Photoaffinity labels for estrogen binding proteins of rat uterus

Katzenellenbogen, John A.; Johnson, Howard J.; Myers, Harvey N.

doi:10.1021/bi00745a010

Cited by 246 publications

(175 citation statements)

References 26 publications

(22 reference statements)

Supporting

Mentioning

173

Contrasting

Order By: Relevance

“…Both cell lines were maintained in estrogenized medium (i.e., phenol redcontaining RPMI 1640, 10% whole fetal bovine serum, 6 ng/mL insulin, 2 mmol/L glutamine, 100 Amol/L nonessential amino acids, and 100 units of penicillin and streptomycin per milliliter). Two days before reseeding of cells for an experiment, the medium was changed to phenol red-and estrogen-free medium containing charcoal-stripped fetal bovine serum (48). The monkey kidney COS-M6 cell line was cultured as previously described (8).…”

Section: Cell Linesmentioning

confidence: 99%

Estrogen-Related Receptor α1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway

Ariazi

Kraus

Farrell

et al. 2007

Molecular Cancer Research

105

106

View full text Add to dashboard Cite

We previously showed that (a) estrogen-related receptor A1 (ERRA1) down-modulates estrogen receptor (ER) -stimulated transcription in low ErbB2 -expressing MCF-7 mammary carcinoma cells, and (b) ERRA and ErbB2 mRNA levels positively correlate in clinical breast tumors. We show here that ERRA1 represses ERA-mediated activation in MCF-7 cells because it failed to recruit the coactivator glucocorticoid receptor interacting protein 1 (GRIP1) when bound to an estrogen response element. In contrast, ERRA1 activated estrogen response element -and ERR response element -mediated transcription in ERA-positive, high ErbB2 -expressing BT-474 mammary carcinoma cells, activation that was enhanced by overexpression of GRIP1. Likewise, regulation of the endogenous genes pS2, progesterone receptor, and ErbB2 by ERRA1 reflected the cell type -specific differences observed with our reporter plasmids. Importantly, overexpression of activated ErbB2 in MCF-7 cells led to transcriptional activation, rather than repression, by ERRA1. Two-dimensional PAGE of radiophosphate-labeled ERRA1 indicated that it was hyperphosphorylated in BT-474 relative to MCF-7 cells; incubation of these cells with anti-ErbB2 antibody led to reduction in the extent of ERRA1 phosphorylation. Additionally, mitogen-activated protein kinases (MAPK) and Akts, components of the ErbB2 pathway, phosphorylated ERRA1 in vitro. ERRA1-activated transcription in BT-474 cells was inhibited by disruption of ErbB2/epidermal growth factor receptor signaling with trastuzumab or gefitinib or inactivation of downstream components of this signaling, MAPK kinase/MAPK, and phosphatidylinositol-3-OH kinase/ Akt, with U0126 or LY294002, respectively. Thus, ERRA1 activities are regulated, in part, via ErbB2 signaling, with ERRA1 likely positively feedback-regulating ErbB2 expression. Taken together, we conclude that ERRA1 phosphorylation status shows potential as a biomarker of clinical course and antihormonal-and ErbB2-based treatment options, with ERRA1 serving as a novel target for drug development. (Mol Cancer Res 2007;5(1):71 -85)

show abstract

Section: Cell Linesmentioning

confidence: 99%

Estrogen-Related Receptor α1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway

Ariazi

Kraus

Farrell

et al. 2007

Molecular Cancer Research

105

106

View full text Add to dashboard Cite

show abstract

“…NaOH and is stable under the moderate-strong acidic conditions (19) . The O-alkylation of estrone with ethyl bromoacetate and sodium ethoxide provided ethyl estrone-3-oxymethylenecarboxylated which treated with 1M KOH and 1M HCL respectively to obtain estrone-3-oxymethylene carboxylic acid which coupled with NH TyrGly Gly phe-met OMe ester by amide bond in the presence of DCC and HOBt to offer Cterminal protective pentapeptide-estrone, which saponified and acidified by using 1N NaOH, and 1N HCL to give the goal analogue (20,21) .…”

Section: Methodsmentioning

confidence: 99%

“…Eestrone (1 mmol, 270 mg) was dissolve in minimum volume of [ethanol: tetrahydrofuran (THF)] (3.5:1) then sodium ethoxide (1.5 mmol; 0.75 ml of 2M in ethanol) and (3 mmol, 500 mg, 0.4 ml) of ethyl bromoacetate were added, the reaction mixture refluxed for 24 hr; An additional portion of sodium ethoxide and ethyl bromoacetate was added and refluxed continued for 2hr and the completion of reaction checked by TLC, the reaction mixture quenched in saturated NaCL, the product isolation by (ethylacetate-THF; MgSO 4 ) after this the solvent evaporated by vacuum and triturate the sticky residue with hexane several times to remove the small amount of contaminated ethyl bromoacetate to get white crystals which recrystalized from acetone-hexane (20) . Yield percent, physical appearance, melting point, R f value, and IR interpretation werelisted in Table (2).…”

