Binding of MCF-7 cell mitochondrial proteins and recombinant human estrogen receptors ? and ? to human mitochondrial dna estrogen response elements

2004 ◽  
Vol 93 (2) ◽  
pp. 358-373 ◽  
Author(s):  
Jin Q. Chen ◽  
Matthewos Eshete ◽  
William L. Alworth ◽  
James D. Yager
Keyword(s):  
Mitochondrial Dna ◽  
Estrogen Receptors ◽  
Mitochondrial Proteins ◽  
Human Mitochondrial Dna ◽  
Response Elements ◽  
Estrogen Response ◽  
Estrogen Response Elements ◽  
Mcf 7

scholarly journals Calmodulin Is a Selective Modulator of Estrogen Receptors

2002 ◽  
Vol 16 (5) ◽  
pp. 947-960 ◽  
Author(s):  
Juana M. García Pedrero ◽  
Beatríz del Rio ◽  
Carlos Martínez-Campa ◽  
Masami Muramatsu ◽  
Pedro S. Lazo ◽  
...  
Keyword(s):  
Estrogen Receptors ◽  
Hela Cells ◽  
Estrogen Response Element ◽  
Activator Protein 1 ◽  
Response Elements ◽  
Transactivation Activity ◽  
Estrogen Response ◽  
Lysine Residues ◽  
Estrogen Response Elements ◽  
Mcf 7

Abstract In the search for differences between ERα and ERβ, we analyzed the interaction of both receptors with calmodulin (CaM) and demonstrated that ERα but not ERβ directly interacts with CaM. Using transiently transfected HeLa cells, we examined the effect of the CaM antagonist N-(6-aminohexyl)-5-chloro-naphthalene sulfonilamide hydrochloride (W7) on the transactivation properties of ERα and ERβ in promoters containing either estrogen response elements or activator protein 1 elements. Transactivation by ERα was dose-dependently inhibited by W7, whereas that of ERβ was not inhibited or even activated at low W7 concentrations. In agreement with these results, transactivation of an estrogen response element containing promoter in MCF-7 cells (which express a high ERα/ERβ ratio) was also inhibited by W7. In contrast, transactivation in T47D cells (which express a low ERα/ERβ ratio) was not affected by this CaM antagonist. The sensitivity of MCF-7 cells to W7 was abolished when cells were transfected with increasing amounts of ERβ, indicating that the sensitivity to CaM antagonists of estrogen-responsive tissues correlates with a high ERα/ERβ ratio. Finally, substitution of lysine residues 302 and 303 of ERα for glycine rendered a mutant ERα unable to interact with CaM whose transactivation activity became insensitive to W7. Our results indicate that CaM antagonists are selective modulators of ER able to inhibit ERα-mediated activity, whereas ERβ actions were not affected or even potentiated by W7.

Interaction of estrogen receptors α and β with estrogen response elements

2001 ◽  
Vol 181 (1-2) ◽  
pp. 151-163 ◽  
Author(s):  
Margaret A. Loven ◽  
Jennifer R. Wood ◽  
Ann M. Nardulli
Keyword(s):  
Estrogen Receptors ◽  
Response Elements ◽  
Estrogen Response ◽  
Estrogen Response Elements

scholarly journals Two functional estrogen response elements are located upstream of the major chicken vitellogenin gene.

1988 ◽  
Vol 8 (3) ◽  
pp. 1123-1131 ◽  
Author(s):  
J B Burch ◽  
M I Evans ◽  
T M Friedman ◽  
P J O'Malley
Keyword(s):  
Essential Feature ◽  
Coding Region ◽  
Transient Expression Assay ◽  
Specific Expression ◽  
Response Elements ◽  
Estrogen Response ◽  
Pair Sequence ◽  
Estrogen Response Elements ◽  
Vitellogenin Gene ◽  
Simplex Virus

We used a transient-expression assay to identify two estrogen response elements (EREs) associated with the major chicken vitellogenin gene (VTGII). Each element was characterized by its ability to confer estrogen responsiveness when cloned in either orientation next to a chimeric reporter gene consisting of the herpes simplex virus thymidine kinase promoter and the chloramphenicol acetyl transferase-coding region. Deletion analyses indicated that sequences necessary for the distal ERE resided within the region from -626 to -613 (nucleotide positions relative to the VTGII start site) whereas those necessary for the proximal ERE were within the region from -358 to -335. These distal and proximal elements contain, respectively, a perfect copy and an imperfect copy of the 13-base-pair sequence that is an essential feature of the EREs associated with two frog vitellogenin genes. These chicken VTGII EREs mapped near regions that were restructured at the chromatin level when the endogenous VTGII gene was expressed in the liver in response to estradiol. These data suggest a model for the tissue-specific expression of this estrogen-responsive gene.

scholarly journals Human URAT1/SLC22A12 gene promoter is regulated by 27-hydroxycholesterol through estrogen response elements

2019 ◽  
Author(s):  
Masaya Matsubayashi ◽  
Yoshihiko M. Sakaguchi ◽  
Yoshiki Sahara ◽  
Hitoki Nanaura ◽  
Sotaro Kikuchi ◽  
...  
Keyword(s):  
Uric Acid ◽  
Serum Uric Acid ◽  
Cholesterol Metabolism ◽  
Gene Promoter ◽  
Human Kidney ◽  
Response Elements ◽  
Estrogen Response ◽  
Uric Acid Transporters ◽  
Estrogen Response Elements ◽  
Phylogenic Relationship

AbstractElevated levels of uric acid, a metabolite of purine in humans, is related to various diseases, such as gout, atherosclerosis and renal dysfunction. The excretion and reabsorption of uric acid to/from urine is tightly regulated by uric acid transporters. The amino acid sequences of uric acid reabsorption transporters, URAT1/SLC22A12, OAT4/SLC22A11, and OAT10/SLC22A13, share closer phylogenic relationship, whereas the gene promoter sequences are distant phylogenic relationship. Through the single-cell RNA-sequencing analysis of an adult human kidney, we found that only a small number of cells express these transporters, despite their role in the regulation of serum uric acid levels. Transcriptional motif analysis on these transporter genes, revealed that the URAT1/SLC22A12 gene promoter displayed the most conserved estrogen response elements (EREs) among the three transporters. The endogenous selective estrogen receptor modulator (SERM) 27-hydroxycholesterol (27HC) had positive effects on the transcriptional activity of URAT1/SLC22A12. We also found that 27HC increased the protein and gene expression of URAT1/SLC22A12 in mouse kidneys and human kidney organoids, respectively. These results strongly suggest the role of 27HC for URAT1/SLC22A12 expression in renal proximal tubules and upregulation of serum uric acid levels and also show the relationship between cholesterol metabolism and serum uric acid regulation.Significance StatementThe elevated levels of serum uric acid cause various diseases, and the excretion/reabsorption of uric acid to/from urine is tightly regulated by the uric acid transporters. We found that despite the role in serum uric acid regulation, only a small number of cells express URAT1/SLC22A12. We also found that URAT1/SLC22A12 gene promoter region has effective estrogen response elements, and endogenous selective estrogen receptor (ER) modulator 27-hydroxycholesterol (27HC) increased URAT1/SLC22A12 expression in the mice kidneys and human kidney organoids. These suggest that 27HC increases URAT1/SLC22A12 expression and upregulate serum uric acid levels. Since 27HC connects cholesterol metabolism, our study indicates the important link between cholesterol metabolism and serum uric acid regulation, and also provides a novel therapeutic approach to hyperuricemia.

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