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Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase
Open accessAbstract
Aims/hypothesis Brain-derived neurotrophic factor (BDNF) is produced in skeletal muscle, but its functional significance is unknown. We aimed to determine the signalling processes and metabolic actions of BDNF.Methods We first examined whether exercise induced BDNF expression in humans. Next, C2C12 skeletal muscle cells were electrically stimulated to mimic contraction. L6 myotubes and isolated rat extensor digitorum longus muscles were treated with BDNF and phosphorylation of the proteins AMP-activated protein kinase (AMPK) (Thr(172)) and acetyl coenzyme A carboxylase beta (ACCbeta) (Ser(79)) were analysed, as was fatty acid oxidation (FAO). Finally, we electroporated a Bdnf vector into the tibialis cranialis muscle of mice.Results BDNF mRNA and protein expression were increased in human skeletal muscle after exercise, but muscle-derived BDNF appeared not to be released into the circulation. Bdnf mRNA and protein expression was increased in muscle cells that were electrically stimulated. BDNF increased phosphorylation of AMPK and ACCbeta and enhanced FAO both in vitro and ex vivo. The effect of BDNF on FAO was AMPK-dependent, since the increase in FAO was abrogated in cells infected with an AMPK dominant negative adenovirus or treated with Compound C, an inhibitor of AMPK. Electroporation of a Bdnf expression vector into the tibialis cranialis muscle resulted in increased BDNF protein production and tropomyosin-related kinase B (TrkB(Tyr706/707)) and extracellular signal-regulated protein kinase (p44/42 Thr(202)/Tyr(204)) phosphorylation in these muscles. In addition, phosphorylation of ACCbeta was markedly elevated in the Bdnf electroporated muscles.Conclusions/interpretation These data identify BDNF as a contraction-inducible protein in skeletal muscle that is capable of enhancing lipid oxidation in skeletal muscle via activation of AMPK.
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TL;DR
BDNF is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via AMPK activation in vitro and ex vivo, but muscle-derived BDNF is not released into the circulation and likely acts locally. Human exercise increased muscle BDNF protein about 50% at 24 h recovery, while serum BDNF rose immediately after exercise and tracked platelet counts.
Key findings
- In eight healthy men, 120 min of bicycle exercise at 60% V̇O₂max increased skeletal muscle BDNF protein about 50% at 24 h recovery (p<0.05); BDNF mRNA showed marked inter-individual variation, with an AUC difference between exercise and resting groups (p<0.05).
- Serum BDNF increased immediately after exercise and returned to pre-exercise levels by 60 min; platelet counts followed a closely matching pattern, suggesting the early circulating BDNF increase may at least partly reflect release from activated platelets rather than muscle.
- Electrically stimulated C2C12 myotubes increased Bdnf mRNA and pro- and mature BDNF protein, with no detectable BDNF release into media.
- BDNF increased phosphorylation of AMPK (Thr172) and ACCβ (Ser79) and enhanced palmitate oxidation in L6 myotubes and rat extensor digitorum longus muscle ex vivo; the FAO increase was AMPK-dependent, as it was abrogated by Compound C or an AMPK dominant negative adenovirus. BDNF did not increase glucose uptake (fold change from vehicle: vehicle=1±0.04; insulin 100 nmol/l=2.32±0.072; BDNF 10 ng/ml=0.94±0.071; insulin+BDNF=1.99±0.185).
Methods
- Human in vivo: 8 healthy, physically active but untrained men (mean±SD age 25±4 years, weight 82±8 kg, height 181±1 cm, BMI 25±2 kg/m²) performed 120 min bicycle exercise at 60% V̇O₂max; vastus lateralis biopsies and serum were collected before, immediately after, and at 3, 5, 8, 24, 48, and 72 h recovery.
- Cell culture: differentiated C2C12 myotubes were electrically stimulated for 120 min (18 V; 1 Hz; 24 ms); L6 myotubes were treated with recombinant human BDNF at 1, 10, and 100 ng/ml for 10 and 30 min, with palmitate oxidation and glucose uptake measured, and AMPK inhibition via 40 µmol/l Compound C or dominant negative AMPK adenovirus.
- Ex vivo and in vivo: rat extensor digitorum longus strips were treated with BDNF for palmitate oxidation and AMPK/ACCβ phosphorylation; 8- to 10-week-old C57BL6/C mice underwent intramuscular electroporation of a Bdnf vector into tibialis cranialis with doxycycline induction, with n=3 mice per group. Statistics included two-way ANOVA for repeated measures, unpaired t test for AUCs, and paired t tests for cell culture experiments from three independent experiments.
