Identification and characterization of heme-interacting proteins in the malaria parasite, Plasmodium falciparum.
Identifieur interne : 000F30 ( Main/Exploration ); précédent : 000F29; suivant : 000F31Identification and characterization of heme-interacting proteins in the malaria parasite, Plasmodium falciparum.
Auteurs : Naomi Campanale [Australie] ; Christine Nickel ; Claudia A. Daubenberger ; Dean A. Wehlan ; Jeff J. Gorman ; Nectarios Klonis ; Katja Becker ; Leann TilleySource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- Agarose (pharmacologie), Animaux (MeSH), Cinétique (MeSH), Facteurs temps (MeSH), Glutarédoxines (MeSH), Glutathione reductase (métabolisme), Humains (MeSH), Hème (composition chimique), Liaison aux protéines (MeSH), Modèles biologiques (MeSH), Oxidoreductases (MeSH), Peptides (composition chimique), Plasmodium falciparum (métabolisme), Protéines (métabolisme), Protéines fongiques (métabolisme), Protéines recombinantes (métabolisme), Relation dose-effet des médicaments (MeSH), Spectrométrie de masse (MeSH), Spectrométrie de masse MALDI (MeSH), Stress oxydatif (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme), Trypsine (pharmacologie), Voie des pentoses phosphates (MeSH), Érythrocytes (métabolisme).
- MESH :
- composition chimique : Hème, Peptides.
- métabolisme : Glutathione reductase, Plasmodium falciparum, Protéines, Protéines fongiques, Protéines recombinantes, Thioredoxin-disulfide reductase, Thiorédoxines, Érythrocytes.
- pharmacologie : Agarose, Trypsine.
- Animaux, Cinétique, Facteurs temps, Glutarédoxines, Humains, Liaison aux protéines, Modèles biologiques, Oxidoreductases, Relation dose-effet des médicaments, Spectrométrie de masse, Spectrométrie de masse MALDI, Stress oxydatif, Voie des pentoses phosphates.
English descriptors
- KwdEn :
- Animals (MeSH), Dose-Response Relationship, Drug (MeSH), Erythrocytes (metabolism), Fungal Proteins (metabolism), Glutaredoxins (MeSH), Glutathione Reductase (metabolism), Heme (chemistry), Humans (MeSH), Kinetics (MeSH), Mass Spectrometry (MeSH), Models, Biological (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Pentose Phosphate Pathway (MeSH), Peptides (chemistry), Plasmodium falciparum (metabolism), Protein Binding (MeSH), Proteins (metabolism), Recombinant Proteins (metabolism), Sepharose (pharmacology), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism), Time Factors (MeSH), Trypsin (pharmacology).
- MESH :
- chemical , chemistry : Heme, Peptides.
- chemical , metabolism : Fungal Proteins, Glutathione Reductase, Proteins, Recombinant Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- metabolism : Erythrocytes, Plasmodium falciparum.
- chemical , pharmacology : Sepharose, Trypsin.
- Animals, Dose-Response Relationship, Drug, Glutaredoxins, Humans, Kinetics, Mass Spectrometry, Models, Biological, Oxidative Stress, Oxidoreductases, Pentose Phosphate Pathway, Protein Binding, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Time Factors.
Abstract
The degradation of hemoglobin by the malaria parasite, Plasmodium falciparum, produces free ferriprotoporphyrin IX (FP) as a toxic by-product. In the presence of FP-binding drugs such as chloroquine, FP detoxification is inhibited, and the build-up of free FP is thought to be a key mechanism in parasite killing. In an effort to identify parasite proteins that might interact preferentially with FP, we have used a mass spectrometry approach. Proteins that bind to FP immobilized on agarose include P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH), P. falciparum glutathione reductase (PfGR), and P. falciparum protein disulfide isomerase. To examine the potential consequences of FP binding, we have examined the ability of FP to inhibit the activities of GAPDH and GR from P. falciparum and other sources. FP inhibits the enzymic activity of PfGAPDH with a Ki value of 0.2 microm, whereas red blood cell GAPDH is much less sensitive. By contrast, PfGR is more resistant to FP inhibition (Ki > 25 microm) than its human counterpart. We also examined the ability of FP to inhibit the activities of the additional antioxidant enzymes, P. falciparum thioredoxin reductase, which exhibits a Ki value of 1 microm, and P. falciparum glutaredoxin, which shows more moderate sensitivity to FP. The exquisite sensitivity of PfGAPDH to FP may indicate that the glycolytic pathway of the parasite is particularly susceptible to modulation by FP stress. Inhibition of this pathway may drive flux through the pentose phosphate pathway ensuring sufficient production of reducing equivalents to counteract the oxidative stress induced by FP build-up.
DOI: 10.1074/jbc.M303634200
PubMed: 12748176
Affiliations:
Links toward previous steps (curation, corpus...)
