Glutathione--functions and metabolism in the malarial parasite Plasmodium falciparum.
Identifieur interne : 000F32 ( Main/Exploration ); précédent : 000F31; suivant : 000F33Glutathione--functions and metabolism in the malarial parasite Plasmodium falciparum.
Auteurs : Katja Becker [Allemagne] ; Stefan Rahlfs ; Christine Nickel ; R Heiner SchirmerSource :
- Biological chemistry [ 1431-6730 ] ; 2003.
Descripteurs français
- KwdFr :
- Algorithmes (MeSH), Animaux (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathion (biosynthèse), Glutathion (métabolisme), Glutathion (physiologie), Glutathione peroxidase (métabolisme), Glutathione transferase (métabolisme), Humains (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Paludisme à Plasmodium falciparum (métabolisme), Paludisme à Plasmodium falciparum (psychologie), Paludisme à Plasmodium falciparum (sang), Plasmodium falciparum (métabolisme), Protéines (métabolisme), Séquence d'acides aminés (MeSH), Voie des pentoses phosphates (physiologie), Érythrocytes (métabolisme), Érythrocytes (parasitologie).
- MESH :
- biosynthèse : Glutathion.
- métabolisme : Glutathion, Glutathione peroxidase, Glutathione transferase, Paludisme à Plasmodium falciparum, Plasmodium falciparum, Protéines, Érythrocytes.
- parasitologie : Érythrocytes.
- physiologie : Glutathion, Voie des pentoses phosphates.
- psychologie : Paludisme à Plasmodium falciparum.
- sang : Paludisme à Plasmodium falciparum.
- Algorithmes, Animaux, Données de séquences moléculaires, Glutarédoxines, Humains, Oxidoreductases, Oxydoréduction, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Algorithms (MeSH), Amino Acid Sequence (MeSH), Animals (MeSH), Erythrocytes (metabolism), Erythrocytes (parasitology), Glutaredoxins (MeSH), Glutathione (biosynthesis), Glutathione (metabolism), Glutathione (physiology), Glutathione Peroxidase (metabolism), Glutathione Transferase (metabolism), Humans (MeSH), Malaria, Falciparum (blood), Malaria, Falciparum (metabolism), Malaria, Falciparum (psychology), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Pentose Phosphate Pathway (physiology), Plasmodium falciparum (metabolism), Proteins (metabolism).
- MESH :
- chemical , biosynthesis : Glutathione.
- chemical , metabolism : Glutathione, Glutathione Peroxidase, Glutathione Transferase, Proteins.
- chemical , physiology : Glutathione.
- chemical : Glutaredoxins, Oxidoreductases.
- blood : Malaria, Falciparum.
- metabolism : Erythrocytes, Malaria, Falciparum, Plasmodium falciparum.
- parasitology : Erythrocytes.
- physiology : Pentose Phosphate Pathway.
- psychology : Malaria, Falciparum.
- Algorithms, Amino Acid Sequence, Animals, Humans, Molecular Sequence Data, Oxidation-Reduction.
Abstract
When present as a trophozoite in human erythrocytes, the malarial parasite Plasmodium falciparum exhibits an intense glutathione metabolism. Glutathione plays a role not only in antioxidative defense and in maintaining the reducing environment of the cytosol. Many of the known glutathione-dependent processes are directly related to the specific lifestyle of the parasite. Reduced glutathione (GSH) supports rapid cell growth by providing electrons for deoxyribonucleotide synthesis and it takes part in detoxifying heme, a product of hemoglobin digestion. Free radicals generated in the parasite can be scavenged in reaction sequences involving the thiyl radical GS* as well as the thiolate GS-. As a substrate of glutathione S-transferase, glutathione is conjugated to non-degradable compounds including antimalarial drugs. Furthermore, it is the coenzyme of the glyoxalase system which detoxifies methylglyoxal, a byproduct of the intense glycolysis taking place in the trophozoite. Proteins involved in GSH-dependent processes include glutathione reductase, glutaredoxins, glyoxalase I and II, glutathione S-transferases, and thioredoxins. These proteins, as well as the ATP-dependent enzymes of glutathione synthesis, are studied as factors in the pathophysiology of malaria but also as potential drug targets. Methylene blue, an inhibitor of the structurally known P. falciparum glutathione reductase, appears to be a promising antimalarial medication when given in combination with chloroquine.
