Accessibility navigation


Thyroid hormone can increase estrogen-mediated transcription from a consensus estrogen response element in neuroblastoma cells

Zhao, X., Lorenc, H., Stephenson, H., Wang, Y. J., Witherspoon, D., Katzenellenbogen, B., Pfaff, D. and Vasudevan, N. (2005) Thyroid hormone can increase estrogen-mediated transcription from a consensus estrogen response element in neuroblastoma cells. Proc Natl Acad Sci U S A, 102 (13). pp. 4890-5.

[img] Text - Accepted Version
· Restricted to Repository staff only
· The Copyright of this document has not been checked yet. This may affect its availability.

480kB

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=...

Abstract/Summary

Thyroid hormones (T) and estrogens (E) are nuclear receptor ligands with at least two molecular mechanisms of action: (i) relatively slow genomic effects, such as the regulation of transcription by cognate T receptors (TR) and E receptors (ER); and (ii) relatively rapid nongenomic effects, such as kinase activation and calcium release initiated at the membrane by putative membrane receptors. Genomic and nongenomic effects were thought to be disparate and independent. However, in a previous study using a two-pulse paradigm in neuroblastoma cells, we showed that E acting at the membrane could potentiate transcription from an E-driven reporter gene in the nucleus. Because both T and E can have important effects on mood and cognition, it is possible that the two hormones can act synergistically. In this study, we demonstrate that early actions of T via TRalpha1 and TRbeta1 can potentiate E-mediated transcription (genomic effects) from a consensus E response element (ERE)-driven reporter gene in transiently transfected neuroblastoma cells. Such potentiation was reduced by inhibition of mitogen-activated protein kinase. Using phosphomutants of ERalpha, we also show that probable mitogen-activated protein kinase phosphorylation sites on the ERalpha, the serines at position 167 and 118, are important in TRbeta1-mediated potentiation of ERalpha-induced transactivation. We suggest that crosstalk between T and E includes potential interactions through both nuclear and membrane-initiated molecular mechanisms of hormone signaling.

Item Type:Article
Refereed:Yes
Divisions:No Reading authors. Back catalogue items
ID Code:58928

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation