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Vol. 9, Issue 5, 1209-1220, May 1998
Subunit in Response to
Dopamine
Departments of
*Molecular Medicine, and
Dopamine (DA) inhibition of Na+,K+-ATPase
in proximal tubule cells is associated with increased endocytosis of
its Clinical
Physiology, Karolinska Institute, Karolinska Hospital, 171 76 Stockholm, Sweden; and
Department of Medicine, The
University of Chicago, Chicago, Illinois 60637
and 
subunits into early and late endosomes via a clathrin
vesicle-dependent pathway. In this report we evaluated intracellular
signals that could trigger this mechanism, specifically the role of
phosphatidylinositol 3-kinase (PI 3-K), the activation of which
initiates vesicular trafficking and targeting of proteins to specific
cell compartments. DA stimulated PI 3-K activity in a time- and
dose-dependent manner, and this effect was markedly blunted by
wortmannin and LY 294002. Endocytosis of the
Na+,K+-ATPase subunit in response to DA was
also inhibited in dose-dependent manner by wortmannin and LY 294002. Activation of PI 3-K generally occurs by association with tyrosine
kinase receptors. However, in this study immunoprecipitation with a
phosphotyrosine antibody did not reveal PI 3-K activity. DA-stimulated
endocytosis of Na+,K+-ATPase subunits
required protein kinase C, and the ability of DA to stimulate PI 3-K
was blocked by specific protein kinase C inhibitors. Activation of PI
3-K is mediated via the D1 receptor subtype and the
sequential activation of phospholipase A2, arachidonic acid, and protein kinase C. The results indicate a key role for activation of PI 3-K in the endocytic sequence that leads to
internalization of Na+,K+-ATPase subunits
in response to DA, and suggest a mechanism for the participation of
protein kinase C in this process.
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