Chemical modifications of band 3 protein affect the adhesion of Plasmodium falciparum-infected erythrocytes to CD36
E Winograd, S Eda, IW Sherman - Molecular and biochemical parasitology, 2004 - Elsevier
The role of the erythrocyte anion exchanger, band 3 protein (AE1), in the adhesion of
Plasmodium falciparum-infected erythrocytes to CD36 and thrombospondin (TSP) was
studied. Two specific anion exchange inhibitors that bind covalently to different regions of
the band 3 molecule affected cytoadherence in dissimilar ways. Modification of lysine 539 by
diisothiocyanostilbene sulfonic acid (DIDS) resulted in a significant reduction in the
adhesive properties of parasitized erythrocytes for CD36, but not TSP, whereas treatment …
Plasmodium falciparum-infected erythrocytes to CD36 and thrombospondin (TSP) was
studied. Two specific anion exchange inhibitors that bind covalently to different regions of
the band 3 molecule affected cytoadherence in dissimilar ways. Modification of lysine 539 by
diisothiocyanostilbene sulfonic acid (DIDS) resulted in a significant reduction in the
adhesive properties of parasitized erythrocytes for CD36, but not TSP, whereas treatment …