Vacuolar-type proton pumps in insect epithelia

DC FieldValueLanguage
dc.contributor.authorWieczorek, Helmut
dc.contributor.authorBeyenbach, Klaus W.
dc.contributor.authorHuss, Markus
dc.contributor.authorVitavska, Olga
dc.date.accessioned2021-12-23T16:08:30Z-
dc.date.available2021-12-23T16:08:30Z-
dc.date.issued2009
dc.identifier.issn00220949
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8319-
dc.description.abstractActive 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.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 431]; VolkswagenStiftungVolkswagen; NSFNational Science Foundation (NSF) [IOB 0542797]; NIHUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USA [R21 AI072102]; NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R21AI072102] Funding Source: NIH RePORTER; Supported by grants awarded to H. W. and M. H. from the Deutsche Forschungsgemeinschaft (SFB 431) and the VolkswagenStiftung (Funding Initiative `Interplay between Molecular Conformations and Biological Function') and by NSF grant IOB 0542797 and NIH grant R21 AI072102 awarded to K. W. B. Deposited in PMC for release after 12 months.
dc.language.isoen
dc.publisherCOMPANY OF BIOLOGISTS LTD
dc.relation.ispartofJOURNAL OF EXPERIMENTAL BIOLOGY
dc.subjectAedes aegypti
dc.subjectAEDES-AEGYPTI
dc.subjectANIMAL PLASMA-MEMBRANE
dc.subjectBiology
dc.subjectBLOWFLY SALIVARY-GLANDS
dc.subjectDrosophila melanogaster
dc.subjectDROSOPHILA-MELANOGASTER
dc.subjectELECTRON-MICROSCOPY
dc.subjectH+-ATPASE
dc.subjectH+-translocating vacuolar-type ATPase
dc.subjectinsect epithelia
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectManduca sexta
dc.subjectMOSQUITO MALPIGHIAN TUBULES
dc.subjectPROTEIN-KINASE-A
dc.subjecttobacco hornworm
dc.subjectTOBACCO HORNWORM MIDGUT
dc.subjectV-ATPase
dc.subjectV-ATPASE SUBUNIT
dc.titleVacuolar-type proton pumps in insect epithelia
dc.typereview
dc.identifier.doi10.1242/jeb.030007
dc.identifier.isiISI:000266113900004
dc.description.volume212
dc.description.issue11
dc.description.startpage1611
dc.description.endpage1619
dc.identifier.eissn14779145
dc.publisher.placeBIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND
dcterms.isPartOf.abbreviationJ. Exp. Biol.
dcterms.oaStatusGreen Published, Bronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidWiHe990-
crisitem.author.netidHuMa001-
crisitem.author.netidViOl437-
Show simple item record

Page view(s)

5
Last Week
0
Last month
0
checked on May 19, 2024

Google ScholarTM

Check

Altmetric