The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation
Identifieur interne : 000729 ( Istex/Corpus ); précédent : 000728; suivant : 000730The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation
Auteurs : Yumiko Sugioka ; Mamoru SuzukiSource :
- BBA - General Subjects [ 0304-4165 ] ; 1991.
English descriptors
- KwdEn :
- Teeft :
- Acta, Active oxygen species, Apotransferrin, Biochim, Biophys, Catalase, Chloroquine, Complex formation, Food vacuole, Fp1x, Fpix, Hydrogen peroxide, Lipid, Lipid peroxidation, Liposome, Malaria pigment, Mefroquine, Molar, Molar ratio, Nakano, Parasite, Peroxidation, Peroxidative, Peroxidative ability, Peroxidative cleavage, Phospholipid, Phospholipid peroxidation, Primaquine, Quinine, Sodium benzoate, Sugioka, Superoxide, Superoxide anion, Vacuole.
Abstract
Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.
Url:
DOI: 10.1016/0304-4165(91)90032-C
Links to Exploration step
ISTEX:C1E79E9C3DD9773BD334C21651DDE7C83298DE1ALe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title><author><name sortKey="Sugioka, Yumiko" sort="Sugioka, Yumiko" uniqKey="Sugioka Y" first="Yumiko" last="Sugioka">Yumiko Sugioka</name><affiliation><mods:affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</mods:affiliation></affiliation></author><author><name sortKey="Suzuki, Mamoru" sort="Suzuki, Mamoru" uniqKey="Suzuki M" first="Mamoru" last="Suzuki">Mamoru Suzuki</name><affiliation><mods:affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:C1E79E9C3DD9773BD334C21651DDE7C83298DE1A</idno><date when="1991" year="1991">1991</date><idno type="doi">10.1016/0304-4165(91)90032-C</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">000729</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000729</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title><author><name sortKey="Sugioka, Yumiko" sort="Sugioka, Yumiko" uniqKey="Sugioka Y" first="Yumiko" last="Sugioka">Yumiko Sugioka</name><affiliation><mods:affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</mods:affiliation></affiliation></author><author><name sortKey="Suzuki, Mamoru" sort="Suzuki, Mamoru" uniqKey="Suzuki M" first="Mamoru" last="Suzuki">Mamoru Suzuki</name><affiliation><mods:affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">BBA - General Subjects</title><title level="j" type="abbrev">BBAGEN</title><idno type="ISSN">0304-4165</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">1074</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="19">19</biblScope><biblScope unit="page" to="24">24</biblScope></imprint><idno type="ISSN">0304-4165</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0304-4165</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antimalaria</term><term>Chloroquine</term><term>FPIX</term><term>Ferriprotoporphyrin IX</term><term>Lipid peroxidation</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Acta</term><term>Active oxygen species</term><term>Apotransferrin</term><term>Biochim</term><term>Biophys</term><term>Catalase</term><term>Chloroquine</term><term>Complex formation</term><term>Food vacuole</term><term>Fp1x</term><term>Fpix</term><term>Hydrogen peroxide</term><term>Lipid</term><term>Lipid peroxidation</term><term>Liposome</term><term>Malaria pigment</term><term>Mefroquine</term><term>Molar</term><term>Molar ratio</term><term>Nakano</term><term>Parasite</term><term>Peroxidation</term><term>Peroxidative</term><term>Peroxidative ability</term><term>Peroxidative cleavage</term><term>Phospholipid</term><term>Phospholipid peroxidation</term><term>Primaquine</term><term>Quinine</term><term>Sodium benzoate</term><term>Sugioka</term><term>Superoxide</term><term>Superoxide anion</term><term>Vacuole</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.</div></front></TEI><istex><corpusName>elsevier</corpusName><keywords><teeft><json:string>fpix</json:string><json:string>lipid</json:string><json:string>peroxidation</json:string><json:string>lipid peroxidation</json:string><json:string>chloroquine</json:string><json:string>phospholipid</json:string><json:string>mefroquine</json:string><json:string>quinine</json:string><json:string>vacuole</json:string><json:string>primaquine</json:string><json:string>peroxidative</json:string><json:string>complex formation</json:string><json:string>liposome</json:string><json:string>superoxide</json:string><json:string>fp1x</json:string><json:string>apotransferrin</json:string><json:string>biophys</json:string><json:string>acta</json:string><json:string>catalase</json:string><json:string>sugioka</json:string><json:string>nakano</json:string><json:string>biochim</json:string><json:string>parasite</json:string><json:string>molar ratio</json:string><json:string>food vacuole</json:string><json:string>sodium benzoate</json:string><json:string>molar</json:string><json:string>hydrogen peroxide</json:string><json:string>peroxidative cleavage</json:string><json:string>malaria pigment</json:string><json:string>phospholipid peroxidation</json:string><json:string>active oxygen species</json:string><json:string>superoxide anion</json:string><json:string>peroxidative ability</json:string></teeft></keywords><author><json:item><name>Yumiko