The Affinity and Activity of the Multiple Hormone Response Element in the Proximal Promoter of the Human Oxytocin Gene

Stedronsky, Katrin; Telgmann, Ralph; Tillmann, G.; Walther, Norbert; Ivell, Richard

doi:10.1046/j.1365-2826.2002.00799.x

Cited by 34 publications

(26 citation statements)

References 60 publications

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“…In certain of these organs, estrogen regulates OT and/or OTR expression (15,16). Likewise, we found that OT is produced in abundance by bone marrow osteoblasts in response to estrogen, with the potential of exerting an anabolic effect on the skeleton (17).…”

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confidence: 64%

Bone Marrow Oxytocin Mediates the Anabolic Action of Estrogen on the Skeleton

Colaianni

Sun

Benedetto

et al. 2012

Journal of Biological Chemistry

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Background:The mechanism underlying the anabolic effect of estrogen on the skeleton is unclear. Results: We report that estrogen-induced bone formation in mice occurs through oxytocin (OT) produced by osteoblasts in bone marrow. Conclusion: Feed-forward OT release in bone marrow by a rising estrogen level may facilitate rapid skeletal recovery after lactation. Significance: The study highlights a novel mechanism for estrogen action on bone.

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confidence: 64%

Bone Marrow Oxytocin Mediates the Anabolic Action of Estrogen on the Skeleton

Colaianni

Sun

Benedetto

et al. 2012

Journal of Biological Chemistry

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“…To examine these in vivo associations, we performed a chromatin immunoprecipitation assay by using full-length hER␣ in MCF7 cells, spliceosome complex components, and a gene promoter region from human oxytocin that contained an estrogen-responsive element (26). Upon 17␤-estradiol (E2) stimulation, the SF3a subunits and hER␣ all were recruited to the oxytocin promoter along with RNA polymerase II (Fig.…”

Section: Resultsmentioning

confidence: 99%

Splicing potentiation by growth factor signals via estrogen receptor phosphorylation

Masuhiro

Mezaki²,

Sakari³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Mitogen-activated protein kinase-mediated growth factor signals are known to augment the ligand-induced transactivation function of nuclear estrogen receptor ␣ (ER␣) through phosphorylation of Ser-118 within the ER␣ N-terminal transactivation (activation function-1) domain. We identified the spliceosome component splicing factor (SF)3a p120 as a coactivator specific for human ER␣ (hER␣) activation function-1 that physically associated with ER␣ dependent on the phosphorylation state of Ser-118. SF3a p120 potentiated hER␣-mediated RNA splicing, and notably, the potentiation of RNA splicing by SF3a p120 depended on hER Ser-118 phosphorylation. Thus, our findings suggest a mechanism by which growth factor signaling can regulate gene expression through the modulation of RNA splicing efficiency via phosphorylation of sequencespecific activators, after association between such activators and the spliceosome.nuclear receptor ͉ estrogen ͉ coactivator ͉ mitogen-activated protein kinase ͉ RNA splicing M ost of the actions of estrogen are thought to be mediated via the transcriptional control of target genes by nuclear estrogen receptors (ER) ␣ and ␤, members of the steroid hormone receptor gene superfamily that act as ligand-inducible transcription factors. ERs bind as dimers to specific estrogen response elements in the promoters of some target genes (1). However, most ER target promoters appear to recruit ERs without specific DNA binding, presumably through associations with sequence-specific factors bound to the promoters (2). ERs contain two transactivation functions (AFs), AF-1 in the Nterminal A͞B domain and AF-2 in the C-terminal ligand-binding E͞F domain. Ligand-induced transactivation by ERs requires multiple distinct classes of coactivator complexes, as well as a number of coregulators. The best-characterized complex contains p160͞SRC family proteins (3, 4) and CBP͞p300 histone acetyltransferases (5, 6), along with the RNA coactivator steroid receptor RNA activator (7) and presumably other known and unknown coactivators (8, 9). Another histone acetyltransferasescontaining complex, the TBP-free TAF II -containing (TFTC)-like complex (10), can also coactivate ER transactivation, as can the nonhistone acetyltransferases DRIP (VDR interacting protein)͞TRAP (thyroid hormone receptor-associated protein)͞ SMCC (SRB͞MED cofactor complexes)͞ARC (activatorrecruited cofactor) complex (11-13).ER-mediated estrogen signaling is known to involve cross-talk with other signaling pathways (14). For instance, growth factors potentiate estrogen-induced cellular proliferation in female reproductive tissues (15). Phosphorylation of the Ser-118 residue in the human ER␣ (hER␣) A͞B domain by mitogen-activated protein kinase (MAPK) activated by growth factors (16, 17) and cyclin-dependent kinase-7 (18) results in the potentiation of AF-1 function (16). However, the molecular basis of ER␣ AF-1 potentiation by MAPK-mediated phosphorylation remains unclear. In a previous study, we identified the DEAD-box RNA helicase subfamily member p68͞p72...

