Animal plasma membrane energization by proton motive V-ATPases
DC Element | Wert | Sprache |
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dc.contributor.author | Wieczorek, H | |
dc.contributor.author | Brown, D | |
dc.contributor.author | Grinstein, S | |
dc.contributor.author | Ehrenfeld, J | |
dc.contributor.author | Harvey, WR | |
dc.date.accessioned | 2021-12-23T16:21:18Z | - |
dc.date.available | 2021-12-23T16:21:18Z | - |
dc.date.issued | 1999 | |
dc.identifier.issn | 02659247 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/13809 | - |
dc.description.abstract | Proton-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.sponsorship | 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) [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.iso | en | |
dc.publisher | COMPANY OF BIOLOGISTS LTD | |
dc.relation.ispartof | BIOESSAYS | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biology | |
dc.subject | FROG-SKIN | |
dc.subject | ION-TRANSPORT | |
dc.subject | K+/H+ ANTIPORT | |
dc.subject | LARVAL MIDGUT | |
dc.subject | Life Sciences & Biomedicine - Other Topics | |
dc.subject | MAMMALIAN KIDNEY | |
dc.subject | MITOCHONDRIA-RICH CELLS | |
dc.subject | MURINE MACROPHAGES | |
dc.subject | RANA-ESCULENTA | |
dc.subject | TOBACCO HORNWORM MIDGUT | |
dc.subject | VACUOLAR H+-ATPASE | |
dc.title | Animal plasma membrane energization by proton motive V-ATPases | |
dc.type | review | |
dc.identifier.doi | 10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W | |
dc.identifier.isi | ISI:000081871700003 | |
dc.description.volume | 21 | |
dc.description.issue | 8 | |
dc.description.startpage | 637 | |
dc.description.endpage | 648 | |
dc.publisher.place | BIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND | |
dcterms.isPartOf.abbreviation | Bioessays | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | WiHe990 | - |
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