ArticleCancer letters2016
Progesterone receptor (PR) polyproline domain (PPD) mediates inhibition of epidermal growth factor receptor (EGFR) signaling in non-small cell lung cancer cells.
Article in Cancer letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The association between breast cancer and lung cancer: a bidirectional Mendelian randomization study.Scientific reports · 2024Article
- A molecular toolbox to study progesterone receptor signaling.Journal of mammary gland biology and neoplasia · 2023Article
- ATOH8 Expression Is Regulated by BMP2 and Plays a Key Role in Human Endometrial Stromal Cell Decidualization.Endocrinology · 2023Article
- Review
- The association between different hormone replacement therapy use and the incidence of lung cancer: a systematic review and meta-analysis.Journal of thoracic disease · 2022Article
- Article
- Triple SILAC identified progestin-independent and dependent PRA and PRB interacting partners in breast cancer.Scientific data · 2021Article
- Pan-Cancer Prognostic Role and Targeting Potential of the Estrogen-Progesterone Axis.Frontiers in oncology · 2021Article
- Hormone receptor expression correlates with EGFR gene mutation in lung cancer in patients with simultaneous primary breast cancer.Translational lung cancer research · 2020Article
- Progesterone receptor isoform B expression in pulmonary neuroendocrine cells decreases cell proliferation.The Journal of steroid biochemistry and molecular biology · 2019Article
- Extranuclear signaling by sex steroid receptors and clinical implications in breast cancer.Molecular and cellular endocrinology · 2018Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Recent evidence has suggested a possible role for progesterone receptor (PR) in the progression of non-small cell lung cancer (NSCLC). However, little is known concerning roles of PR in NSCLC. PR contains a polyproline domain (PPD), which directly binds to the SH3 domain of signaling molecules. Because PPD-SH3 interactions are essential for EGFR signaling, we hypothesized that the presence of PR-PPD interfered with EGFR-mediated signaling and cell proliferation. We examined the role of PR-PPD in cell proliferation and signaling by stably expressing PR-B, or PR-B with disrupting mutations in the PPD (PR-BΔSH3), from a tetracycline-regulated promoter in A549 NSCLC cells. PR-B dose-dependently inhibited cell growth in the absence of ligand, and progestin (R5020) treatment further suppressed the growth. Treatment with RU486 abolished PR-B- and R5020-mediated inhibition of cell proliferation. Expression of PR-BΔSH3 and treatment with R5020 or RU486 had no effect on cell proliferation. Furthermore, PR-B expression but not PR-BΔSH3 expression reduced EGF-induced A549 proliferation and activation of ERK1/2, in the absence of ligand. Taken together, our data demonstrated the significance of PR extranuclear signaling through PPD interactions in EGFR-mediated proliferation and signaling in NSCLC.
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