Limitations
- Stated: the contraction-induced increase in BDNF both in vivo and in vitro was relatively modest, whereas electroporation increased BDNF several fold, so whether BDNF plays an important role in vivo is unclear.
- Stated: whether the ACCβ phosphorylation effect after BDNF overproduction is due to paracrine/autocrine signaling or a direct intracellular signaling event requires further clarification.
- Stated: BDNF plays no role in mediating contraction-induced increases in fat oxidation, because fat oxidation increases at the onset of contraction while muscle BDNF increases well into recovery. Evident: the human exercise cohort was small (n=8), and the paper reports no direct measurement of autocrine/paracrine BDNF action within muscle.
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37 Own result · 16 Own interpretation · 15 Not checked yet · 1 Own method
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In the paper
“We also showed that contraction did not increase LDH release from cells into the media (Fig. 3b).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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“There were no differences in BDNF mRNA levels in the exercise cohort compared with the resting cohort (Fig. 1a).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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In the paper
“Irrespective of whether cells were treated with PBS (Fig. 4d) or infected with a control virus (AdGO) (Fig. 4e) treatment of cells with BDNF enhanced fat oxidation.”
- Also stated in: § Abstract · plain
“BDNF increased phosphorylation of AMPK and ACCβ and enhanced FAO both in vitro and ex vivo.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes
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In the paper
“BDNF increased phosphorylation of AMPK and ACCβ and enhanced FAO both in vitro and ex vivo.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Abstract
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In the paper
“We were unable to detect any differences in BDNF release in the media of control compared with contraction-treated cells (data not shown).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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In the paper
“In addition, the plasma levels of P-selectin, a marker of platelet activation, were also increased immediately following exercise (data not shown).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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In the paper
“The effect of BDNF on FAO was AMPK-dependent, since the increase in FAO was abrogated in cells infected with an AMPK dominant negative adenovirus or treated with Compound C, an inhibitor of AMPK.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Abstract
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- Rests on an assumption: AMPK phosphorylation of ACCβ inhibits ACC, lowers malonyl-CoA, relieves CPT1 inhibition, and increases fatty acid oxidation.
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In the paper
“The time-dependent effects were transient as no differences were seen in phospho-AMPK or phospho-ACCβ at 30 min (data not shown), with the effects present at only 10 min (Fig. 4a-c).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes
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In the paper
“To confirm that this increase in BDNF expression was indeed increased within muscle fibres, we performed IHC experiments and showed that the increased BDNF production 24 h after exercise was indeed intramyocellular (Fig. 1d).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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- Rests on an assumption: The BDNF antibody used recognizes both pro- and mature forms of BDNF.
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In the paper
“In addition, muscle contraction increased Bdnf mRNA levels compared with non-contracted cells (Fig. 3d).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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“We showed that at the two higher doses, BDNF markedly phosphorylated ACCβ, while a similar effect was seen for phospho-AMPK at the higher dose.”
- Also stated in: § BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes · plain
“The lack of effect of phospho-AMPK at 10 ng/ml was unexpected since phospho-ACCβ was increased.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes
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“we first showed that PCr, but not ATP, stores were decreased by contraction (Fig. 3a).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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“Moreover, such a treatment increased both the pro-and mature BDNF protein levels immediately after the contraction protocol (Fig. 3e, f).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Rests on an assumption: The BDNF antibody used recognizes both pro- and mature forms of BDNF.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“We showed that at the two higher doses, BDNF markedly phosphorylated ACCβ, while a similar effect was seen for phospho-AMPK at the higher dose.”
- Also stated in: § BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes · plain
“with the effects present at only 10 min (Fig. 4a-c).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes
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- Also stated in: § BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes · plain
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In the paper
“Serum BDNF concentrations increased immediately following exercise, before returning to pre-exercise levels 60 min following the cessation of exercise (Fig. 2a).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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“BDNF mRNA and protein expression were increased in human skeletal muscle after exercise, but muscle-derived BDNF appeared not to be released into the circulation.”
- Also stated in: § Results · plain
“As such, we calculated the AUC over time for both groups and showed a difference (p<0.05) for the AUC when comparing the two groups.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Abstract
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“At 24 h into recovery from exercise, BDNF protein levels were increased (about 50%; p<0.05) in the muscle homogenates (Fig. 1b, c).”
- Also stated in: § Abstract · hedged
“BDNF mRNA and protein expression were increased in human skeletal muscle after exercise, but muscle-derived BDNF appeared not to be released into the circulation.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
plaindirect- Asserted: passes — The authors put it forward as true.
