scholarly journals 17β-estradiol regulation of the mRNA expression of t-type calcium channel subunits: Role of estrogen receptor α and estrogen receptor β

2009 ◽  
Vol 512 (3) ◽  
pp. 347-358 ◽  
Author(s):  
Martha A. Bosch ◽  
Jingwen Hou ◽  
Yuan Fang ◽  
Martin J. Kelly ◽  
Oline K. RØnnekleiv
Keyword(s):  
Estrogen Receptor ◽  
Calcium Channel ◽  
Mrna Expression ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
17Β Estradiol

Prognostic Role of Estrogen Receptor α and Estrogen Receptor β in Gastric Cancer

2010 ◽  
Vol 17 (9) ◽  
pp. 2503-2509 ◽  
Author(s):  
C. Y. Xu ◽  
J. L. Guo ◽  
Z. N. Jiang ◽  
S. D. Xie ◽  
J. G. Shen ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
Prognostic Role

scholarly journals Palmitoylation-dependent Estrogen Receptor α Membrane Localization: Regulation by 17β-Estradiol

2005 ◽  
Vol 16 (1) ◽  
pp. 231-237 ◽  
Author(s):  
Filippo Acconcia ◽  
Paolo Ascenzi ◽  
Alessio Bocedi ◽  
Enzo Spisni ◽  
Vittorio Tomasi ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Estrogen Receptor ◽  
Plasma Membrane ◽  
Estrogen Receptor Α ◽  
Membrane Localization ◽  
Target Cells ◽  
Dependent Manner ◽  
Caveolin 1 ◽  
17Β Estradiol

A fraction of the nuclear estrogen receptor α (ERα) is localized to the plasma membrane region of 17β-estradiol (E2) target cells. We previously reported that ERα is a palmitoylated protein. To gain insight into the molecular mechanism of ERα residence at the plasma membrane, we tested both the role of palmitoylation and the impact of E2 stimulation on ERα membrane localization. The cancer cell lines expressing transfected or endogenous human ERα (HeLa and HepG2, respectively) or the ERα nonpalmitoylable Cys447Ala mutant transfected in HeLa cells were used as experimental models. We found that palmitoylation of ERα enacts ERα association with the plasma membrane, interaction with the membrane protein caveolin-1, and nongenomic activities, including activation of signaling pathways and cell proliferation (i.e., ERK and AKT activation, cyclin D1 promoter activity, DNA synthesis). Moreover, E2 reduces both ERα palmitoylation and its interaction with caveolin-1, in a time- and dose-dependent manner. These data point to the physiological role of ERα palmitoylation in the receptor localization to the cell membrane and in the regulation of the E2-induced cell proliferation.

Mechanisms of membrane estrogen receptor-α-mediated rapid stimulation of Ca2+ levels and prolactin release in a pituitary cell line

2005 ◽  
Vol 288 (2) ◽  
pp. E388-E397 ◽  
Author(s):  
Nataliya N. Bulayeva ◽  
Ann L. Wozniak ◽  
L. Leanne Lash ◽  
Cheryl S. Watson
Keyword(s):  
Estrogen Receptor ◽  
Cell Line ◽  
Estrogen Receptor Α ◽  
Signaling Mechanism ◽  
Signaling Mechanisms ◽  
Intracellular Ca ◽  
A Cell ◽  
17Β Estradiol ◽  
Rapid Stimulation

The role of membrane estrogen receptor-α (mERα) in rapid nongenomic responses to 17β-estradiol (E2) was tested in sublines of GH3/B6 rat prolactinoma cells selected for high (GH3/B6/F10) and low (GH3/B6/D9) mERα expression. E2 elicited rapid, concentration-dependent intracellular Ca2+ concentration ([Ca2+]i) increases in the F10 subline. Lack of inhibition by thapsigargin depletion of intracellular Ca2+ pools, together with abrogation of the response in Ca2+-free medium, suggested an extracellular source of Ca2+ for this response. The participation of voltage-dependant channels in the E2-induced [Ca2+]i increase was confirmed by the specific L-type Ca2+ channel inhibitor nifedipine. For comparison, the D9 mERα-depleted subline was insensitive to steroid action via this signaling mechanism. [Ca2+]i elevation was correlated with prolactin (PRL) release in the F10 cell line in as little as 3 min. E2 caused a much higher PRL release than KCl treatment (which caused maximal Ca2+ elevation), suggesting that secretion was also controlled by additional mechanisms. Participation of mERα in these effects was confirmed by the ability of E2-peroxidase (a cell-impermeable analog of E2) to cause these responses, blockage of the responses with the ER antagonist ICI 182 780, and the inability of the E2 stereoisomer 17α-E2 to elicit a response. Thus rapid exocytosis of PRL is regulated in these cells by mERα signaling to specific Ca2+ channels utilizing extracellular Ca2+ sources and additional signaling mechanisms.

scholarly journals The Role of Steroid Hormone Receptors in Urothelial Tumorigenesis

Cancers ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2155
Author(s):  
Hiroki Ide ◽  
Hiroshi Miyamoto
Keyword(s):  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Glucocorticoid Receptor ◽  
Hormone Receptors ◽  
Steroid Hormone ◽  
Tumor Development ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
Steroid Hormone Receptors

