ArticleHormones & cancer2018
O-GlcNAc-Dependent Regulation of Progesterone Receptor Function in Breast Cancer.
Article in Hormones & cancer, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Protein O-GlcNAcylation in reproductive biology and the impact of metabolic disease.Human reproduction update · 2025Review
- O-GlcNAcylation in Endocrinology: The Sweet Link.Endocrinology · 2025Review
- Site-specific O-GlcNAcylation of progesterone receptor (PR) supports PR attenuation of interferon stimulated genes (ISGs) and tumor growth in breast cancer.The Journal of biological chemistry · 2024Article
- A GREB1-steroid receptor feedforward mechanism governs differential GREB1 action in endometrial function and endometriosis.Nature communications · 2024Article
- TRIM28 modulates nuclear receptor signaling to regulate uterine function.Nature communications · 2023Article
- Recent development of analytical methods for disease-specific proteinRSC advances · 2022Review
- Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease.Frontiers in molecular biosciences · 2022Review
- TargetingFrontiers in oncology · 2022Review
- Metabolic Adaptations in an Endocrine-Related Breast Cancer Mouse Model Unveil Potential Markers of Tumor Response to Hormonal Therapy.Frontiers in oncology · 2022Article
- Article
- O-GlcNAcylation and O-GlcNAc Cycling Regulate Gene Transcription: Emerging Roles in Cancer.Cancers · 2021Review
- O-GlcNAcylation: the "stress and nutrition receptor" in cell stress response.Cell stress & chaperones · 2021Review
- O-GlcNAcylation Enhances NUSAP1 Stability and Promotes Bladder Cancer Aggressiveness.OncoTargets and therapy · 2021Article
- MicroRNAs MiR-15a and MiR-26a cooperatively regulate O-GlcNAc-transferase to control proliferation in clear cell renal cell carcinoma.Cancer biomarkers : section A of Disease markers · 2021Article
- Inhibition of O-GlcNAc transferase activates tumor-suppressor gene expression in tamoxifen-resistant breast cancer cells.Scientific reports · 2020Article
- Functional Analysis ofFrontiers in oncology · 2020Review
- Non-targeted metabolomics reveals diagnostic biomarker in the tongue coating of patients with chronic gastritis.Journal of pharmaceutical and biomedical analysis · 2019Article
- Progesterone Receptor Attenuates STAT1-Mediated IFN Signaling in Breast Cancer.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- O-GlcNAc Transferase Inhibition Differentially Affects Breast Cancer Subtypes.Scientific reports · 2019Article
- Suppressed OGT expression inhibits cell proliferation and modulates EGFR expression in renal cell carcinoma.Cancer management and research · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Emerging clinical trial data implicate progestins in the development of breast cancer. While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer. PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases). Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins. This interaction between PR and OGT leads to the post-translational modification of PR by O-GlcNAc. Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high. O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT. These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity. Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.