yw-3548 and 1-10-phenanthroline

yw-3548 has been researched along with 1-10-phenanthroline* in 1 studies

Other Studies

1 other study(ies) available for yw-3548 and 1-10-phenanthroline

Article	Year
Differential effect of 1,10-phenanthroline on mammalian, yeast, and parasite glycosylphosphatidylinositol anchor synthesis. Biochemical and biophysical research communications, 2001, Nov-16, Volume: 288, Issue:5 Glycosylphosphatidylinositol (GPI) anchoring of proteins to the plasma membrane is a common mechanism utilized by all eukaryotes including mammals, yeast, and the Trypanosoma brucei parasite. We have previously shown that in mammals phenanthroline (PNT) blocks the attachment of phosphoethanolamine (P-EthN) groups to mannose residues in GPI anchor intermediates, thus preventing the synthesis of mammalian GPI anchors. Therefore, PNT is likely to inhibit GPI-phosphoethanolamine transferases (GPI-PETs). Here we report that in yeast, PNT also inhibits the synthesis of the GPI anchor as well as GPI-anchored proteins. Interestingly, the mechanism of PNT inhibition of GPI synthesis is different from that of YW3548, another putative GPI-PET inhibitor. In contrast to mammals and yeast, the synthesis of GPIs in T. brucei is not affected by PNT. Our results indicate that the T. brucei GPI-PET could be a potential target for antiparasitic drugs. Topics: Animals; Cell Membrane; Enzyme Inhibitors; Ethanolaminephosphotransferase; Glycosylphosphatidylinositols; HeLa Cells; Humans; Lactones; Models, Chemical; Phenanthrolines; Species Specificity; Terpenes; Trypanosoma brucei brucei; Yeasts; Zinc	2001

Article

Year

Differential effect of 1,10-phenanthroline on mammalian, yeast, and parasite glycosylphosphatidylinositol anchor synthesis.

Biochemical and biophysical research communications, 2001, Nov-16, Volume: 288, Issue:5

Glycosylphosphatidylinositol (GPI) anchoring of proteins to the plasma membrane is a common mechanism utilized by all eukaryotes including mammals, yeast, and the Trypanosoma brucei parasite. We have previously shown that in mammals phenanthroline (PNT) blocks the attachment of phosphoethanolamine (P-EthN) groups to mannose residues in GPI anchor intermediates, thus preventing the synthesis of mammalian GPI anchors. Therefore, PNT is likely to inhibit GPI-phosphoethanolamine transferases (GPI-PETs). Here we report that in yeast, PNT also inhibits the synthesis of the GPI anchor as well as GPI-anchored proteins. Interestingly, the mechanism of PNT inhibition of GPI synthesis is different from that of YW3548, another putative GPI-PET inhibitor. In contrast to mammals and yeast, the synthesis of GPIs in T. brucei is not affected by PNT. Our results indicate that the T. brucei GPI-PET could be a potential target for antiparasitic drugs.

Topics: Animals; Cell Membrane; Enzyme Inhibitors; Ethanolaminephosphotransferase; Glycosylphosphatidylinositols; HeLa Cells; Humans; Lactones; Models, Chemical; Phenanthrolines; Species Specificity; Terpenes; Trypanosoma brucei brucei; Yeasts; Zinc

2001