Animal plasma membrane energization by proton motive V-ATPases

DC FieldValueLanguage
dc.contributor.authorWieczorek, H
dc.contributor.authorBrown, D
dc.contributor.authorGrinstein, S
dc.contributor.authorEhrenfeld, J
dc.contributor.authorHarvey, WR
dc.date.accessioned2021-12-23T16:21:18Z-
dc.date.available2021-12-23T16:21:18Z-
dc.date.issued1999
dc.identifier.issn02659247
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/13809-
dc.description.abstractProton-translocating, vacuolar-type ATPases, well known energizers of eukaryotic, vacuolar membranes, now emerge as energizers of many plasma membranes. Just as Na+ gradients, imposed by Na+/K+ ATPases, energize basolateral plasma membranes of epithelia, so voltage gradients, imposed by H+ V-ATPases, energize apical plasma membranes. The energized membranes acidify or alkalinize compartments, absorb or secrete ions and fluids, and underwrite cellular homeostasis. V-ATPases acidify extracellular spaces of single cells such as phagocytes and osteoclasts and of polarized epithelia, such as vertebrate kidney and epididymis. They alkalinize extracellular spaces of lepidopteran midgut. V-ATPases energize fluid secretion by insect Malpighian tubules and fluid absorption by insect oocytes. They hyperpolarize external plasma membranes for Na+ uptake by amphibian skin and fish gills. Indeed, it is likely that ion uptake by osmotically active membranes of all fresh water organisms is energized by V-ATPases. Awareness of plasma membrane energization by V-ATPases provides new perspectives for basic science and presents new opportunities for medicine and agriculture. BioEssays 21.637-648, 1999. (C) 1999 John Wiley & Sons, Inc.
dc.description.sponsorshipNATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R01AI022444] Funding Source: NIH RePORTER; NIAID NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [AI22444] Funding Source: Medline; NIDCD NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute on Deafness & Other Communication Disorders (NIDCD) [DC42956] Funding Source: Medline
dc.language.isoen
dc.publisherCOMPANY OF BIOLOGISTS LTD
dc.relation.ispartofBIOESSAYS
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiology
dc.subjectFROG-SKIN
dc.subjectION-TRANSPORT
dc.subjectK+/H+ ANTIPORT
dc.subjectLARVAL MIDGUT
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectMAMMALIAN KIDNEY
dc.subjectMITOCHONDRIA-RICH CELLS
dc.subjectMURINE MACROPHAGES
dc.subjectRANA-ESCULENTA
dc.subjectTOBACCO HORNWORM MIDGUT
dc.subjectVACUOLAR H+-ATPASE
dc.titleAnimal plasma membrane energization by proton motive V-ATPases
dc.typereview
dc.identifier.doi10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W
dc.identifier.isiISI:000081871700003
dc.description.volume21
dc.description.issue8
dc.description.startpage637
dc.description.endpage648
dc.publisher.placeBIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND
dcterms.isPartOf.abbreviationBioessays
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidWiHe990-
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