Section: Synthesis Of Ethyl Estron-3-o-ylacetate (3-ocarbethoxymethylmentioning

confidence: 99%

“…The washed residue was dissolved in water and acidified with 0.1 N of HCL. The product isolation with (ether-THF; MgSO 4 ) to gave crude acid which recrtylized from benzene-ethylacetate (20) . Yield percent, physical appearance, melting point, R f v a l u e , I R i n t e r p r e t a t i o n , e l e m e n t a lmicroanalysis, and 1 H-NMR results were listed in Tables (2, 3, and 5) respectively.…”

Section: Synthesis Of Estrone-3-o-ylacetic Acid (3-ocarboxymethylestrmentioning

confidence: 99%

See 1 more Smart Citation

Synthesis of Estrone-Opioid Peptide Analogue With Expected Analgesic Activity

Al-Hamashi¹,

Saour²

2010

JNUS

View full text Add to dashboard Cite

The search for new peptides to be used as analgesics in place of morphine has been mainly directed to develop peptide analogues to have higher biological stability and receptor selectivity.Therefore extensive researches have been carried out on naturally occurring and synthetic opiates in order to enhance the analgesic potency, so we intended to prepare opioiod peptide analogue linked to estrone which may increase the analgesic effect of this compound. Steric hindrance clearly will be produced by estrone may affect the enzymatic activity on the synthesized analogue and this in turn may enhance the bioavailability of the analogue itself, meanwhile estrone may affect physicochemical properties of the analogue by increasing its lipophilicity and so facilitate its passage through the biological barriers, also estrone may affect receptor binding selectivity of this analogue and decrease the side effect of the original opioid peptide.The designed analogue is (estrone-3-O-acyl-tyr-gly-gly-phe-met-OH), where this opioid peptide synthesized following the conventional solution method, then linked to estrone by amide linkage and it was characterized using: thin layer chromatography (TLC), melting point, infrared spectroscopy (IR), elemental microanalysis(CHN), optical rotation, amino acid analysis, and hydrogen-nuclear magnetic resonance( 1 H-NMR).

show abstract

“…The data reported in Figure 4 are expressed as the relative binding affinity (RBA) values relative to estradiol, which is set at 100%. 20,21 The affinity of estradiol for the two receptors is high:…”

Section: Figurementioning

confidence: 99%

Salicylaldoximes and anthranylaldoximes as alternatives to phenol-based estrogen receptor ligands

Minutolo¹,

Bertini²,

Martinelli³

et al. 2006

Arkivoc

Self Cite

View full text Add to dashboard Cite

Estrogens play a crucial role in the development and function of female reproductive tissues. They have positive effects on the maintenance of bone mineral density, on the liver, and on the cardiovascular and central nervous systems.Selective Estrogen Receptor Modulators (SERMs) are particularly attractive as therapeutic agents because they are able to block estrogen action at those sites where stimulation would be undesirable, such as the breast and uterus, but at the same time stimulate estrogen actions in other tissues where they are desired, such as the bone and liver.Most synthetic estrogen receptor ligands possess a phenolic ring, mimicking the phenolic "Aring" of the natural ligand estradiol.In an attempt to increase the structural diversity of estrogen receptor (ER) ligands, we designed and synthesized molecules containing unprecedented replacements of the prototypical phenolic "A-ring" of estrogens with an oxime and a hydroxy-(salicylaldoximes) or aminomoieties (anthranylaldoximes), forming intramolecularly H-bonded pseudocycles. These new classes of compounds showed interesting ER binding properties on both receptor subtypes (ERα and ERβ). These results proved that the six-membered ring formed by an intramolecular hydrogen bond, and containing an exocyclic oxime OH, is an effective stereoelectronic replacement of the phenolic ring of typical ER ligands.

show abstract

Photoaffinity labels for estrogen binding proteins of rat uterus

Cited by 246 publications

References 26 publications

Estrogen-Related Receptor α1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway

Estrogen-Related Receptor α1 Transcriptional Activities Are Regulated in Part via the ErbB2/HER2 Signaling Pathway

Synthesis of Estrone-Opioid Peptide Analogue With Expected Analgesic Activity

Salicylaldoximes and anthranylaldoximes as alternatives to phenol-based estrogen receptor ligands

Contact Info

Product

Resources

About