NDLI: Nuclear Factor κB Mediates Suppression of Canonical Transient Receptor Potential 6 Expression by Reactive Oxygen Species and Protein Kinase C in Kidney Cells

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Nuclear Factor κB Mediates Suppression of Canonical Transient Receptor Potential 6 Expression by Reactive Oxygen Species and Protein Kinase C in Kidney Cells

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Nuclear Factor κB Mediates Suppression of Canonical Transient Receptor Potential 6 Expression by Reactive Oxygen Species and Protein Kinase C in Kidney Cells

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, Yanxia Chaudhari, Sarika Ding, Min Stankowska, Dorota Krishnamoorthy, Raghu Ma, Rong He, Shaoqing Yuan, Joseph Cunningham, Joseph T. Ding, Yanfeng
Description	Author Affiliation: Wang Y ( Department of Integrative Physiology and Cardiovascular Research Institute, University of North Texas Health Science Center, Fort Worth, Texas 76107, USA.)
Abstract	This study was carried out to explore the molecular mechanism for down-regulation of TRPC6 expression in the reactive oxygen species (ROS)/PKC signaling in kidney cells. In cultured human mesangial cells, H2O2 and TNF- inhibited TRPC6 mRNA expression in a time-dependent manner. Inhibition of NF-κB reversed both H2O2- and phorbol 12-myristate 13-acetate (PMA)-induced decrease in TRPC6 protein expression. Activation of NF-κB by knocking down IκB using siRNA could mimic the suppressive effect of ROS/PKC on TRPC6. a Ca(2+) imaging study showed that activation and inhibition of NF-κB significantly decreased and increased the TRPC6-mediated Ca(2+) entry, respectively. Further experiments showed that PMA, but not its inactive analog 4 -phorbol 12, 13-didecanoate (4 -PDD), caused phosphorylation of IκB and stimulated the nuclear translocation of NF-κB p50 and p65 subunits. The PMA-dependent IκB phosphorylation was significantly inhibited by Gö6976. Electrophoretic mobility shift assay revealed that PMA stimulated DNA binding activity of NF-κB. Furthermore, specific knockdown of p65, but not p50, prevented an H2O2 inhibitory effect on TRPC6 protein expression, suggesting p65 as a predominant NF-κB subunit repressing TRPC6. In agreement with a major role of p65, chromatin immunoprecipitation assays showed that PMA treatment induced p65 binding to the TRPC6 promoter. Moreover, PMA treatment increased the association of p65 with histone deacetylase (HDAC) and decreased histone acetylation at the TRPC6 promoter. Consistently, knockdown of HDAC2 by siRNA or inhibition of HDAC with trichostatin A prevented a H2O2-induced decrease in TRPC6 mRNA and protein expressions, respectively. Taken together, our findings imply an important role of NF-κB in a negative regulation of TRPC6 expression at the gene transcription level in kidney cells.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	18
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-05-03
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Gene Expression Regulation Drug Effects Hydrogen Peroxide Pharmacology Kidney Metabolism NF-kappa B P50 Subunit Oxidants Protein Kinase C TRPC Cation Channels Biosynthesis Transcription Factor RelA Carbazoles Carcinogens Cell Line Enzyme Inhibitors Physiology Gene Knockdown Techniques Histone Deacetylase 2 Antagonists & Inhibitors Genetics Histone Deacetylase Inhibitors Hydroxamic Acids Cytology Response Elements Tetradecanoylphorbol Acetate Transcription, Genetic Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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