Sugioka</name><affiliations><json:string>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</json:string></affiliations></json:item><json:item><name>Mamoru Suzuki</name><affiliations><json:string>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>Chloroquine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Ferriprotoporphyrin IX</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Lipid peroxidation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>Antimalaria</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>FPIX : ferriprotoporphyrin IX</value></json:item></subject><articleId><json:string>90032</json:string></articleId><arkIstex>ark:/67375/6H6-K2J3RS4B-C</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>Full-length article</json:string></originalGenre><abstract>Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.</abstract><qualityIndicators><score>8.733</score><pdfWordCount>4693</pdfWordCount><pdfCharCount>23552</pdfCharCount><pdfVersion>1.2</pdfVersion><pdfPageCount>6</pdfPageCount><pdfPageSize>346 x 447 pts</pdfPageSize><refBibsNative>true</refBibsNative><abstractWordCount>170</abstractWordCount><abstractCharCount>1237</abstractCharCount><keywordCount>5</keywordCount></qualityIndicators><title>The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title><pmid><json:string>2043670</json:string></pmid><pii><json:string>0304-4165(91)90032-C</json:string></pii><genre><json:string>research-article</json:string></genre><host><title>BBA - General Subjects</title><language><json:string>unknown</json:string></language><publicationDate>1991</publicationDate><issn><json:string>0304-4165</json:string></issn><pii><json:string>S0304-4165(00)X0487-4</json:string></pii><volume>1074</volume><issue>1</issue><pages><first>19</first><last>24</last></pages><genre><json:string>journal</json:string></genre></host><namedEntities><unitex><date><json:string>1991</json:string></date><geogName></geogName><orgName><json:string>Biochem</json:string><json:string>State University</json:string><json:string>Lumigen, Inc., Detroit</json:string></orgName><orgName_funder></orgName_funder><orgName_provider></orgName_provider><persName><json:string>J. 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[36]</json:string><json:string>[22]</json:string><json:string>[8]</json:string><json:string>[17]</json:string><json:string>[21]</json:string><json:string>Folch et al. [23]</json:string><json:string>[38]</json:string><json:string>[13,14]</json:string><json:string>Ohkawa et al. [26]</json:string><json:string>[32-34]</json:string><json:string>Moreau et al. [7]</json:string><json:string>[37]</json:string><json:string>[1,7,20]</json:string><json:string>[30]</json:string><json:string>[7]</json:string><json:string>[14]</json:string><json:string>[9]</json:string><json:string>[11,12]</json:string><json:string>[24]</json:string><json:string>[1,7]</json:string><json:string>[19]</json:string></ref_bibl><bibl></bibl></unitex></namedEntities><ark><json:string>ark:/67375/6H6-K2J3RS4B-C</json:string></ark><categories><wos><json:string>1 - science</json:string><json:string>2 - biophysics</json:string><json:string>2 - biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>1 - health sciences</json:string><json:string>2 - biomedical research</json:string><json:string>3 - biochemistry & molecular biology</json:string></scienceMetrix><scopus><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Molecular Biology</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biochemistry</json:string><json:string>1 - Life Sciences</json:string><json:string>2 - Biochemistry, Genetics and Molecular Biology</json:string><json:string>3 - Biophysics</json:string></scopus><inist><json:string>1 - sciences appliquees, technologies et medecines</json:string><json:string>2 - sciences biologiques et medicales</json:string><json:string>3 - sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1991</publicationDate><copyrightDate>1991</copyrightDate><doi><json:string>10.1016/0304-4165(91)90032-C</json:string></doi><id>C1E79E9C3DD9773BD334C21651DDE7C83298DE1A</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/fulltext.pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/bundle.zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/fulltext.tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher scheme="https://scientific-publisher.data.istex.fr">ELSEVIER</publisher><availability><licence><p>elsevier</p></licence></availability><p scheme="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M"></p><date>1991</date></publicationStmt><notesStmt><note type="research-article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</note><note type="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title><author xml:id="author-0000"><persName><forename type="first">Yumiko</forename><surname>Sugioka</surname></persName><note type="biography">Present address: Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</note><note type="correspondence"><p>Correspondence: Y. Sugioka, c/o Professor A.P. Schaap, Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</p></note><affiliation>Present