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Articles in PresS, published online ahead of print August 8, 2001
Am J Physiol Renal Physiol, 10.1152/ajprenal.0091.2001
Submitted on March 16, 2001
Accepted on August 1, 2001
1 Dipartimento di Fisiologia Generale ed Ambientale, University of Bari, Bari, Italy
2 Campus Berlin-Buch, Forschungsinstitut fur Molekulare Pharmakologie, Berlin, Germany
3 Institut fur Pharmakologie und Toxikologie, Albert-Ludwigs-Universitat Freiburg, Freiburg, Germany
4 Campus Berlin-Buch, Forschungsinstitut fur Molekulare Pharmakologie, Berlin, Germany; Institut fur Pharmakologie, Freie Universitat Berlin, Berlin, Germany
* To whom correspondence should be addressed. E-mail: g.valenti{at}biologia.uniba.it.
We have recently demonstrated that actin depolymerization is a prerequisite for cAMP-dependent translocation of the water channel aquaporin 2 (AQP2) into the apical membrane in AQP2-transfected renal CD8 cells (29). The Rho family of small GTPases including Cdc42, Rac and Rho, regulates the actin cytoskeleton. In AQP2-transfected CD8 cells inhibition of Rho GTPases with Clostridium difficile toxin B or with Clostridium limosum C3-fusion toxin, as well as incubation with the Rho kinase inhibitor, Y-27632, caused actin depolymerization and translocation of AQP2 in the absence of the cAMP-elevating agent forskolin. Both forskolin and C3 fusion toxin-induced AQP2 translocation were associated to a similar increase in the osmotic water permeability coefficient (Pf). Expression of constitutively active RhoA induced formation of stress fibers and abolished AQP2 translocation in response to forskolin. Cytochalasin D induced both depolymerization of F-actin and AQP2 translocation, suggesting that depolymerization of F-actin is sufficient to induce AQP2 translocation. Together these data indicate that Rho inhibits cAMP-dependent translocation of AQP2 into the apical membrane of renal principal cells by controlling the organization of the actin cytoskeleton.
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