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- Also stated in: § Abstract · hedged
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation
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“It should also be noted that while both BDNF and the positive control 5-aminoimidazole-4-carboxamide 1-β-D-ribofuranoside (AICAR) increased 14 C in the CO 2 fraction, this was not seen in the acid soluble metabolite fraction, indicating complete oxidation of the label.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation
hedgeddirect- Asserted: passes — The authors put it forward as true.
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In the paper
“By conducting muscle cell culture experiments, we show that C2C12 murine cells not only produce BDNF, but that this production can be increased by contraction.”
- Also stated in: § BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes · plain
“Bdnf mRNA and protein expression is increased in contracting muscle cells.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
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In the paper
“However, when cells were treated with the AMPK inhibitor Compound C or infected with an AMPK dominant negative adenovirus, the BDNF-induced increase in fat oxidation was completely abrogated (Fig. 4d, e)”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases fat oxidation in an AMPK-dependent manner in L6 myotubes
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In the paper
“It must be acknowledged, however, that the contraction-induced increase in BDNF both in vivo (Fig. 1) and in vitro (Fig. 3) was relatively modest, whereas we increased BDNF several fold with electroporation (Fig. 6).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
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In the paper
“BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation
plaindirect- Asserted: passes — The authors put it forward as true.
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In the paper
“In addition, we were unable to detect any BDNF in the media from cells that underwent contraction, even though such an intervention increased BDNF protein production.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
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In the paper
“We showed that circulating levels of BDNF increased immediately after exercise and did not correlate with the elevated muscle-derived BDNF 24 h after exercise.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
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“Since platelets are known to store and release BDNF [35], we examined the relationship between circulating BDNF and platelet count.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
What the sources say
- Not checked yetcites [35] Fujimura H, Altar CA, Chen R et al (2002) Brain-derived neurotrophic factor is stored in human platelets and released by agonist stimulation. Thromb Haemost 87:728–734 source
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In the paper
“Recent studies have demonstrated that physical exercise can increase circulating BDNF levels in both healthy humans [19,20] and patients with multiple sclerosis [21], although the cellular origin of this increase is unclear.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [19] Ferris LT, Williams JS, Shen CL (2007) The effect of acute exercise on serum brain-derived neurotrophic factor levels and cognitive function. Med Sci Sports Exerc 39:728–734 source
- Not checked yetcites [20] Rojas Vega S, Strüder HK, Vera Wahrmann B, Schmidt A, Bloch W, Hollmann W (2006) Acute BDNF and cortisol response to low intensity exercise and following ramp incremental exercise to exhaustion in humans. Brain Res 1121:59–65 source
- Not checked yetcites [21] Gold SM, Schulz KH, Hartmann S et al (2003) Basal serum levels and reactivity of nerve growth factor and brain-derived neurotrophic factor to standardized acute exercise in multiple sclerosis and controls. J Neuroimmunol 138:99–105 source
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In the paper
“However, in a recent study, Bdnf mRNA was shown to be expressed in murine skeletal muscle and was increased by inhibition of histone deacetylases [24].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [24] Avila AM, Burnett BG, Taye AA et al (2007) Trichostatin A increases SMN expression and survival in a mouse model of spinal muscular atrophy. J Clin Invest 117:659–671 source
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In the paper
“The kinetics of the exercise-induced elevation in serum BDNF levels failed to correlate with the increased production of BDNF in muscle 24 h after exercise, suggesting that the skeletal muscle is not a source of the increase in serum BDNF observed early into recovery from exercise.”
