Interleukin-6 Increases Insulin-Stimulated Glucose Disposal in Humans and Glucose Uptake and Fatty Acid Oxidation In Vitro via AMP-Activated Protein Kinase
Open accessAbstract
Although interleukin-6 (IL-6) has been associated with insulin resistance, little is known regarding the effects of IL-6 on insulin sensitivity in humans in vivo. Here, we show that IL-6 infusion increases glucose disposal without affecting the complete suppression of endogenous glucose production during a hyperinsulinemic-euglycemic clamp in healthy humans. Because skeletal muscle accounts for most of the insulin-stimulated glucose disposal in vivo, we examined the mechanism(s) by which IL-6 may affect muscle metabolism using L6 myotubes. IL-6 treatment increased fatty acid oxidation, basal and insulin-stimulated glucose uptake, and translocation of GLUT4 to the plasma membrane. Furthermore, IL-6 rapidly and markedly increased AMP-activated protein kinase (AMPK). To determine whether the activation of AMPK mediated cellular metabolic events, we conducted experiments using L6 myotubes infected with dominant-negative AMPK alpha-subunit. The effects described above were abrogated in AMPK dominant-negative-infected cells. Our results demonstrate that acute IL-6 treatment enhances insulin-stimulated glucose disposal in humans in vivo, while the effects of IL-6 on glucose and fatty acid metabolism in vitro appear to be mediated by AMPK.
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IL-6 released during exercise promotes insulin-independent glucose uptake by inducing translocation of GLUT4 transporters in adipose tissue via PI3K/Akt signaling.
“While IL-6 released during exercise promotes insulin-independent glucose uptake by inducing the translocation of GLUT4 transporters in adipose tissue via the phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt) signaling pathway”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [50]
The paper reports that IL-6 increases basal glucose transport in cultured 3T3-L1 adipocytes, and that it increases GLUT4 translocation in L6 myotubes (Results; page unavailable). It does not show GLUT4 translocation in adipocytes or attribute the effect to PI3K/Akt signaling: the muscle-cell results found no evidence that IL-6 alone increased those insulin-signaling processes, and the paper instead emphasizes AMPK. Its link between exercise-released IL-6 and these effects is suggested, not directly tested. (LLM, conf=0.89)
Experimental — accuracy not yet measuredExercise-inducible myokines irisin, IL-6, IL-15, BAIBA, and METRNL, as well as osteokine OCN, directly stimulate oxidative metabolism in autocrine and endocrine ways.
“Exercise-inducible myokines, such as irisin [62,63], IL-6 [76,77], IL-15 [91,126], BAIBA [111], and METRNL [100], as well as the osteokine OCN [71] have been shown to directly stimulate oxidative metabolism in autocrine and endocrine ways, respectively (1).”
IL-6 promotes hepatic gluconeogenesis by activating key gluconeogenic enzymes including PEPCK and G-6-Pase.
“IL-6 also promotes hepatic gluconeogenesis by activating key gluconeogenic enzymes, including phosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase (G-6-Pase) [49,50].”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [50]
The section on endogenous glucose production reports that IL-6 did not change its suppression during an insulin clamp in healthy humans. Our copy does not address whether IL-6 activates hepatic PEPCK or G-6-Pase or promotes gluconeogenesis through those enzymes (searched: PEPCK, glucose-6-phosphatase, hepatic gluconeogenesis). The clamp result alone does not settle that distinct mechanistic claim. (LLM, conf=0.72)
Experimental — accuracy not yet measuredIL-6 can increase intramyocellular or whole body fatty acid oxidation via AMPK activation.
“Several other studies have described that IL-6 can increase intramyocellular (58-60) or whole body (61) fatty acid oxidation via AMPK activation (58, 62).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [58]
IL-6 increases both basal glucose uptake and glucose transporter GLUT4 translocation.
“It is well documented that IL-6 increases both basal glucose uptake and glucose transporter GLUT4 translocation (58).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [58]
The effects of IL-6 on glucose uptake in vitro are mediated by activation of AMPK.
“The effects of IL-6 on glucose uptake in vitro was shown to be mediated by activation of adenosine 5′-monophosphate-activated protein kinase (AMPK) (58).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [58]
Muscle-derived IL-6 contributes markedly to systemic levels and acts in a hormone-like manner in lipid and glucose metabolism, principally via AMPK activation.
“Muscle-derived IL-6, but not IL-8, contributes markedly to systemic levels, where it works in a hormone-like fashion and plays an important role in lipid and glucose metabolism [9,10], principally via activation of AMP-activated protein kinase (AMPK) [10].”