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(chemistry)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Mass Spectrometry (MeSH)</term><term>Models, Biological (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Pentose Phosphate Pathway (MeSH)</term><term>Peptides (chemistry)</term><term>Plasmodium falciparum (metabolism)</term><term>Protein Binding (MeSH)</term><term>Proteins (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Sepharose (pharmacology)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (metabolism)</term><term>Time Factors (MeSH)</term><term>Trypsin (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agarose (pharmacologie)</term><term>Animaux (MeSH)</term><term>Cinétique (MeSH)</term><term>Facteurs temps (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathione reductase (métabolisme)</term><term>Humains (MeSH)</term><term>Hème (composition chimique)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Peptides (composition chimique)</term><term>Plasmodium falciparum (métabolisme)</term><term>Protéines (métabolisme)</term><term>Protéines fongiques (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Spectrométrie de masse (MeSH)</term><term>Spectrométrie de masse MALDI (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (métabolisme)</term><term>Trypsine (pharmacologie)</term><term>Voie des pentoses phosphates (MeSH)</term><term>Érythrocytes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Heme</term><term>Peptides</term></keywords><keywords scheme="MESH" 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phosphates</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The degradation of hemoglobin by the malaria parasite, Plasmodium falciparum, produces free ferriprotoporphyrin IX (FP) as a toxic by-product. In the presence of FP-binding drugs such as chloroquine, FP detoxification is inhibited, and the build-up of free FP is thought to be a key mechanism in parasite killing. In an effort to identify parasite proteins that might interact preferentially with FP, we have used a mass spectrometry approach. Proteins that bind to FP immobilized on agarose include P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH), P. falciparum glutathione reductase (PfGR), and P. falciparum protein disulfide isomerase. To examine the potential consequences of FP binding, we have examined the ability of FP to inhibit the activities of GAPDH and GR from P. falciparum and other sources. FP inhibits the enzymic activity of PfGAPDH with a Ki value of 0.2 microm, whereas red blood cell GAPDH is much less sensitive. By contrast, PfGR is more resistant to FP inhibition (Ki > 25 microm) than its human counterpart. We also examined the ability of FP to inhibit the activities of the additional antioxidant enzymes, P. falciparum thioredoxin reductase, which exhibits a Ki value of 1 microm, and P. falciparum glutaredoxin, which shows more moderate sensitivity to FP. The exquisite sensitivity of PfGAPDH to FP may indicate that the glycolytic pathway of the parasite is particularly susceptible to modulation by FP stress. Inhibition of this pathway may drive flux through the pentose phosphate pathway ensuring sufficient production of reducing equivalents to counteract the oxidative stress induced by FP build-up.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12748176</PMID><DateCompleted><Year>2003</Year><Month>08</Month><Day>26</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>278</Volume><Issue>30</Issue><PubDate><Year>2003</Year><Month>Jul</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Identification and characterization of heme-interacting proteins in the malaria parasite, Plasmodium falciparum.</ArticleTitle><Pagination><MedlinePgn>27354-61</MedlinePgn></Pagination><Abstract><AbstractText>The degradation of hemoglobin by the malaria parasite, Plasmodium falciparum, produces free ferriprotoporphyrin IX (FP) as a toxic by-product. In the presence of FP-binding drugs such as chloroquine, FP detoxification is inhibited, and the build-up of free FP is thought to be a key mechanism in parasite killing. In an effort to identify parasite proteins that might interact preferentially with FP, we have used a mass spectrometry approach. Proteins that bind to FP immobilized on agarose include P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH), P. falciparum glutathione reductase (PfGR), and P. falciparum protein disulfide isomerase. To examine the potential consequences of FP binding, we have examined the ability of FP to inhibit the activities of GAPDH and GR from P. falciparum and other sources. FP inhibits the enzymic activity of PfGAPDH with a Ki value of 0.2 microm, whereas red blood cell GAPDH is much less sensitive. By contrast, PfGR is more resistant to FP inhibition (Ki > 25 microm) than its human counterpart. We also examined the ability of FP to inhibit the activities of the additional antioxidant enzymes, P. falciparum thioredoxin reductase, which exhibits a Ki value of 1 microm, and P. falciparum glutaredoxin, which shows more moderate sensitivity to FP. The exquisite sensitivity of PfGAPDH to FP may indicate that the glycolytic pathway of the parasite is particularly susceptible to modulation by FP stress. Inhibition of this pathway may drive flux through the pentose phosphate pathway ensuring sufficient production of reducing equivalents to counteract the oxidative stress induced by FP build-up.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Campanale</LastName><ForeName>Naomi</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Co-operative Research Centre for Diagnostics, La Trobe University, Melbourne 3086, Victoria, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nickel</LastName><ForeName>Christine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Daubenberger</LastName><ForeName>Claudia A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Wehlan</LastName><ForeName>Dean A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Gorman</LastName><ForeName>Jeff J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Klonis</LastName><ForeName>Nectarios</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Katja</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Tilley</LastName><ForeName>Leann</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9012-36-6</RegistryNumber><NameOfSubstance UI="D012685">Sepharose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005980" MajorTopicYN="N">Glutathione Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010427" MajorTopicYN="N">Pentose Phosphate Pathway</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012685" MajorTopicYN="N">Sepharose</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</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="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName><QualifierName 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sortKey="Daubenberger, Claudia A" sort="Daubenberger, Claudia A" uniqKey="Daubenberger C" first="Claudia A" last="Daubenberger">Claudia A. Daubenberger</name><name sortKey="Gorman, Jeff J" sort="Gorman, Jeff J" uniqKey="Gorman J" first="Jeff J" last="Gorman">Jeff J. Gorman</name><name sortKey="Klonis, Nectarios" sort="Klonis, Nectarios" uniqKey="Klonis N" first="Nectarios" last="Klonis">Nectarios Klonis</name><name sortKey="Nickel, Christine" sort="Nickel, Christine" uniqKey="Nickel C" first="Christine" last="Nickel">Christine Nickel</name><name sortKey="Tilley, Leann" sort="Tilley, Leann" uniqKey="Tilley L" first="Leann" last="Tilley">Leann Tilley</name><name sortKey="Wehlan, Dean A" sort="Wehlan, Dean A" uniqKey="Wehlan D" first="Dean A" last="Wehlan">Dean A. Wehlan</name></noCountry><country name="Australie"><noRegion><name sortKey="Campanale, Naomi" sort="Campanale, Naomi" uniqKey="Campanale N" first="Naomi" last="Campanale">Naomi Campanale</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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