ChloroquineV1, Main, Exploration, bibRecord, 002378

Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin

Identifieur interne : 002378 ( Main/Exploration ); précédent : 002377; suivant : 002379

Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin

Auteurs : Mary M. Chen [États-Unis] ; Lirong Shi [États-Unis] ; David J. Sullivan Jr. [États-Unis]

Source :

Molecular & Biochemical Parasitology [ 0166-6851 ] ; 2001.

RBID : ISTEX:A7690AAB8E28AAE2A58875F301E538AB5298FD21

English descriptors

Abstract

Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.

Url:

https://api.istex.fr/ark:/67375/6H6-Q51W98V0-3/fulltext.pdf

DOI: 10.1016/S0166-6851(00)00365-0

Affiliations:

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Le document en format XML

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<term>H2O2, hydrogen peroxide</term>
<term>Haemoproteus columbae</term>
<term>Heme polymer</term>
<term>Hemozoin</term>
<term>Plasmodium falciparum</term>
<term>Quinoline</term>
<term>SDS, sodium dodecyl sulfate</term>
<term>Schistosoma mansoni</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Antimalarial</term>
<term>Chloroquine</term>
<term>Columbae</term>
<term>Columbae heme polymers</term>
<term>Degradation</term>
<term>Erythrocyte</term>
<term>Falciparum</term>
<term>Falciparum heme polymer</term>
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<term>Haemoproteus</term>
<term>Heme</term>
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<term>Heme polymer</term>
<term>Heme polymer extension</term>
<term>Heme polymer formation</term>
<term>Heme polymers</term>
<term>Hemozoin</term>
<term>Mansoni</term>
<term>Monomer</term>
<term>Parasite</term>
<term>Parasitology</term>
<term>Plasmodium</term>
<term>Polymer</term>
<term>Quinoline</term>
<term>Quinoline inhibition</term>
<term>Quinolines</term>
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<front><div type="abstract" xml:lang="en">Abstract: Many parasites digest hemoglobin as an amino acid source, but only a few produce heme polymer pigment instead of catabolizing heme via heme oxygenase. This work compares purified heme polymers produced by Haemoproteus columbae and Schistosoma mansoni to that of Plasmodium falciparum hemozoin and synthetic β-hematin. Fourier-transform infrared spectroscopy identifies the signature peaks of the common iron–carboxylate bond characteristic in all four heme polymers. However, all pigments could be distinguished by quite different three-dimensional structure visualized by Field Emission Inlens Scanning Electron Microscopy. Both P. falciparum and H. columbae heme polymers had a symmetrical shape unlike the amorphous S. mansoni heme polymer and β-hematin. All four heme pigments serve as templates for heme polymer extension, which was inhibitable by chloroquine and other quinoline antimalarials. The polymers showed different levels of resistance to hydrogen peroxide degradation. This work identifies another genus, Haemoproteus, capable of intracellular heme polymer formation. The different three-dimensional structures of each pigment implicate genus specific formation of heme polymer, variation of inhibition of polymer extension by the quinolines and degradation by hydrogen peroxide.</div>
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Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin

Haemoproteus and Schistosoma synthesize heme polymers similar to Plasmodium hemozoin and β-hematin

Source :

English descriptors

Abstract

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

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Pour mettre un lien sur cette page dans le réseau Wicri