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Inhibition of invasion and intraerythrocytic development ofPlasmodium falciparum by kinase inhibitors (1996)

Dluzewski, A. R. ; Garcia, C. R.

Springer

Cellular and molecular life sciences 52 (1996), S. 621-623

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ISSN: 1420-9071

Keywords: Malaria ; Plasmodium falciparum ; kinase inhibitors ; okadaic acid

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Abstract We have examined the effects of seven protein kinase inhibitors (staurosporine, genistein, methyl 2,5-dihydroxycinnamate, tyrphostins B44 and B46, lavendustin A and R03) on the erythrocytic cycle of the malaria parasite,Plasmodium falciparum. One (staurosporine) strongly inhibits serine/threonine kinases, but the remainder all exhibit a strong preference for tyrosine kinases. We have been able to discriminate between effects on invasion and on intraerythrocytic development. All reagents impeded development of intraerythrocytic parasites, though at widely differing concentrations, from the sub-micromolar to the millimolar. Several inhibitors, including staurosporine, also reduced invasion. The phosphatase inhibitor, okadaic acid, had a strong inhibitory effect both on invasion and development. The regulation of malaria development by phosphorylation or dephosphorylation reactions at several points in the blood-stage cycle is implied.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01969742

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Actin in the merozoite of the malaria parasite, Plasmodium falciparum (1993)

Field, S. J. ; Pinder, Jennifer C. ; Clough, Barbara ; [et al.]

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 25 (1993), S. 43-48

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ISSN: 0886-1544

Keywords: malaria ; Plasmodium falciparum ; merozoite ; actin ; ubiquitin ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Merozoites of the human malaria parasite, Plasmodium falciparum, when treated with cytochalasin B, will attach irreversibly to red cells with formation of a vestigial internal (parasitophorous) vacuole, but they are inhibited from moving into the cell. The existence of an actin-based motile mechanism is implied. Immunoblotting, peptide mapping and the DNase inhibition assay have been used to show that the merozoite contains actin. It makes up an estimated 0.3% of the total parasite protein and is partitioned in the ratio of about 1:2 between the cytosolic and particulate protein fractions. In the former it is unpolymerised and in the latter filamentous. Most of the anti-actin-reactive protein in the soluble fraction and about 20% of that in the pellet has an apparent molecular weight of 55,000 and reacts with an anti-ubiquitin antibody; it is thus evidently ubiquitinyl actin, or arthrin, which has so far been detected only in insect flight muscle. © 1993 Wiley-Liss, Inc.

Additional Material: 5 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/cm.970250106

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