DOI: 10.1515/BC.2003.063
PubMed: 12751785
Affiliations:
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Glutathione plays a role not only in antioxidative defense and in maintaining the reducing environment of the cytosol. Many of the known glutathione-dependent processes are directly related to the specific lifestyle of the parasite. Reduced glutathione (GSH) supports rapid cell growth by providing electrons for deoxyribonucleotide synthesis and it takes part in detoxifying heme, a product of hemoglobin digestion. Free radicals generated in the parasite can be scavenged in reaction sequences involving the thiyl radical GS* as well as the thiolate GS-. As a substrate of glutathione S-transferase, glutathione is conjugated to non-degradable compounds including antimalarial drugs. Furthermore, it is the coenzyme of the glyoxalase system which detoxifies methylglyoxal, a byproduct of the intense glycolysis taking place in the trophozoite. Proteins involved in GSH-dependent processes include glutathione reductase, glutaredoxins, glyoxalase I and II, glutathione S-transferases, and thioredoxins. These proteins, as well as the ATP-dependent enzymes of glutathione synthesis, are studied as factors in the pathophysiology of malaria but also as potential drug targets. Methylene blue, an inhibitor of the structurally known P. falciparum glutathione reductase, appears to be a promising antimalarial medication when given in combination with chloroquine.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12751785</PMID><DateCompleted><Year>2003</Year><Month>12</Month><Day>04</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1431-6730</ISSN><JournalIssue CitedMedium="Print"><Volume>384</Volume><Issue>4</Issue><PubDate><Year>2003</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Biological chemistry</Title><ISOAbbreviation>Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Glutathione--functions and metabolism in the malarial parasite Plasmodium falciparum.</ArticleTitle><Pagination><MedlinePgn>551-66</MedlinePgn></Pagination><Abstract><AbstractText>When present as a trophozoite in human erythrocytes, the malarial parasite Plasmodium falciparum exhibits an intense glutathione metabolism. Glutathione plays a role not only in antioxidative defense and in maintaining the reducing environment of the cytosol. Many of the known glutathione-dependent processes are directly related to the specific lifestyle of the parasite. Reduced glutathione (GSH) supports rapid cell growth by providing electrons for deoxyribonucleotide synthesis and it takes part in detoxifying heme, a product of hemoglobin digestion. Free radicals generated in the parasite can be scavenged in reaction sequences involving the thiyl radical GS* as well as the thiolate GS-. As a substrate of glutathione S-transferase, glutathione is conjugated to non-degradable compounds including antimalarial drugs. Furthermore, it is the coenzyme of the glyoxalase system which detoxifies methylglyoxal, a byproduct of the intense glycolysis taking place in the trophozoite. Proteins involved in GSH-dependent processes include glutathione reductase, glutaredoxins, glyoxalase I and II, glutathione S-transferases, and thioredoxins. These proteins, as well as the ATP-dependent enzymes of glutathione synthesis, are studied as factors in the pathophysiology of malaria but also as potential drug targets. Methylene blue, an inhibitor of the structurally known P. falciparum glutathione reductase, appears to be a promising antimalarial medication when given in combination with chloroquine.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Katja</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Interdisciplinary Research Center, Justus-Liebig-University, D-35392 Giessen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rahlfs</LastName><ForeName>Stefan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Nickel</LastName><ForeName>Christine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Schirmer</LastName><ForeName>R Heiner</ForeName><Initials>RH</Initials></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></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biol Chem</MedlineTA><NlmUniqueID>9700112</NlmUniqueID><ISSNLinking>1431-6730</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000465" MajorTopicYN="N">Algorithms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016778" MajorTopicYN="N">Malaria, Falciparum</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000523" MajorTopicYN="N">psychology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010427" MajorTopicYN="N">Pentose Phosphate Pathway</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>145</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>5</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>12</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>5</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12751785</ArticleId><ArticleId IdType="doi">10.1515/BC.2003.063</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Nickel, Christine" sort="Nickel, Christine" uniqKey="Nickel C" first="Christine" last="Nickel">Christine Nickel</name><name sortKey="Rahlfs, Stefan" sort="Rahlfs, Stefan" uniqKey="Rahlfs S" first="Stefan" last="Rahlfs">Stefan Rahlfs</name><name sortKey="Schirmer, R Heiner" sort="Schirmer, R Heiner" uniqKey="Schirmer R" first="R Heiner" last="Schirmer">R Heiner Schirmer</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Becker, Katja" sort="Becker, Katja" uniqKey="Becker K" first="Katja" last="Becker">Katja Becker</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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