In vivo stimulation of oestrogen receptor α increases insulin‐stimulated skeletal muscle glucose uptake
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Non‐technical summary Previous studies show that oestrogen is beneficial for maintaining blood glucose levels and helping the body respond to insulin. Despite these previous findings, the mechanism by which oestrogen acts is unknown. We show that specific activation of oestrogen receptor α (ERα) increases glucose uptake into skeletal muscle when insulin is present. Activation of oestrogen receptor β (ERβ) alone or activation of both ERα and ERβ together did not increase glucose uptake into skeletal muscle. This suggests that oestrogen's beneficial effect occurs by activating ERα. These results have important implications for understanding the mechanisms of glucose homeostasis, particularly in postmenopausal women with low oestrogen levels.
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Increased ERα expression increased skeletal muscle glucose uptake in ovariectomized female mice given E2.
“An in vivo experiment similarly showed that increased ERα expression increased skeletal muscle glucose uptake in ovariectomized female mice given E2 (151).”
From Metabolic impact of endogenously produced estrogens by adipose tissue in females and males across the lifespan (2025) · cites this paper as [151]
The Experimental animals and treatment section (page not available) identifies the animals as ovariectomized female rats, not mice, and describes separate estradiol benzoate (EB) and ERα-agonist (PPT) treatments. The Results section, “PPT increases insulin-stimulated glucose transport in soleus and EDL muscle” (page not available), says PPT increased uptake but EB did not; the study tested ERα activation, not increased ERα expression. (LLM, conf=0.90)
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ESTROGEN RECEPTOR REGULATION OF GLUCOSE AND FAT METABOLISM IN THE SKELETAL MUSCLE AND ADIPOSE TISSUE
Gorres, B. K. (2011) · KU ScholarWorks (The University of Kansas)
Self-citationAskin, N. (2014) · TSpace (University of Toronto)
Investigating Ectopic Sites for Islet Transplantation
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Heat Shock Protein 72 Regulation of Metabolism
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- Authors
- Gorres, B. K., Bomhoff, G. L., Morris, J. K., & Geiger, P. C.
- Affiliations
- University of Kansas Medical Center (US)
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2011-04
- Volume
- 589
- Issue
- 8
- Pages
- 2041-2054
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- PMC
- PMC3090602
- OpenAlex
- W1588360729
- Cited by
- 116
- References
- 62
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 5 · 2023: 12 · 2022: 12 · 2021: 4 · 2020: 7 · 2019: 6 · 2018: 8 · 2017: 12 · 2016: 5 · 2015: 7 · 2014: 6 · 2013: 10 · 2012: 7
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (HD02528, RR016475)
- National Institute on Aging (R01AG031575, AG031575)
- National Center for Research Resources (HD02528, RR016475, P20RR016475)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (P30HD002528, HD-02528)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- estrogen receptor alpha, insulin-stimulated glucose uptake, skeletal muscle, estradiol benzoate, diarylpropionitrile, insulin signaling, Akt phosphorylation, AMPK, GLUT4, ovariectomy, glucose homeostasis, postmenopausal women, estrogen
- MeSH terms
- Analysis of Variance, Animals, Biological Transport, Estradiol, Female, Glucose, Injections, Subcutaneous, Insulin, Nitriles, Ovariectomy, Phenols, Phosphorylation, Propionates, Pyrazoles, Time Factors, Blotting, Western, Signal Transduction, Rats, Sprague-Dawley, Muscle, Skeletal, GTPase-Activating Proteins, Estrogen Receptor alpha, Estrogen Receptor beta, Proto-Oncogene Proteins c-akt, Glucose Transporter Type 4, Rats, AMP-Activated Protein Kinases
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