The DOI matches its Crossref record; 188 of the 190 references it cites were found in a registry or an index.
New Insights into the Anti-inflammatory Mechanisms of Glucocorticoids: An Emerging Role for Glucocorticoid-Receptor-Mediated Transactivation
Open accessAbstract
Glucocorticoids are anti-inflammatory drugs that are widely used for the treatment of numerous (autoimmune) inflammatory diseases. They exert their actions by binding to the glucocorticoid receptor (GR), a member of the nuclear receptor family of transcription factors. Upon ligand binding, the GR translocates to the nucleus, where it acts either as a homodimeric transcription factor that binds glucocorticoid response elements (GREs) in promoter regions of glucocorticoid (GC)-inducible genes, or as a monomeric protein that cooperates with other transcription factors to affect transcription. For decades, it has generally been believed that the undesirable side effects of GC therapy are induced by dimer-mediated transactivation, whereas its beneficial anti-inflammatory effects are mainly due to the monomer-mediated transrepressive actions of GR. Therefore, current research is focused on the development of dissociated compounds that exert only the GR monomer-dependent actions. However, many recent reports undermine this dogma by clearly showing that GR dimer-dependent transactivation is essential in the anti-inflammatory activities of GR. Many of these studies used GR(dim/dim) mutant mice, which show reduced GR dimerization and hence cannot control inflammation in several disease models. Here, we review the importance of GR dimers in the anti-inflammatory actions of GCs/GR, and hence we question the central dogma. We summarize the contribution of various GR dimer-inducible anti-inflammatory genes and question the use of selective GR agonists as therapeutic agents.
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“The single point mutation A458T engineered in GRdim is thus unlikely to fully abrogate the formation of functional GR homodimers (30, 112, 113).”
From The HPA – Immune Axis and the Immunomodulatory Actions of Glucocorticoids in the Brain (2014) · cites this paper as [30]
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Metadata
- Authors
- Vandevyver, S., Dejager, L., Tuckermann, J., & Libert, C.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Universität Ulm (DE)
- Corresponding author
- Libert, Claude
- Venue
- Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2013-03-01
- Volume
- 154
- Issue
- 3
- Pages
- 993-1007
- ISSN
- 0013-7227 (ISSN-L)
- 1945-7170
- OpenAlex
- W2054115898
- Cited by
- 296
- References
- 190
- Citations by year
- 2026: 11 · 2025: 8 · 2024: 17 · 2023: 21 · 2022: 19 · 2021: 24 · 2020: 25 · 2019: 29 · 2018: 19 · 2017: 23 · 2016: 34 · 2015: 24 · 2014: 31 · 2013: 11
- FWCI
- 4.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Endocrinology (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, other-oa)
- Funders
- Universiteit Gent
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- glucocorticoids, glucocorticoid receptor, anti-inflammatory mechanism, receptor dimerization, transcriptional activation, transrepression, glucocorticoid response element, inflammatory diseases
- MeSH terms
- Animals, Anti-Inflammatory Agents, Glucocorticoids, Humans, Mice, Mutant Strains, Models, Biological, Receptors, Glucocorticoid, Signal Transduction, Transcriptional Activation, Annexin A1, Response Elements, Mice, Protein Multimerization
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