In healthy humans, IL-6 infusion at levels comparable to strenuous exercise improves insulin-stimulated glucose uptake without changing whole-body lipolysis or lipid oxidation.
“In healthy humans, IL-6 infusion to levels similar to those seen with strenuous exercise enhances insulin-stimulated glucose-uptake but does not alter whole-body lipolysis or lipid oxidation120.”
From Exerkines in health, resilience and disease (2022) · cites this paper as [120]
In these same contexts, others have shown that IL6 induces insulin sensitivity, while IL6 has been shown to be insulin sensitizing in exercise.
“On the other hand, in these same contexts, others have shown that IL6 induces insulin sensitivity (Carey et al., 2006; Findeisen et al., 2019; Matthews et al., 2010; Mauer et al., 2014; Steensberg et al., 2003; Timper et al., 2017), while IL6 has been shown to be insulin sensitizing in exercise (Benrick et al., 2012).”
From Origin and function of stress-induced IL-6 in murine models (2020) · cites this paper as Carey et al., 2006
IL-6 increases glucose disposal in humans and glucose uptake in L6 myotubes; an effect dependent on AMPK signaling.
“Carey et al. [163] was one of the first studies to show that IL-6 increases glucose disposal in humans and glucose uptake in L6 myotubes; an effect dependent on AMPK signaling.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [163]
IL-6 increases the glucose infusion rate and glucose oxidation without affecting suppression of endogenous glucose production during a hyperinsulinemic euglycemic clamp in healthy humans.
“Recently, we demonstrated that IL-6 increased the glucose infusion rate [56] and glucose oxidation without affecting the suppression of endogenous glucose production during a hyperinsulinemic euglycemic clamp in healthy humans.”
From Exercise as a Mean to Control Low‐Grade Systemic Inflammation (2008) · cites this paper as [56]
Accumulating data suggest that IL-6 enhances glucose uptake in myocytes.
“Thus, accumulating data suggest that IL-6 enhances glucose uptake in myocytes [54–57].”
From Exercise as a Mean to Control Low‐Grade Systemic Inflammation (2008) · cites this paper as [56]
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Self-citation
- Authors
- Carey, A. L., Steinberg, G. R., Macaulay, S. L., Thomas, W. G., Holmes, A. G., Ramm, G., Prelovsek, O., Hohnen-Behrens, C., Watt, M. J., James, D. E., Kemp, B. E., Pedersen, B. K., & Febbraio, M. A.
- Affiliations
- The University of Melbourne (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Baker Heart and Diabetes Institute (AU)
- RMIT University (AU)
- Garvan Institute of Medical Research (AU)
- University of Copenhagen (DK)
- ORCID
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2006-10-01
- Volume
- 55
- Issue
- 10
- Pages
- 2688-2697
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2109384991
- Cited by
- 898
- References
- 48
- Citations by year
- 2026: 30 · 2025: 49 · 2024: 48 · 2023: 64 · 2022: 55 · 2021: 45 · 2020: 50 · 2019: 46 · 2018: 51 · 2017: 53 · 2016: 40 · 2015: 42 · 2014: 50 · 2013: 59 · 2012: 44
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- UCLA - Biblioteca de Ciencias de la Salud (submittedVersion)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Heart and Stroke Foundation of Canada
- Canadian Diabetes Association
- Sundhed og Sygdom, Det Frie Forskningsråd (22-01-009)
- National Research Foundation
- Danmarks Grundforskningsfond (22-01-009, LSHM-CT-2004-005272)
- Javna Agencija za Raziskovalno Dejavnost RS
- Univerza v Ljubljani
- Canadian Institutes of Health Research
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council (251558)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- interleukin-6, insulin sensitivity, insulin-stimulated glucose disposal, skeletal muscle glucose uptake, fatty acid oxidation, GLUT4 translocation, AMPK, L6 myotubes, hyperinsulinemic-euglycemic clamp, insulin resistance
- MeSH terms
- Suppressor of Cytokine Signaling 3 Protein, Adult, Aminoimidazole Carboxamide, Animals, Cell Line, Cell Membrane, Fatty Acids, Glucose, Humans, Hyperinsulinism, Insulin, Male, Multienzyme Complexes, Recombinant Proteins, Ribonucleotides, Glucose Clamp Technique, Signal Transduction, Interleukin-6, Protein Serine-Threonine Kinases, Mice, Knockout, Myoblasts, 3T3-L1 Cells, STAT3 Transcription Factor, Suppressor of Cytokine Signaling Proteins, Glucose Transporter Type 4, Mice, Rats, AMP-Activated Protein Kinases
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