- Also stated in: § Abstract · hedged
“but muscle-derived BDNF appeared not to be released into the circulation.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
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In the paper
“Since exercise can inhibit histone deacetylases [25], the possibility exists that the increase in circulating BDNF in humans during exercise may originate in the contracting muscle cells and that BDNF may be a novel contraction-induced myokine.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [25] McGee SL, Hargreaves M (2004) Exercise and myocyte enhancer factor 2 regulation in human skeletal muscle. Diabetes 53:1208–1214 source
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In the paper
“It is also known that BDNF reduces food intake and lowers blood glucose in genetically modified (db/db) obese mice [15][16][17][18].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [15][16][17][18]
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- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Taken together, these results demonstrate that physical exercise increases circulating BDNF and that the increase may at least to some extent reflect in vivo release of BDNF from activated platelets.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“it is now clear that IL-6 [7] and IL-8 [8] production is upregulated by muscle contraction and that these cytokines may be released from contracting skeletal muscle.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [7] Febbraio MA, Pedersen BK (2002) Muscle-derived interleukin-6: mechanisms for activation and possible biological roles. FASEB J 16:1335–1347 source
- Not checked yetcites [8] Pedersen BK, Steensberg A, Fischer C et al (2003) Searching for the exercise factor—is IL-6 a candidate. J Muscle Res Cell Motil 24:113–119 source
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“Recently, we demonstrated a strong association between low plasma BDNF and type 2 diabetes on the one hand and both obesity and insulin resistance on the other [37].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [37] Krabbe KS, Nielsen AR, Krogh-Madsen R et al (2007) Brain-derived neurotrophic factor (BDNF) and type 2 diabetes. Diabetologia 50:431–438 source
boostedcorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Hence, we have identified BDNF as being a novel contraction-induced protein that may contribute to the multiple health benefits associated with exercise, possibly by enhancing fat oxidation in skeletal muscle.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
hedgedconditional- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“since we show both in vitro and in intact muscle ex vivo that, like CNTF, BDNF activates AMPK signalling and enhances FAO.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“This hypothesis is plausible since overproduction of BDNF resulted in marked ERK (Fig. 6c) and TrkB (Fig. 6d, e) phosphorylation, which is indicative of signalling through TrkB, which is produced in skeletal muscle and myotubes [43].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
hedgeddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
- Rests on an assumption: BDNF binding to TrkB causes TrkB phosphorylation and downstream ERK phosphorylation.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Taken together, our data demonstrate that BDNF is a protein produced in skeletal muscle cells that is increased by contraction to enhance fat oxidation in an AMPKdependent fashion, most probably by acting in an autocrine and/or paracrine manner within skeletal muscle.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
hedgeddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“Recent studies have demonstrated that Bdnf mRNA increases in the contracting skeletal muscle of rodents [22,23]”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [22] Dupont-Versteegden EE, Houlé JD, Dennis RA et al (2004) Exercise-induced gene expression in soleus muscle is dependent on time after spinal cord injury in rats. Muscle Nerve 29:73–81 source
- Not checked yetcites [23] Gómez-Pinilla F, Ying Z, Opazo P, Roy RR, Edgerton VR (2001) Differential regulation by exercise of BDNF and NT-3 in rat spinal cord and skeletal muscle. Eur J Neurosci 13:1078–1084 source
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“In summary, we have identified BDNF as being a novel contraction-induced muscle cell-derived protein that can increase fat oxidation in skeletal muscle in an AMPKdependent fashion.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“The latter findings are supported by animal studies, which demonstrate an insulin-sensitising effect of BDNF [15][16][17].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [15] Ono M, Ichihara J, Nonomura T et al (1997) Brain-derived neurotrophic factor reduces blood glucose level in obese diabetic mice but not in normal mice. Biochem Biophys Res Commun 238:633–637 source
- Not checked yetcites [16] Tonra JR, Ono M, Liu X et al (1999) Brain-derived neurotrophic factor improves blood glucose control and alleviates fasting hyperglycemia in C57BLKS-leprdb/leprdb mice. Diabetes 48:588–594 source
- Not checked yetcites [17] Nakagawa T, Tsuchida A, Itakura Y et al (2000) Brain-derived neurotrophic factor regulates glucose metabolism by modulating energy balance in diabetic mice. Diabetes 49:436–444 source
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“As no differences were reported when comparing the muscles of the control with the sham group, data from sham-treated muscles are reported.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Human in vivo experiments
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“These data suggest that BDNF may act in an autocrine and/ or paracrine fashion in skeletal muscle.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
hedgedconditionaln = 3- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“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].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Introduction
What the sources say
- Not checked yetcites [9] Febbraio MA, Hiscock N, Sacchetti M, Fischer CP, Pedersen BK (2004) Interleukin-6 is a novel factor mediating glucose homeostasis in skeletal muscle contraction. Diabetes 53:1643–1648 source
- Not checked yetcites [10] Carey AL, Steinberg GR, Macaulay SL et al (2006) Interleukin-6 increases insulin-stimulated glucose disposal in humans and glucose uptake and fatty acid oxidation in vitro via AMP-activated protein kinase. Diabetes 55:2688–2697 source
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“we have recently demonstrated that a different neurotrophin, namely ciliary neurotrophic factor (CNTF) can increase insulin sensitivity and decrease obesity by acting on both central [38] and peripheral [39,40] tissues.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [38] Steinberg GR, Watt MJ, Fam BC et al (2006) Ciliary neurotrophic factor suppresses hypothalamic AMPK signaling in leptin resistant obese mice. Endocrinology 147:3906–3914 source
- Not checked yetcites [39] Watt MJ, Dzamko N, Thomas W et al (2006) CNTF reverses obesity-induced insulin resistance by activating skeletal muscle AMPK. Nat Med 12:541–548 source
- Not checked yetcites [40] Watt MJ, Hevener A, Lancaster GI, Febbraio MA (2006) Ciliary neurotrophic factor prevents acute lipid-induced insulin resistance by attenuating ceramide accumulation and phosphorylation of JNK in peripheral tissues. Endocrinology 147:2077–2085 source
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“providing further evidence that BDNF exerts its action locally and is not released into the circulation when intramuscular production is increased.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
In the paper
“in a recent study, the mRNA of Bdnf was shown to be expressed in murine skeletal muscle homogenates and that this was increased by inhibition of histone deacetylases [24]”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [24] Avila AM, Burnett BG, Taye AA et al (2007) Trichostatin A increases SMN expression and survival in a mouse model of spinal muscular atrophy. J Clin Invest 117:659–671 source
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Results from our human exercise studies and cell culture experiments suggested that BDNF was produced by muscle cells during contraction, but was not released into the circulation or media.”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > BDNF increases phosphorylation of AMPK and its downstream target ACCβ and results in enhanced fat oxidation
hedged- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
It may state two separate claims as one.
