ChloroquineV1, Main, Exploration, bibRecord, 002F55

The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation

Identifieur interne : 002F55 ( Main/Exploration ); précédent : 002F54; suivant : 002F56

The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation

Auteurs : Yumiko Sugioka [Japon] ; Mamoru Suzuki [Japon]

Source :

BBA - General Subjects [ 0304-4165 ] ; 1991.

RBID : ISTEX:C1E79E9C3DD9773BD334C21651DDE7C83298DE1A

English descriptors

KwdEn :
- Antimalaria, Chloroquine, FPIX, Ferriprotoporphyrin IX, Lipid peroxidation.
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:

https://api.istex.fr/ark:/67375/6H6-K2J3RS4B-C/fulltext.pdf

DOI: 10.1016/0304-4165(91)90032-C

Affiliations:

Japon

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antimalaria</term>
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<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>
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<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>
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<name sortKey="Suzuki, Mamoru" sort="Suzuki, Mamoru" uniqKey="Suzuki M" first="Mamoru" last="Suzuki">Mamoru Suzuki</name>
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The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation

The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri