The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Plasma membrane localization and function of the estrogen receptor α variant (ER46) in human endothelial cells
Open accessAbstract
Estrogen receptor (ER) α variants have been identified in an array of nonendothelial cells. We previously demonstrated that estrogen rapidly induces nitric oxide release via a phosphatidylinositol 3-kinase/Akt/endothelial nitric-oxide synthase (eNOS) pathway in EA.hy926 cells (immortalized human endothelial cells), which express a 46-kDa ER. We now confirm that, due to alternative splicing, the 46-kDa endothelial cell protein (ER46) is an amino-terminal truncated product of full-length ERα (ER66). ER46 is expressed in the plasma membrane, cytosol, and nucleus of resting, estrogen-deprived cells. Flow cytometric and immunofluorescence microscopic analyses demonstrated that the ER46 C but not N terminus is Ab-accessible in the plasma membrane. Inhibition of palmitoylation with tunicamycin and [3 H]palmitic acid labeling demonstrated an estrogen-induced, palmitoylation-dependent plasma membrane ER46 recruitment, with reorganization into caveolae. In reconstituted, estrogen-stimulated COS-7 (ER-null) cells, membrane ER46 more efficiently triggered membrane eNOS phosphorylation than ER66. Conversely, ER66 more efficiently mediated estrogen response element reporter-gene transactivation than ER46. These results demonstrate that ER46 is localized and further dynamically targeted to the plasma membrane in a palmitoylation-dependent manner. ER46 more efficiently modulates membrane-initiated estrogen actions, including eNOS activation, than full-length ER66. These findings may have important implications in vascular-specific targeting of estrogen receptor agonists.
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Self-citationSynaptic Strength Regulated by Palmitate Cycling on PSD-95
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Heldring, N., Pike, A., Andersson, S., Matthews, J., Cheng, G., Hartman, J., Tujague, M., Ström, A., Treuter, E., Warner, M., et al. (2007) · Physiological Reviews · doi:10.1152/physrev.00026.2006 · Cited by 1,857
Estrogen receptor signaling mechanisms
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Integration of the extranuclear and nuclear actions of estrogen
Levin, E. R. (2005) · Molecular Endocrinology · doi:10.1210/me.2004-0390 · Cited by 708
Mechanisms of tamoxifen resistance
Ring, A., & Dowsett, M. (2004) · Endocrine-Related Cancer · doi:10.1677/erc.1.00776 · Cited by 651
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Metadata
- Authors
- Li, L., Haynes, M. P., & Bender, J. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-04-07
- Volume
- 100
- Issue
- 8
- Pages
- 4807-4812
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1982365009
- Cited by
- 465
- References
- 31
- FWCI
- 18.08
- Type
- journal article
- Language
- en
- Open access
- green
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