malaria/phosphatase

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Phosphatidic acid homeostasis regulated by a type-2 phosphatidic acid phosphatase represents a novel druggable target in malaria intervention.

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Type-2 phosphatidic acid phosphatase (PAP2) a member of PAP2 superfamily mediates the conversion of phosphatidic acid (PA) to diacylglycerol (DAG) and thus plays a pivotal role in numerous cellular signaling processes in diverse organisms. An elevated level of intracellular PA is detrimental for the

[Variation of cholostase enzymes (5'-nucleotidase and alkaline phosphatase) during a specific treatment for malaria in the Gabonese child].

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Biological variations of 5'nucleotidase (5'NU) and alkaline phosphatase (AP) in 102 Gabonese children with malaria features (MF) and malaria infection (MI) receiving treatment are reported. [formula: see text] During the therapeutic assay, 5'NU rate decreases faster than AP'S; Fourteen days after

Characterisation and expression of a PP1 serine/threonine protein phosphatase (PfPP1) from the malaria parasite, Plasmodium falciparum: demonstration of its essential role using RNA interference.

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BACKGROUND Reversible protein phosphorylation is relatively unexplored in the intracellular protozoa of the Apicomplexa family that includes the genus Plasmodium, to which belong the causative agents of malaria. Members of the PP1 family represent the most highly conserved protein phosphatase

Post-translational generation of constitutively active cores from larger phosphatases in the malaria parasite, Plasmodium falciparum: implications for proteomics.

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BACKGROUND Although the complete genome sequences of a large number of organisms have been determined, the exact proteomes need to be characterized. More specifically, the extent to which post-translational processes such as proteolysis affect the synthesized proteins has remained unappreciated. We

Acid phosphatase as a marker in malaria.

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The serum acid phosphatase (ACP) activity and Hemoglobin (Hb) levels were measured in malaria patients and nonmalarial fever patients. The results were compared with normal healthy control subjects. ACP was significantly increased (P < 0.001) in all the malaria patients. ACP was significantly higher

Protein Tyrosine Phosphatase Inhibition Prevents Experimental Cerebral Malaria by Precluding CXCR3 Expression on T Cells.

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Cerebral malaria induced by Plasmodium berghei ANKA infection is dependent on the sequestration of cytotoxic T cells within the brain and augmentation of the inflammatory response. Herein, we demonstrate that inhibition of protein tyrosine phosphatase (PTP) activity significantly attenuates T cell

A bacterial phosphatase-like enzyme of the malaria parasite Plasmodium falciparum possesses tyrosine phosphatase activity and is implicated in the regulation of band 3 dynamics during parasite invasion.

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Eukaryotic parasites of the genus Plasmodium cause malaria by invading and developing within host erythrocytes. Here, we demonstrate that PfShelph2, a gene product of Plasmodium falciparum that belongs to the Shewanella-like phosphatase (Shelph) subfamily, selectively hydrolyzes phosphotyrosine, as

Genetic analysis of two enzyme polymorphisms in a malaria vector mosquito: octanol dehydrogenase and acid phosphatase in Anopheles culicifacies Giles.

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Genetic analysis was performed on two polymorphic enzyme systems in the malaria vector, Anopheles culicifacies Giles. The data indicate that both enzymes, octanol dehydrogenase and acid phosphatase, are controlled by autosomal loci but that these two loci are not linked. The three expected linkage

Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex.

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Two major protein phosphatase (PP) activities were purified from cytosolic extracts of the erythrocytic stage of the malaria parasite, Plasmodium falciparum. Both enzymes were specific for phosphoserine and phosphothreonine residues with very little activity against phosphotyrosine residues. The

Elevated total and isoenzyme forms of acid phosphatase in falciparum malaria.

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The activities of total serum acid phosphatase (E.C. 3.1.3.2) and of two of its isoenzymes, tartrate-resistant acid phosphatase and erythrocyte-specific acid phosphatase were measured in 109 adult male and female patients presenting acute falciparum malaria infection, and a normal, healthy control

Leukocyte alkaline phosphatase in Plasmodium falciparum malaria.

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We studied leukocyte alkaline phosphatase in malaria to assess leukocyte defence mechanisms. Twenty-seven patients with malaria were stratified into two classes on the basis of disease severity. Fifteen malaria negative patients were taken as controls. Data showed mild polymorphonucleated cell

Shelph2, a bacterial-like phosphatase of the malaria parasite Plasmodium falciparum, is dispensable during asexual blood stage.

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During the erythrocytic cycle of the malaria parasite Plasmodium falciparum, egress and invasion are essential steps finely controlled by reversible phosphorylation. In contrast to the growing number of kinases identified as key regulators, phosphatases have been poorly studied, and calcineurin is

Red cell acid phosphatase: another polymorphism correlated with Malaria?

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The frequency of PC allele for acid phosphatase in fourteen Sardinian villages correlates positively with the altitude and negatively with past malarial morbidity and GdMed prevalence. The susceptibility towards hemolytic favism in Sardinian males with G6PD deficiency is dependent on the erythrocyte

Characterization of a novel serine/threonine protein phosphatase (PfPPJ) from the malaria parasite, Plasmodium falciparum.

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A novel protein phosphatase cDNA of the PPP superfamily was identified from the malaria parasite, Plasmodium falciparum (Pf), and tentatively named PfPPJ. The predicted primary structure of the phosphatase contained all the known conserved motifs of the PPP superfamily essential for catalytic

Protein phosphatase beta, a putative type-2A protein phosphatase from the human malaria parasite Plasmodium falciparum.

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Protein phosphatases play a critical role in the regulation of the eukaryotic cell cycle and signal transduction. A putative protein serine/threonine phosphatase gene has been isolated from the human malaria parasite Plasmodium falciparum. The gene has an unusual intron that contains four repeats of

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