address: Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</affiliation><affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Mamoru</forename><surname>Suzuki</surname></persName><affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</affiliation></author><idno type="istex">C1E79E9C3DD9773BD334C21651DDE7C83298DE1A</idno><idno type="ark">ark:/67375/6H6-K2J3RS4B-C</idno><idno type="DOI">10.1016/0304-4165(91)90032-C</idno><idno type="PII">0304-4165(91)90032-C</idno><idno type="article-id">90032</idno></analytic><monogr><title level="j">BBA - General Subjects</title><title level="j" type="abbrev">BBAGEN</title><idno type="pISSN">0304-4165</idno><idno type="PII">S0304-4165(00)X0487-4</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991"></date><biblScope unit="volume">1074</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="19">19</biblScope><biblScope unit="page" to="24">24</biblScope></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1991</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Keywords</head><item><term>Chloroquine</term></item><item><term>Ferriprotoporphyrin IX</term></item><item><term>Lipid peroxidation</term></item><item><term>Antimalaria</term></item></list></keywords></textClass><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Abbreviations</head><item><term>FPIX</term><term>ferriprotoporphyrin IX</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1990-12-19">Modified</change><change when="1991">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/fulltext.txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Elsevier doc found" wicri:toSee="Elsevier, no converted or simple article"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" </istex:xmlDeclaration><istex:docType PUBLIC="-//ES//DTD journal article DTD version 5.1.0//EN//XML" URI="art510.dtd" name="istex:docType"></istex:docType><istex:document><article version="5.1" xml:lang="en" docsubtype="fla"><item-info><jid>BBAGEN</jid><aid>90032</aid><ce:pii>0304-4165(91)90032-C</ce:pii><ce:doi>10.1016/0304-4165(91)90032-C</ce:doi><ce:copyright type="unknown" year="1991"></ce:copyright></item-info><head><ce:title>The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</ce:title><ce:author-group><ce:author><ce:given-name>Yumiko</ce:given-name><ce:surname>Sugioka</ce:surname><ce:cross-ref refid="cor1"><ce:sup>†</ce:sup></ce:cross-ref><ce:cross-ref refid="fn1"><ce:sup>*</ce:sup></ce:cross-ref></ce:author><ce:author><ce:given-name>Mamoru</ce:given-name><ce:surname>Suzuki</ce:surname></ce:author><ce:affiliation><ce:textfn>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</ce:textfn></ce:affiliation><ce:correspondence id="cor1"><ce:label>†</ce:label><ce:text>Correspondence: Y. Sugioka, c/o Professor A.P. Schaap, Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</ce:text></ce:correspondence><ce:footnote id="fn1"><ce:label>*</ce:label><ce:note-para>Present address: Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</ce:note-para></ce:footnote></ce:author-group><ce:date-received day="6" month="9" year="1990"></ce:date-received><ce:date-revised day="19" month="12" year="1990"></ce:date-revised><ce:abstract id="ab1" class="author" xml:lang="en"><ce:abstract-sec><ce:simple-para>Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.</ce:simple-para></ce:abstract-sec></ce:abstract><ce:keywords class="keyword"><ce:section-title>Keywords</ce:section-title><ce:keyword><ce:text>Chloroquine</ce:text></ce:keyword><ce:keyword><ce:text>Ferriprotoporphyrin IX</ce:text></ce:keyword><ce:keyword><ce:text>Lipid peroxidation</ce:text></ce:keyword><ce:keyword><ce:text>Antimalaria</ce:text></ce:keyword></ce:keywords><ce:keywords class="abr" xml:lang="en"><ce:section-title>Abbreviations</ce:section-title><ce:keyword><ce:text>FPIX</ce:text><ce:keyword><ce:text>ferriprotoporphyrin IX</ce:text></ce:keyword></ce:keyword></ce:keywords></head><tail><ce:bibliography><ce:section-title>References</ce:section-title><ce:bibliography-sec><ce:bib-reference id="bib1"><ce:label>1</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Cohen</ce:surname><ce:given-name>S.N.</ce:given-name></sb:author><sb:author><ce:surname>Phifer</ce:surname><ce:given-name>K.O.</ce:given-name></sb:author><sb:author><ce:surname>Yielding</ce:surname><ce:given-name>K.L.</ce:given-name></sb:author></sb:authors></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nature</sb:maintitle></sb:title><sb:volume-nr>202</sb:volume-nr></sb:series><sb:date>1964</sb:date></sb:issue><sb:pages><sb:first-page>805</sb:first-page><sb:last-page>806</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib2"><ce:label>2</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Macomber</ce:surname><ce:given-name>P.B.</ce:given-name></sb:author><sb:author><ce:surname>Sprinz</ce:surname><ce:given-name>H.</ce:given-name></sb:author><sb:author><ce:surname>Tousimis</ce:surname><ce:given-name>A.J.</ce:given-name></sb:author></sb:authors></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Nature</sb:maintitle></sb:title><sb:volume-nr>214</sb:volume-nr></sb:series><sb:date>1967</sb:date></sb:issue><sb:pages><sb:first-page>937</sb:first-page><sb:last-page>939</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib3"><ce:label>3</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Macomber</ce:surname><ce:given-name>P.B.