Inhibition of Sodium–Hydrogen Antiport by Antibodies to NHA1 in Brush Border Membrane Vesicles from Whole Aedes aegypti Larvae

摘要: The present research report describes Na+/H+ antiport by brush border membrane vesicles isolated from whole larvae of Aedes aegypti (AeBBMVw). Our hypothesis is that acid quenching acridine orange AeBBMVw predominantly mediated via the NHA1 component in absence amino acids and ATP. AeNHA1 a antiporter has been postulated to exchange Na+ H+ across apical plasma posterior midgut A. larvae. Its principal function recycle are transported during uptake, e.g., phenylalanine. This uptake mediated, part, voltage-driven, Na+-coupled, nutrient transporter (AeNAT8). voltage generated an V-ATPase. All three components, V-ATPase, antiporter, (VAN), aegypti. By omitting ATP acids, was measured fluorescence (AO) caused acidification either internal vesicle medium (Na+in > Na+out) or external fluid-membrane interface < Na+out). Vesicles with 100 micromolar inside 10 outside 0.01 quenched AO as much 30%. Acidification did not occur AeBBMVw. Preincubation antibodies inhibit dependent quenching, indicating significant role exchange.