PHOSPHORYLATION OF A P-GLYCOPROTEIN HOMOLOG IN PLASMODIUM-FALCIPARUM
- Author(s)
- Lim, ASY; Cowman, AF;
- Details
- Publication Year 1993-12,Volume 62,Issue #2,Page 293-302
- Journal Title
- MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- Publication Type
- Journal Article
- 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 [P-32]orthophosphate, that PGH 1 was phosphorylated throughout the entire asexual erythrocytic life cycle of the parasite, with the maximum level of P-32 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 I could also be phosphorylated in the presence of gamma-(32)p ATp on purified digestive vacuoles where this protein has previously been localized. Two-dimensional phospho-amino acid analysis revealed that PGH 1 was phosphorylated on serine and threonine residues and the pattern of amino acid phosphorylation was similar for PGH I 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 I phosphorylation.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- MULTIDRUG-RESISTANCE GENE; CHLOROQUINE RESISTANCE; FALCIPARUM; CELLS; IDENTIFICATION; AMPLIFICATION; TRANSPORT
- Publisher's Version
- https://doi.org/10.1016/0166-6851(93)90118-H
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1993-12-01 12:00:00