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RORα controls hepatic lipid homeostasis via negative regulation of PPARγ transcriptional network. | LitMetric

AI Article Synopsis

  • RORα is a key protein that helps control important functions in our bodies like brain development and how we process fats.
  • When this protein is missing in the liver, it can cause problems like fatty liver, obesity, and trouble using insulin, especially when eating a lot of fatty foods.
  • Scientists found that RORα works by stopping another protein, PPARγ, from doing its job with fats, and improving RORα's function could help treat conditions connected to weight and metabolism issues.

Article Abstract

The retinoic acid receptor-related orphan receptor-α (RORα) is an important regulator of various biological processes, including cerebellum development, circadian rhythm and cancer. Here, we show that hepatic RORα controls lipid homeostasis by negatively regulating transcriptional activity of peroxisome proliferators-activated receptor-γ (PPARγ) that mediates hepatic lipid metabolism. Liver-specific Rorα-deficient mice develop hepatic steatosis, obesity and insulin resistance when challenged with a high-fat diet (HFD). Global transcriptome analysis reveals that liver-specific deletion of Rorα leads to the dysregulation of PPARγ signaling and increases hepatic glucose and lipid metabolism. RORα specifically binds and recruits histone deacetylase 3 (HDAC3) to PPARγ target promoters for the transcriptional repression of PPARγ. PPARγ antagonism restores metabolic homeostasis in HFD-fed liver-specific Rorα deficient mice. Our data indicate that RORα has a pivotal role in the regulation of hepatic lipid homeostasis. Therapeutic strategies designed to modulate RORα activity may be beneficial for the treatment of metabolic disorders.Hepatic steatosis development may result from dysregulation of lipid metabolism, which is finely tuned by several transcription factors including the PPAR family. Here Kim et al. show that the nuclear receptor RORα inhibits PPARγ-mediated transcriptional activity by interacting with HDAC3 and competing for the promoters of lipogenic genes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5534431PMC
http://dx.doi.org/10.1038/s41467-017-00215-1DOI Listing

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