title: Vacuolar-type proton pumps in insect epithelia.
abstract: Active transepithelial cation transport in insects was initially discovered in Malpighian tubules, and was subsequently also found in other epithelia such as salivary glands, labial glands, midgut and sensory sensilla. Today it appears to be established that the cation pump is a two-component system of a H(+)-transporting V-ATPase and a cation/nH(+) antiporter. After tracing the discovery of the V-ATPase as the energizer of K(+)/nH(+) antiport in the larval midgut of the tobacco hornworm Manduca sexta we show that research on the tobacco hornworm V-ATPase delivered important findings that emerged to be of general significance for our knowledge of V-ATPases, which are ubiquitous and highly conserved proton pumps. We then discuss the V-ATPase in Malpighian tubules of the fruitfly Drosophila melanogaster where the potential of post-genomic biology has been impressively illustrated. Finally we review an integrated physiological approach in Malpighian tubules of the yellow fever mosquito Aedes aegypti which shows that the V-ATPase delivers the energy for both transcellular and paracellular ion transport.
authors.affiliation: Department of Biology/Chemistry, University of Osnabrück, 49069 Osnabrück, Germany. wieczorek@biologie.uni-osnabrueck.de
authors.forename: Helmut
authors.initials: H
authors.lastname: Wieczorek
authors.forename: Klaus W
authors.initials: KW
authors.lastname: Beyenbach
authors.forename: Markus
authors.initials: M
authors.lastname: Huss
authors.forename: Olga
authors.initials: O
authors.lastname: Vitavska
mesh_terms: D000818:Animals; D004848:Epithelium / Q000378:metabolism* / Q000648:ultrastructure; D015971:Gene Expression Regulation, Enzymologic; D007313:Insecta / Q000378:metabolism*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D025262:Vacuolar Proton-Translocating ATPases