Show simple item record

dc.contributor.authorBaum, Bruce J.
dc.contributor.authorDelporte, Christine
dc.contributor.authorAmbudkar, Indu S.
dc.contributor.authorHe, Xinjun
dc.contributor.authorO'Connell, Brian C.
dc.contributor.authorAgre, Peter
dc.date.accessioned2010-03-03T22:01:59Z
dc.date.available2010-03-03T22:01:59Z
dc.date.issued1996-09-06
dc.identifier.citationJ Biol Chem. 1996 Sep 6;271(36):22070-5. doi: 10.1074/jbc.271.36.22070en_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/33871
dc.description.abstractA recombinant adenovirus coding for rat aquaporin-5 was constructed and plaque purified. The recombinant adenovirus (AdrAQP5) mediated the expression of aquaporin-5 in rat and human salivary cell lines and in dog kidney cells in vitro as demonstrated by Northern blot and Western blot analyses, and by confocal microscopy after immunofluorescent labeling. In kidney cells, expression of the transgene was optimal if cells were infected at their basolateral surface, a phenomenon associated with the distribution of integrin receptors on these cells. The expressed aquaporin-5 protein was functionally active because viral-mediated gene transfer resulted in a significant increase in the osmotically directed net fluid secretion rate across monolayers of kidney cells. AdrAQP5 should provide an efficient and useful means to impart facilitated water permeability to cells lacking such a pathway.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.source.urihttp://www.jbc.org/content/271/36/22070.abstract?sid=dd1ab0b8-3c9f-4248-926d-fede84860517
dc.subjectMembrane Proteinsen_US
dc.subjectIon Channels/biosynthesisen_US
dc.subjectSalivary Glands/metabolismen_US
dc.subjectAdenoviridae/geneticsen_US
dc.subjectAquaporinsen_US
dc.titleAdenovirus-mediated Expression of Aquaporin-5 in Epithelial Cellsen_US
dc.typeArticleen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record