ADENOVIRUS-MEDIATED EXPRESSION OF AQUAPORIN-5 IN EPITHELIAL-CELLS

A recombinant adenovirus coding for rat aquaporin-5 was constructed an d plaque purified. The recombinant adenovirus (AdrAQP5) mediated the e xpression of aquaporin-5 in rat and human salivary cell lines and in d og kidney cells in vitro as demonstrated by Northern blot and Western blot analyses, and by confocal microscopy after immunofluorescent labe ling. In kidney cells, expression of the transgene was optimal if cell s were infected at their basolateral surface, a phenomenon associated with the distribution of integrin receptors on these cells. The expres sed aquaporin-5 protein was functionally active because viral-mediated gene transfer resulted in a significant increase in the osmotically d irected net fluid secretion rate across monolayers of kidney cells. Ad rAQP5 should provide an efficient and useful means to impart facilitat ed water permeability to cells lacking such a pathway.