par Delporte, Christine 
;O'Connell, Brian C.;He, Xinjun;Ambudkar, Indu S.;Agre, P;Baum, Bruce J.
Référence The Journal of biological chemistry, 271, 36, page (22070-22075)
Publication Publié, 1996-09
;O'Connell, Brian C.;He, Xinjun;Ambudkar, Indu S.;Agre, P;Baum, Bruce J.Référence The Journal of biological chemistry, 271, 36, page (22070-22075)
Publication Publié, 1996-09
Article révisé par les pairs
| Résumé : | 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. |
