ER alpha 17p, a peptide reproducing the hinge region of the estrogen receptor alpha associates to biological membranes: A biophysical approach

作者：Byrne Cillian; Khemtemourian Lucie; Pelekanou Vassiliki; Kampa Marilena; Leclercq Guy; Sagan Sandrine; Castanas Elias; Burlina Fabienne; Jacquot Yves^*

来源：Steroids, 2012, 77(10): 979-987.

DOI：10.1016/j.steroids.2012.02.022

• Peptide
• Estrogen receptor
• Membrane interaction
• Cellular internalization

Recently, we identified a peptide (ER alpha 17p, P(295)LMIKRSKKNSLALSLT(311)) that corresponds to the 295-311 sequence of the estrogen receptor a (ER alpha, hinge region) and which exerts a panel of pharmacological effects in breast cancer cells. Remarkably, these effects can result from the interaction of ER alpha 17p with the plasma membrane. Herein, we show that ER alpha 17p adopts a beta-sheet secondary structure when in contact with anionic phospholipids and that it is engulfed within the lipid bilayer. While ER alpha 17p increases the fluidity of membrane mimics, it weakly internalizes in living cells. In light of the above, one may evoke one important role of the 295-311 region of the ER alpha: the corresponding peptide could be secreted/delivered to the extracellular medium to interact with neighboring cells, both intracellularly and at the membrane level. Finally, the 295-311 region of ER alpha being in proximity to the cystein-447, the palmitoylation site of the ERa raises the question of its involvement in the interaction/stabilization of the protein with the membrane.

• 出版日期2012-8