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Am J Physiol Renal Physiol (July 9, 2002). doi:10.1152/ajprenal.00156.2002
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Articles in PresS, published online ahead of print July 9, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00156.2002
Submitted on April 22, 2002
Accepted on June 19, 2002

NF-{kappa}B Inhibits Transcription of the H+-K+-ATPase {alpha}2 Subunit Gene: Role of Histone Deacetylases

Wenzheng Zhang1 and Bruce C. Kone1*

1 Department of Internal Medicine, The University of Texas Medical School at Houston, Houston, TX, USA

* To whom correspondence should be addressed. E-mail: bruce.c.kone{at}uth.tmc.edu.

The H+-K+-ATPase {alpha}2 (HK{alpha}2) gene plays a central role in potassium homeostasis, yet little is known about its transcriptional control. We recently demonstrated that the proximal promoter confers basal transcriptional activity in mIMCD3 cells. We sought to determine whether the {kappa}B DNA binding element at -104 to -94 influences HK{alpha}2 gene transcription in these cells. Recombinant NF-{kappa}B p50 footprinted the region -116/-94 in vitro. Gel shift and supershift analysis revealed NF-{kappa}B p50- and p65-containing DNA-protein complexes in nuclear extracts of mIMCD3 cells. A promoter-luciferase construct with a mutated -104/-94 NF-{kappa}B element exhibited higher activity than the wild type promoter in transfection assays. Overexpression of NF-{kappa}B p50, p65 or their combination transrepressed the HK{alpha}2 promoter. The histone deacetylase (HDAC) inhibitor trichostatin A partially reversed NF-{kappa}B-mediated transrepression of the HK{alpha}2 promoter. HDAC6 overexpression inhibited HK{alpha}2 promoter activity, and HDAC6 co-immunoprecipitated with NF-{kappa}B p50 and p65. These results suggest that HDAC6, recruited to the DNA protein complex, acts with NF-{kappa}B to suppress HK{alpha}2 transcription, and identify NF-{kappa}B p50 and p65 as a novel binding partner for HDAC6.




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