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(Received for publication, March 26, 1996, and in revised form, June 6, 1996)
and
From the Clinical Investigations and Patient Care Branch, NIDR,
National Institutes of Health, Bethesda, Maryland 20892-1190 and
the A 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.
Department of Biological Chemistry, The Johns
Hopkins University School of Medicine,
Baltimore, Maryland 21205
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