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Am J Physiol Renal Physiol (March 6, 2007). doi:10.1152/ajprenal.00360.2006
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Submitted on September 8, 2006
Accepted on February 22, 2007

SELECTIVE BASOLATERAL LOCALIZATION OF OVER-EXPRESSED Na,K-ATPase {beta}1 AND {beta}2SUBUNITS IS DISRUPTED BY BUTYRATE TREATMENT OF MDCK CELLS

Melissa D Laughery1, Rebecca J Clifford1, Yiqing Chi1, and Jack H Kaplan1*

1 Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois, United States

* To whom correspondence should be addressed. E-mail: kaplanj{at}uic.edu.

The exclusive basolateral localization of the Na,K-ATPase in kidney epithelium is a critical aspect of nephron function. It has been suggested that mislocalized delivery of the Na,K-ATPase to the apical surface in Autosomal Dominant Polycystic Kidney Disease (ADPKD) is due to the inappropriate expression of an alternative isoform of the {beta} subunit, the {beta}2 isoform. It has been reported that heterologous expression of this {beta}2 isoform in MDCK cells results in apical delivery of the Na,K-ATPase. We created a MDCK cell line containing a tetracycline-inducible promoter and expressed either myc-tagged {beta}2 or flag-tagged {beta}1 subunits to study the surface localization of these {beta} subunit isoforms in polarized monolayers. We find that the {beta}2 isoform is targeted to the basolateral surface of the plasma membrane in a polarization pattern indistinguishable from the {beta}1 isoform. However, inclusion of butyrate in the growth medium leads to up-regulation of over-expressed {beta}1 or {beta}2 subunits and to their appearance at the apical surface. The {beta}2 isoform expressed in MDCK cells does not assemble into {alpha}1{beta}2 heterodimers with the endogenous {alpha}1. Our findings demonstrate that expression of the {beta}2 isoform does not lead to apical localization of the Na,K-ATPase in MDCK cells and provides evidence for an unexpected effect of butyrate on the trafficking of Na pump subunits.




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Am J Physiol Renal Physiol, November 1, 2008; 295(5): F1314 - F1323.
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