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“…Initially, it was believed that OXT expression was directly regulated by the binding of estrogen to ERE in the promoter region (42,46). However, this mechanism is now in doubt as the ERE in the promoter of OXT is not a good match to the ERE consensus sequence (51,29). Induction of OXT Fig.…”

Section: Discussionmentioning

confidence: 99%

Chronic exposure to anabolic steroids induces the muscle expression of oxytocin and a more than fiftyfold increase in circulating oxytocin in cattle

Jager

Hudson

Reverter

et al. 2011

Physiological Genomics

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Chronic exposure to anabolic steroids induces the muscle expression of oxytocin and a more than fiftyfold increase in circulating oxytocin in cattle. Physiol Genomics 43: 467-478, 2011. First published February 15, 2011 doi:10.1152/physiolgenomics.00226.2010.-Molecular mechanisms in skeletal muscle associated with anabolic steroid treatment of cattle are unclear and we aimed to characterize transcriptional changes. Cattle were chronically exposed (68 Ϯ 20 days) to a steroid hormone implant containing 200 mg trenbolone acetate and 20 mg estradiol (Revalor-H). Biopsy samples from 48 cattle (half treated) from longissimus dorsi (LD) muscle under local anesthesia were collected. Gene expression levels were profiled by microarray, covering 16,944 unique bovine genes: 121 genes were differentially expressed (DE) due to the implant (99.99% posterior probability of not being false positives). Among DE genes, a decrease in expression of a number of fat metabolism-associated genes, likely reflecting the lipid storage activity of intramuscular adipocytes, was observed. The expression of IGF1 and genes related to the extracellular matrix, slow twitch fibers, and cell cycle (including SOX8, a satellite cell marker) was increased in the treated muscle. Unexpectedly, a very large 21-(microarray) to 97 (real time quantitative PCR)-fold higher expression of the mRNA encoding the neuropeptide hormone oxytocin was observed in treated muscle. We also observed an ϳ50-fold higher level of circulating oxytocin in the plasma of treated animals at the time of biopsy. Using a coexpression network strategy OXTR was identified as more likely than IGF1R to be a major mediator of the muscle response to Revalor-H. A re-investigation of in vivo cattle LD muscle samples during early to mid-fetal development identified a Ͼ128-fold increased expression of OXT, coincident with myofiber differentiation and fusion. We propose that oxytocin may be involved in mediating the anabolic effects of Revalor-H treatment.

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The Affinity and Activity of the Multiple Hormone Response Element in the Proximal Promoter of the Human Oxytocin Gene

Cited by 34 publications

References 60 publications

Bone Marrow Oxytocin Mediates the Anabolic Action of Estrogen on the Skeleton

Bone Marrow Oxytocin Mediates the Anabolic Action of Estrogen on the Skeleton

Splicing potentiation by growth factor signals via estrogen receptor phosphorylation

Chronic exposure to anabolic steroids induces the muscle expression of oxytocin and a more than fiftyfold increase in circulating oxytocin in cattle

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