Differential Expression and Function of Alternative Splicing Variants of Human Liver X Receptor α

2012 ◽  
Vol 81 (6) ◽  
pp. 800-810 ◽  
Author(s):  
Kaori Endo-Umeda ◽  
Shigeyuki Uno ◽  
Ko Fujimori ◽  
Yoshikazu Naito ◽  
Koichi Saito ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Differential Expression ◽  
Human Liver ◽  
Liver X Receptor ◽  
Splicing Variants ◽  
Liver X Receptor Α ◽  
And Function

Liver X receptor α participates in LPS-induced reduction of triglyceride synthesis in bovine mammary epithelial cells

2020 ◽  
pp. 1-7
Author(s):  
Jianfa Wang ◽  
Shuai Lian ◽  
Jun Song ◽  
Hai Wang ◽  
Xu Zhang ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Epithelial Cells ◽  
Dairy Cow ◽  
Milk Fat ◽  
Mammary Epithelial Cells ◽  
Liver X Receptor ◽  
Mammary Epithelial ◽  
Triglyceride Synthesis ◽  
Milk Fat Depression ◽  
Liver X Receptor Α

Abstract Lipopolysaccharides (LPS) could induce milk fat depression via regulating the body and blood fat metabolism. However, it is not completely clear how LPS might regulate triglyceride synthesis in dairy cow mammary epithelial cells (DCMECs). DCMECs were isolated and purified from dairy cow mammary tissue and treated with LPS. The level of triglyceride synthesis, the expression and activity of the liver X receptor α (LXRα), enzymes related to de novo fatty acid synthesis, and the expression of the fatty acid transporters were investigated. We found that LPS decreased the level of triglyceride synthesis via a down-regulation of the transcription, translation, and nuclear translocation level of the LXRα. The results also indicated that the transcription level of the LXRα target genes, sterol regulatory element binding protein 1 (SREBP1), fatty acid synthetase (FAS), acetyl-CoA carboxylase-1 (ACC1), were significantly down-regulated in DCMECs after LPS treatment. Our data may provide new insight into the mechanisms of milk fat depression caused by LPS.

Alternative splicing variants of carbonic anhydrase IX in human non-small cell lung cancer

Lung Cancer ◽  
2009 ◽  
Vol 64 (3) ◽  
pp. 271-276 ◽  
Author(s):  
Francesca Malentacchi ◽  
Lisa Simi ◽  
Caterina Nannelli ◽  
Matteo Andreani ◽  
Alberto Janni ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Alternative Splicing ◽  
Carbonic Anhydrase ◽  
Small Cell Lung Cancer ◽  
Cell Lung Cancer ◽  
Small Cell ◽  
Carbonic Anhydrase Ix ◽  
Small Cell Lung ◽  
Splicing Variants

scholarly journals The CYP3A4 intron 6 C>T polymorphism (CYP3A4*22) is associated with reduced CYP3A4 protein level and function in human liver microsomes

2013 ◽  
Vol 38 (3) ◽  
pp. 349-354 ◽  
Author(s):  
Maho Okubo ◽  
Norie Murayama ◽  
Makiko Shimizu ◽  
Tsutomu Shimada ◽  
F. Peter Guengerich ◽  
...  
Keyword(s):  
Protein Level ◽  
Human Liver ◽  
Liver Microsomes ◽  
Human Liver Microsomes ◽  
And Function

scholarly journals Liver X Receptor-α Regulates Proopiomelanocortin (POMC) Gene Transcription in the Pituitary

2009 ◽  
Vol 23 (1) ◽  
pp. 47-60 ◽  
Author(s):  
Shunichi Matsumoto ◽  
Koshi Hashimoto ◽  
Masanobu Yamada ◽  
Teturou Satoh ◽  
Junko Hirato ◽  
...  
Keyword(s):  
Gene Transcription ◽  
Liver X Receptor ◽  
Liver X Receptor Α ◽  
Pomc Gene

scholarly journals Estrogen-related Receptor β (ERRβ) – Renaissance Receptor or Receptor Renaissance?

2016 ◽  
Vol 14 (1) ◽  
pp. nrs.14002 ◽  
Author(s):  
Shailaja D. Divekar ◽  
Deanna M. Tiek ◽  
Aileen Fernandez ◽  
Rebecca B. Riggins
Keyword(s):  
Alternative Splicing ◽  
Nuclear Receptor ◽  
Family Members ◽  
Structure And Function ◽  
The Other ◽  
Orphan Nuclear Receptor ◽  
Nuclear Receptor Superfamily ◽  
And Function ◽  
The Impact ◽  
Estrogen Related Receptor

Estrogen-related receptors (ERRs) are founding members of the orphan nuclear receptor (ONR) subgroup of the nuclear receptor superfamily. Twenty-seven years of study have yet to identify cognate ligands for the ERRs, though they have firmly placed ERRα (ESRRA) and ERRγ (ESRRG) at the intersection of cellular metabolism and oncogenesis. The pace of discovery for novel functions of ERRβ (ESRRB), however, has until recently been somewhat slower than that of its family members. ERRβ has also been largely ignored in summaries and perspectives of the ONR literature. Here, we provide an overview of established and emerging knowledge of ERRβ in mouse, man, and other species, highlighting unique aspects of ERRβ biology that set it apart from the other two estrogen-related receptors, with a focus on the impact of alternative splicing on the structure and function of this receptor.

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