A Theoretical Insight into the Interaction of Fatty Acids Involved in Royal Jelly with the Human Estrogen Receptor β

2008 ◽  
Vol 81 (10) ◽  
pp. 1258-1266 ◽  
Author(s):  
Toshiaki Matsubara ◽  
Hiroyuki Sugimoto ◽  
Misako Aida
Keyword(s):  
Fatty Acids ◽  
Estrogen Receptor ◽  
Royal Jelly ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor ◽  
Theoretical Insight ◽  
Insight Into

scholarly journals Human Estrogen Receptor β Binds DNA in a Manner Similar to and Dimerizes with Estrogen Receptor α

1997 ◽  
Vol 272 (41) ◽  
pp. 25832-25838 ◽  
Author(s):  
Paul Pace ◽  
Jacqueline Taylor ◽  
Sumathy Suntharalingam ◽  
R. Charles Coombes ◽  
Simak Ali
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor

scholarly journals Fatty Acids Derived from Royal Jelly Are Modulators of Estrogen Receptor Functions

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e15594 ◽  
Author(s):  
Paraskevi Moutsatsou ◽  
Zoi Papoutsi ◽  
Eva Kassi ◽  
Nina Heldring ◽  
Chunyan Zhao ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Estrogen Receptor ◽  
Royal Jelly

Cloning and Characterization of Human Estrogen Receptor β Promoter

2000 ◽  
Vol 275 (2) ◽  
pp. 682-689 ◽  
Author(s):  
Long-Cheng Li ◽  
Che-Chung Yeh ◽  
Dana Nojima ◽  
Rajvir Dahiya
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Β ◽  
Human Estrogen Receptor

scholarly journals Human Estrogen Receptor β 548 Is Not a Common Variant in Three Distinct Populations

Endocrinology ◽  
2003 ◽  
Vol 144 (8) ◽  
pp. 3541-3546 ◽  
Author(s):  
Li Xu ◽  
Qiang Pan-Hammarström ◽  
Asta Försti ◽  
Kari Hemminki ◽  
Lennart Hammarström ◽  
...  
Keyword(s):  
Amino Acids ◽  
Estrogen Receptor ◽  
Base Pair ◽  
Estrogen Receptor Β ◽  
Common Variant ◽  
Human Populations ◽  
Functional Characteristics ◽  
Human Estrogen Receptor

Abstract Several isoforms of estrogen receptor (ER) β (also known as NR3A2) have been reported, including variants with different N-terminal ends. In rodents, two in-frame initiation codons (ATGs) are used to produce proteins of 530 and 549 amino acids, respectively. In humans, the upstream ATG is out of frame in all clones reported, until recently, when human clones with an extra A-T base pair placing the upstream ATG in frame were reported. The authors suggested that this could represent a novel polymorphism in the ERβ gene. Because human ERβ548 (hERβ548) and hERβ530 display different functional characteristics in vitro, it is of interest to determine if this variant constitutes a polymorphism in human populations. We therefore determined the frequency of this novel isoform in several populations including African (n = 96), Caucasian (n = 100), and Asian (n = 128) subjects using denaturing HPLC. We did not detect any alleles that correspond to hERβ548 in these samples or in additional samples of heterogeneous origin. It is concluded that hERβ548 is not a common variant in Africans, Caucasians, or Asians.

scholarly journals Induction of Estrogen Receptor β-mediated Autophagy Sensitizes Breast Cancer Cells to TAD1822-7, a Novel Biphenyl Urea Taspine Derivative

2021 ◽  
Author(s):  
Qi Su ◽  
Qing Wu ◽  
Kun Chen ◽  
Jingjing Wang ◽  
Ammar Sarwar ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Death ◽  
Estrogen Receptor ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Annexin V ◽  
Female Breast Cancer ◽  
Estrogen Receptor Β ◽  
Inhibitory Effects ◽  
Insight Into

Abstract Female breast cancer has become the most commonly diagnosed cancer worldwide. As a tumor suppressor, estrogen receptor β (ERβ) is a potential target for breast cancer therapy. TAD1822-7 was evaluated for ERβ-mediated autophagy and cell death using cell proliferation assay, Annexin V/PI staining, immunofluorescence, western blotting and hypoxia cell models. TAD1822-7 upregulated ERβ causing cell death and induced mitochondrial dysfunction and autophagy companied with mitochondrial located ERβ. Enhanced levels of LC3-II and p62 indicated that TAD1822-7 blocked the late-stage autolysosome formation, leading to cell death. Mechanistically, TAD1822-7-induced cell death was mediated by PI3K/AKT signaling pathways. Moreover, TAD1822-7 modulated HIF functions and autophagy via the inhibition of HIF-1β in the context of hypoxia-induced autophagy. TAD1822-7 inhibited hypoxia-inducted autophagy and PI3K/AKT pathway. These findings provide new insight into the mechanism underlying the inhibitory effects of TAD1822-7 via ERβ-mediated pathways in breast cancer cells.

Sign in / Sign up

Export Citation Format

Share Document