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A more recent version of this article appeared on April 1, 2002
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Submitted on July 2, 2001
Revised on October 15, 2001
Accepted on February 11, 2002
1 Pulmonary and Critical Care Medicine, Northwestern University Medical School, Chicago, Illinois 60611
2 Department of Molecular Medicine, Karolinska Institutet, Karolinska Hospital, S-171 76 Stockholm, Sweden
3 Department of Medicine, University of Chicago, Chicago, Illinois 60637
4 Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305
* Corresponding author. E-mail address: j-sznajder{at}northwestern.edu.
The purpose of this study was to define mechanisms by which DA regulates the Na,K-ATPase in alveolar epithelial type 2 (AT2) cells. The Na,K-ATPase activity increased by 2-fold in cells incubated with either 1 µM DA or a dopaminergic D1 agonist, fenoldopam, but not with the dopaminergic D2 agonist, quinpirole. The increase in activity paralleled an increase in Na,K-ATPase 
1 and ß1 protein abundance in the basolateral membrane (BLM) of AT2 cells. This increase in protein abundance was mediated by the exocytosis of Na,K-pumps from late endosomal compartments into the BLM. Downregulation of diacylglycerol-sensitive PKCs by pre-treatment with phorbol 12-myristate 13-acetate (PMA) or inhibition with bisindolylmaleimide prevented the DA-mediated increase in Na,K-ATPase activity and exocytosis of Na,K-pumps to the BLM. Preincubation of AT2 cells with either Gö6983, a selective inhibitor of PKC-
, or isozyme specific inhibitor peptides for PKC- or PKC-
, inhibited the DA-mediated increase in Na,K-ATPase. PKC- and PKC-, but not PKC- or -ß, translocated from the cytosol to the membrane fraction following exposure to DA. PKC- and PKC- specific peptide agonists increased Na,K-ATPase protein abundance in the BLM. Accordingly, dopamine increased Na,K-ATPase activity in alveolar epithelial cells through the exocytosis of Na,K-pumps from late endosomes into the basolateral membrane in a mechanism dependent on activation of the novel protein kinase C isozymes, PKC- and PKC-.
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