</ce:given-name></sb:author><sb:author><ce:surname>O'Brien</ce:surname><ce:given-name>R.L.</ce:given-name></sb:author><sb:author><ce:surname>Hahn</ce:surname><ce:given-name>F.E.</ce:given-name></sb:author></sb:authors></sb:contribution><sb:host><sb:issue><sb:series><sb:title><sb:maintitle>Science</sb:maintitle></sb:title><sb:volume-nr>152</sb:volume-nr></sb:series><sb:date>1966</sb:date></sb:issue><sb:pages><sb:first-page>1374</sb:first-page><sb:last-page>1375</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference><ce:bib-reference id="bib4"><ce:label>4</ce:label><sb:reference><sb:contribution><sb:authors><sb:author><ce:surname>Fitch</ce:surname><ce:given-name>C.D.</ce:given-name></sb:author></sb:authors></sb:contribution><sb:host><sb:edited-book><sb:edition>3rd Edn.</sb:edition><sb:book-series><sb:series><sb:title><sb:maintitle>Proc. 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Parasitol.</sb:maintitle></sb:title><sb:volume-nr>62</sb:volume-nr></sb:series><sb:date>1986</sb:date></sb:issue><sb:pages><sb:first-page>356</sb:first-page><sb:last-page>361</sb:last-page></sb:pages></sb:host></sb:reference></ce:bib-reference></ce:bibliography-sec></ce:bibliography></tail></article></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title></titleInfo><titleInfo type="alternative" lang="en" contentType="CDATA"><title>The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation</title></titleInfo><name type="personal"><namePart type="given">Yumiko</namePart><namePart type="family">Sugioka</namePart><affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</affiliation><description>Correspondence: Y. Sugioka, c/o Professor A.P. Schaap, Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</description><description>Present address: Department of Chemistry, Wayne State University, Detroit, MI 48202, U.S.A.</description><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Mamoru</namePart><namePart type="family">Suzuki</namePart><affiliation>Department of Parasitology, Gumma University School of Medicine, Gunma, Japan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="Full-length article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued><dateModified encoding="w3cdtf">1990-12-19</dateModified><copyrightDate encoding="w3cdtf">1991</copyrightDate></originInfo><language><languageTerm type="code" authority="iso639-2b">eng</languageTerm><languageTerm type="code" authority="rfc3066">en</languageTerm></language><abstract lang="en">Ferriprotoporphyrin IX (FPIX) forms a coordination complex with chloroquine, an anti-malarial drug. The FPIX-chloroquine complex strongly promotes the peroxidative cleavage of phospholipid membrane. Iron in the complex is essential for the complex to induce lipid peroxidation. In this paper a more detailed mechanism of the complex promoted lipid peroxidation was investigated. Apotransferrin exhibited no apparent inhibition of the complex evoked lipid peroxidation, indicating no mobilization of iron from the complex. No significant inhibitory effect by superoxide dismutase, catalase and sodium benzoate on the complex induced lipid peroxidative reaction, suggesting little involvement of superoxide anion, hydrogen peroxide and hydroxyl radical in the reaction. Quinine and mefroquine, blood shizontocidal drugs as well as chloroquine, formed a complex with FPIX and each complex more rapidly induced lipid peroxidation than FPIX alone. Phrimaquine, which is not as effective as quinine or mefroquine on an intraerythrocytic malaria parasite, neither coordinated to FPIX nor promoted lipid peroxidation. The complex formation between FPIX and chloroquine, quinine or mefroquine could play a key role in their anti-malarial actions.</abstract><subject lang="en"><genre>Keywords</genre><topic>Chloroquine</topic><topic>Ferriprotoporphyrin IX</topic><topic>Lipid peroxidation</topic><topic>Antimalaria</topic></subject><subject lang="en"><genre>Abbreviations</genre><topic>FPIX : ferriprotoporphyrin IX</topic></subject><relatedItem type="host"><titleInfo><title>BBA - General Subjects</title></titleInfo><titleInfo type="abbreviated"><title>BBAGEN</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>ELSEVIER</publisher><dateIssued encoding="w3cdtf">1991</dateIssued></originInfo><identifier type="ISSN">0304-4165</identifier><identifier type="PII">S0304-4165(00)X0487-4</identifier><part><date>1991</date><detail type="volume"><number>1074</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="issue-pages"><start>1</start><end>216</end></extent><extent unit="pages"><start>19</start><end>24</end></extent></part></relatedItem><identifier type="istex">C1E79E9C3DD9773BD334C21651DDE7C83298DE1A</identifier><identifier type="ark">ark:/67375/6H6-K2J3RS4B-C</identifier><identifier type="DOI">10.1016/0304-4165(91)90032-C</identifier><identifier type="PII">0304-4165(91)90032-C</identifier><identifier type="ArticleID">90032</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-HKKZVM7B-M">elsevier</recordContentSource></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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