Preclinical and/or clinical evidence has indicated a potential role of steroid hormone-mediated signaling pathways in the development of various neoplastic diseases, while precise mechanisms for the functions of specific receptors remain poorly understood. Specifically, in urothelial cancer where sex-related differences particularly in its incidence are noted, activation of sex hormone receptors, such as androgen receptor and estrogen receptor-β, has been associated with the induction of tumor development. More recently, glucocorticoid receptor has been implied to function as a suppressor of urothelial tumorigenesis. This article summarizes and discusses available data suggesting that steroid hormone receptors, including androgen receptor, estrogen receptor-α, estrogen receptor-β, glucocorticoid receptor, progesterone receptor and vitamin D receptor, as well as their related signals, contribute to modulating urothelial tumorigenesis.

Dilatory responses to estrogenic compounds in small femoral arteries of male and female estrogen receptor-β knockout mice

2006 ◽  
Vol 290 (2) ◽  
pp. H823-H829 ◽  
Author(s):  
Maria Natalia Cruz ◽  
Gillian Douglas ◽  
Jan-Å Gustafsson ◽  
Lucilla Poston ◽  
Karolina Kublickiene
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Estrogen Receptor Β ◽  
Response Curves ◽  
Estrogenic Compounds ◽  
Male And Female ◽  
Femoral Arteries ◽  
Before And After ◽  
17Β Estradiol ◽  
Isolated Arteries

The objectives of this study were to determine whether acute dilatory responses to estrogen receptor agonists are altered in isolated arteries from estrogen receptor β-deficient mice (β-ERKO) and to gain insight into the role of nitric oxide (NO) in these responses. Femoral arteries (∼250 μm) from male and female β-ERKO mice and wild-type (WT) littermates (26 female, 13 in each group; and 24 male, 12 in each group) were mounted on a Multi-Myograph. Concentration-response curves to 17β-estradiol (17β-E2) and the selective estrogen receptor-α (ER-α) agonist propyl-[1H]-pyrazole-1,3,5-triy-trisphenol (PPT) were obtained before and after NO synthase (NOS) inhibition [ Nω-nitro-l-arginine methyl ester (l-NAME), 0.1 mM] in arteries preconstricted with U-46619 (a thromboxane analog). In WT mice, responses to the potent estrogen receptor-β (ER-β) agonist 2,3-bis(4-hydroxyphenyl)-propionitrile (DPN) and the contribution of NO were also assessed. Concentration-response curves to 17β-E2 and PPT were similar in arteries from WT and β-ERKO mice of both genders, but NO-mediated relaxation was different, since l-NAME reduced 17β-E2 mediated relaxation in arteries from male and female β-ERKO but not WT mice ( P < 0.05). NOS inhibition reduced dilation to PPT in arteries from male and female WT mice, as well as arteries from female β-ERKO mice ( P < 0.05). Responses to DPN in arteries from WT female and male mice did not differ after NOS inhibition. The acute dilatory responses to estrogenic compounds are similar in WT and β-ERKO mice but differ mechanistically. Because NO appeared to contribute to responses to 17β-E2 in arteries from β-ERKO but not WT mice, the presence of ER-β apparently inhibits ER-α-mediated NO relaxation.

Estrogen receptor-β mediates male-female differences in the development of pressure overload hypertrophy

2005 ◽  
Vol 288 (2) ◽  
pp. H469-H476 ◽  
Author(s):  
Maryanne Skavdahl ◽  
Charles Steenbergen ◽  
James Clark ◽  
Page Myers ◽  
Tracy Demianenko ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Weight Ratio ◽  
Pressure Overload ◽  
Estrogen Receptor Α ◽  
Epidemiological Studies ◽  
Estrogen Receptor Β ◽  
Heart Weight ◽  
Receptor Subtypes ◽  
Lung Weight

The goal of this study was to determine the role of estrogen receptor subtypes in the development of pressure overload hypertrophy in mice. Epidemiological studies have suggested gender differences in the development of hypertrophy and heart disease, but the mechanism and the role of estrogen receptor subtypes are not established. We performed transverse aortic constriction (TAC) and sham operations in male and female wild-type (WT) mice and mice lacking functional estrogen receptor-α [α-estrogen receptor knockout (α-ERKO)] and mice lacking estrogen receptor-β (β-ERKO). Body, heart, and lung weights were measured 2 wk postsurgery. WT male mice subjected to TAC showed a 64% increase in the heart weight-to-body weight ratio (HW/BW) compared with sham, and WT males have increased lung weight at 2 wk. WT female mice subjected to TAC showed a 31% increase in HW/BW compared with sham, which was significantly less than their male counterparts and with no evidence of heart failure. α-ERKO females developed HW/BW nearly identical to that seen in WT littermate females in response to TAC, indicating that estrogen receptor-α is not essential for the attenuation of hypertrophy observed in WT females. In contrast, β-ERKO females responded to TAC with a significantly greater increase in HW/BW than WT littermate females. β-ERKO females have lower expression of lipoprotein lipase at baseline than WT or α-ERKO females. These data suggest an important role for estrogen receptor-β in attenuating the hypertrophic response to pressure overload in females.

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