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Articles in PresS, published online ahead of print February 19, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00260.2001
Submitted on August 17, 2001
Accepted on February 16, 2002
1 Department of Woman and Child Health, Karolinska Institutet, Stockholm, Sweden; Laboratory of Physiological Genetics, Institute of Cytology and Genetics, Novosibirsk, Russian Federation
2 Department of Woman and Child Health, Karolinska Institutet, Stockholm, Sweden; Group of Functional Genomics, Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, Russian Federation
3 Group of Functional Genomics, Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, Russian Federation
4 Department of Woman and Child Health, Karolinska Institutet, Stockholm, Sweden
* To whom correspondence should be addressed. E-mail: marina.zelenina{at}ks.se.
Aquaporin 4 (AQP4) plays an important role for the basolateral movement of water in collecting duct. Here we show that this water channel can be dynamically regulated. Water permeability (Pf) was measured in individual LLC-PK1 cells that were transiently transfected with AQP4. To identify which cells that were transfected, AQP4 was tagged at N-terminus with green fluorescent protein. Transfected cells showed strong fluorescent signal in basolateral membrane and low to negligible signal in cytosol and apical membrane. Activation of protein kinase C (PKC) with phorbol 12,13-dibutyrate (PDBu) significantly decreased Pf of cells expressing AQP4, but had no effect on untransfected neighbor cells. No redistribution of AQP4 in response to PDBu was detected. Dopamine also inhibited the Pf in transfected cells. The effect was abolished by PKC inhibitor Ro 31-8220. Inhibition of AQP4 by PDBu and dopamine was abolished by point mutation of serine-180 (Ser180), a consensus site for PKC phosphorylation. We conclude that PKC and dopamine inhibit AQP4 via phosphorylation at Ser180 and that the effect is likely mediated by gating of the channel.
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