Phosphorylation of a P-glycoprotein homologue in Plasmodium falciparum
Identifieur interne : 002D35 ( Main/Exploration ); précédent : 002D34; suivant : 002D36Phosphorylation of a P-glycoprotein homologue in Plasmodium falciparum
Auteurs : Amanda S. Y. Lim [Australie] ; Alan F. Cowman [Australie]Source :
- Molecular & Biochemical Parasitology [ 0166-6851 ] ; 1993.
English descriptors
- Teeft :
- Acid analysis, Amino, Amino acids, Asexual, Asexual erythrocytic life cycle, Asexual life cycle, Chloride channel activity, Chloroquine, Chloroquine resistance, Cowman, Dependent protein kinase, Digestive, Digestive vacuole, Digestive vacuoles, Drug transport, Erythrocyte, Fac8, Fac8 culture, Falciparum, Homologue, Immunoprecipitation, Inhibitor, Karcz, Kinase, Kinase activity, Mefloquine, Multidrug, Parasite, Pfmdrl, Pfmdrl gene, Phosphorylated, Phosphorylation, Plasmodium, Plasmodium falciparum, Protein kinase, Protein kinases, Radiolabeled proteins, Reaction mixture, Ring stage, Serine, Threonine, Threonine residues, Trophozoite, Vacuole.
Abstract
Abstract: A P-glycoprotein homologue has been previously identified in Plasmodium falciparum and was termed PGH 1. This paper describes studies analyzing the phosphorylation of the PGH 1 molecule. It was found, by metabolic labeling with [32P]orthophosphate, that PGH 1 was phosphorylated throughout the entire asexual erythrocytic life cycle of the parasite, with the maximum level of 32P incorporation during the trophozoite and schizont stages. Incubation of trophozoites with modulators of mammalian protein kinases suggests that a Ca2+-dependent protein kinase is involved in phosphorylation of PGH 1. PGH 1 could also be phosphorylated in the presence of γ-32P ATP on purified digestive vacuoles where this protein has previously been localized. Two-dimensional phospho-amino acids analysis revealed that PGH 1 was phosphorylated on serine and threonine residues and the pattern of amino acid phosphorylation was similar for PGH 1 phosphorylated in infected red blood cells and on purified digestive vacuoles. PGH 1 phosphorylation in the presence of some antimalarial drugs was analyzed and it was found that neither chloroquine nor compounds that modulate chloroquine resistance had any effect on PGH 1 phosphorylation.
Url:
DOI: 10.1016/0166-6851(93)90118-H
Affiliations:
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Y." last="Lim">Amanda S. Y. Lim</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>The Walter and Eliza Hall Institute of Medical Research, Post Office, Royal Melbourne Hospital, Melbourne, Victoria 3050</wicri:regionArea><wicri:noRegion>Victoria 3050</wicri:noRegion></affiliation></author><author><name sortKey="Cowman, Alan F" sort="Cowman, Alan F" uniqKey="Cowman A" first="Alan F." last="Cowman">Alan F. Cowman</name><affiliation wicri:level="1"><country xml:lang="fr">Australie</country><wicri:regionArea>The Walter and Eliza Hall Institute of Medical Research, Post Office, Royal Melbourne Hospital, Melbourne, Victoria 3050</wicri:regionArea><wicri:noRegion>Victoria 3050</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular & Biochemical Parasitology</title><title level="j" type="abbrev">MOLBIO</title><idno type="ISSN">0166-6851</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">62</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="293">293</biblScope><biblScope unit="page" to="302">302</biblScope></imprint><idno type="ISSN">0166-6851</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0166-6851</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acid analysis</term><term>Amino</term><term>Amino acids</term><term>Asexual</term><term>Asexual erythrocytic life cycle</term><term>Asexual life cycle</term><term>Chloride channel activity</term><term>Chloroquine</term><term>Chloroquine resistance</term><term>Cowman</term><term>Dependent protein kinase</term><term>Digestive</term><term>Digestive vacuole</term><term>Digestive vacuoles</term><term>Drug transport</term><term>Erythrocyte</term><term>Fac8</term><term>Fac8 culture</term><term>Falciparum</term><term>Homologue</term><term>Immunoprecipitation</term><term>Inhibitor</term><term>Karcz</term><term>Kinase</term><term>Kinase activity</term><term>Mefloquine</term><term>Multidrug</term><term>Parasite</term><term>Pfmdrl</term><term>Pfmdrl gene</term><term>Phosphorylated</term><term>Phosphorylation</term><term>Plasmodium</term><term>Plasmodium falciparum</term><term>Protein kinase</term><term>Protein kinases</term><term>Radiolabeled proteins</term><term>Reaction mixture</term><term>Ring stage</term><term>Serine</term><term>Threonine</term><term>Threonine residues</term><term>Trophozoite</term><term>Vacuole</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: A P-glycoprotein homologue has been previously identified in Plasmodium falciparum and was termed PGH 1. This paper describes studies analyzing the phosphorylation of the PGH 1 molecule. It was found, by metabolic labeling with [32P]orthophosphate, that PGH 1 was phosphorylated throughout the entire asexual erythrocytic life cycle of the parasite, with the maximum level of 32P incorporation during the trophozoite and schizont stages. Incubation of trophozoites with modulators of mammalian protein kinases suggests that a Ca2+-dependent protein kinase is involved in phosphorylation of PGH 1. PGH 1 could also be phosphorylated in the presence of γ-32P ATP on purified digestive vacuoles where this protein has previously been localized. Two-dimensional phospho-amino acids analysis revealed that PGH 1 was phosphorylated on serine and threonine residues and the pattern of amino acid phosphorylation was similar for PGH 1 phosphorylated in infected red blood cells and on purified digestive vacuoles. PGH 1 phosphorylation in the presence of some antimalarial drugs was analyzed and it was found that neither chloroquine nor compounds that modulate chloroquine resistance had any effect on PGH 1 phosphorylation.</div></front></TEI><affiliations><list><country><li>Australie</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Lim, Amanda S Y" sort="Lim, Amanda S Y" uniqKey="Lim A" first="Amanda S. Y." last="Lim">Amanda S. Y. Lim</name></noRegion><name sortKey="Cowman, Alan F" sort="Cowman, Alan F" uniqKey="Cowman A" first="Alan F." last="Cowman">Alan F. Cowman</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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