-transferase and glutaredoxin. Recent findings have shown that in addition to these cytosolic redox systems the parasite also has an important mitochondrial antioxidant defence system and it is suggested that lipoic acid plays a pivotal part in defending the organelle from oxidative damage.
DOI: 10.1111/j.1365-2958.2004.04257.x
PubMed: 15387810
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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This includes the defence against oxidative insults arising from the parasite's metabolism of haemoglobin which results in the formation of reactive oxygen species and the release of toxic ferriprotoporphyrin IX. Central to the parasite's defences are superoxide dismutases and thioredoxin-dependent peroxidases; however, they lack catalase and glutathione peroxidases. The vital importance of the thioredoxin redox cycle (comprising NADPH, thioredoxin reductase and thioredoxin) is emphasized by the confirmation that thioredoxin reductase is essential for the survival of intraerythrocytic P. falciparum. The parasites also contain a fully functional glutathione redox system and the low-molecular-weight thiol glutathione is not only an important intracellular thiol redox buffer but also a cofactor for several redox active enzymes such as glutathione S-transferase and glutaredoxin. Recent findings have shown that in addition to these cytosolic redox systems the parasite also has an important mitochondrial antioxidant defence system and it is suggested that lipoic acid plays a pivotal part in defending the organelle from oxidative damage.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15387810</PMID><DateCompleted><Year>2005</Year><Month>01</Month><Day>24</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0950-382X</ISSN><JournalIssue CitedMedium="Print"><Volume>53</Volume><Issue>5</Issue><PubDate><Year>2004</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Molecular microbiology</Title><ISOAbbreviation>Mol Microbiol</ISOAbbreviation></Journal><ArticleTitle>Redox and antioxidant systems of the malaria parasite Plasmodium falciparum.</ArticleTitle><Pagination><MedlinePgn>1291-305</MedlinePgn></Pagination><Abstract><AbstractText>The malaria parasite Plasmodium falciparum is highly adapted to cope with the oxidative stress to which it is exposed during the erythrocytic stages of its life cycle. This includes the defence against oxidative insults arising from the parasite's metabolism of haemoglobin which results in the formation of reactive oxygen species and the release of toxic ferriprotoporphyrin IX. Central to the parasite's defences are superoxide dismutases and thioredoxin-dependent peroxidases; however, they lack catalase and glutathione peroxidases. The vital importance of the thioredoxin redox cycle (comprising NADPH, thioredoxin reductase and thioredoxin) is emphasized by the confirmation that thioredoxin reductase is essential for the survival of intraerythrocytic P. falciparum. The parasites also contain a fully functional glutathione redox system and the low-molecular-weight thiol glutathione is not only an important intracellular thiol redox buffer but also a cofactor for several redox active enzymes such as glutathione S-transferase and glutaredoxin. Recent findings have shown that in addition to these cytosolic redox systems the parasite also has an important mitochondrial antioxidant defence system and it is suggested that lipoic acid plays a pivotal part in defending the organelle from oxidative damage.</AbstractText><CopyrightInformation>Copyright 2004 Blackwell Publishing Ltd</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Müller</LastName><ForeName>Sylke</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Life Sciences, Wellcome Trust Biocentre, University of Dundee, UK. s.muller@dundee.ac.uk</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol 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MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</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="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013482" MajorTopicYN="N">Superoxide Dismutase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>144</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>9</Month><Day>25</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>1</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>9</Month><Day>25</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15387810</ArticleId><ArticleId IdType="doi">10.1111/j.1365-2958.2004.04257.x</ArticleId><ArticleId IdType="pii">MMI4257</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Muller, Sylke" sort="Muller, Sylke" uniqKey="Muller S" first="Sylke" last="Müller">Sylke Müller</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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