In the paper
“It is well known that pro-BDNF can be processed into mature BDNF by several matrix metalloproteinases and thereby regulate activation of TrkB either by autophosphorylation or via an interaction with a neighbouring cell [44].”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
What the sources say
- Not checked yetcites [44] Ethell IM, Ethell DW (2007) Matrix metalloproteinases in brain development and remodeling: synaptic functions and targets. J Neurosci Res 85:2813–2823 source
boosteddirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
The paper relies on this without support.
AMPK phosphorylation of ACCβ inhibits ACC, lowers malonyl-CoA, relieves CPT1 inhibition, and increases fatty acid oxidation.
“AMPK phosphorylates ACCβ resulting in inhibition of ACC activity, which in turn leads to a decrease in malonyl-CoA content, relieving inhibition of carnitine palmitoyl transferase 1 and increasing fatty acid oxidation (FAO).”
The paper relies on this without support.
The BDNF antibody used recognizes both pro- and mature forms of BDNF.
“The antibody against BDNF protein recognises both the pro-and mature forms of BDNF.”
The paper relies on this without support.
During exercise in humans, fat oxidation increases at the onset of contraction.
“It should be noted that during exercise in humans, fat oxidation is increased at the onset of contraction while the increase in BDNF in skeletal muscle does not occur until well into recovery.”
The paper relies on this without support.
During exercise in humans, the increase in BDNF in skeletal muscle does not occur until well into recovery.
“It should be noted that during exercise in humans, fat oxidation is increased at the onset of contraction while the increase in BDNF in skeletal muscle does not occur until well into recovery.”
The paper relies on this without support.
BDNF binding to TrkB causes TrkB phosphorylation and downstream ERK phosphorylation.
“Upon BDNF binding, TrkB is phosphorylated (Tyr 705/706 ) resulting in a signalling cascade that includes phosphorylation of ERK (Thr 202 /Tyr 204 ).”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“BDNF mRNA and protein expression were increased in human skeletal muscle after exercise, but muscle-derived BDNF appeared not to be released into the circulation (332).”
From Lack of Exercise Is a Major Cause of Chronic Diseases (2012) · cites this paper as [332]
In the citing paper
“In contrast, BDNF is identified as a myokine capable of enhancing AMPK activation and hence lipid oxidation in an autocrine or paracrine manner (63).”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [63]
In the citing paper
“Brain-derived neurotrophic factor (BDNF) is also expressed in human skeletal muscles, but BDNF is not released into the circulation and does not work in an endocrine way.”
From Muscle–Organ Crosstalk: The Emerging Roles of Myokines (2020) · cites this paper as [63]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
Each contradiction between two passages listed here was confirmed by an independent check.
Rated minor: it would not touch a result — a value no result rests on, a p-value that stays on the same side of the significance level, or a conflict that is clerical, resolved elsewhere in the paper, or outside its own findings.
In the paper
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Results
“Serum BDNF concentrations increased immediately following exercise, before returning to pre-exercise levels 60 min following the cessation of exercise (Fig. 2a).”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Human in vivo experiments
“Muscle biopsy samples were obtained from vastus lateralis before exercise, immediately after exercise, and 3, 5, 8, 24, 48 and 72 h into recovery using a percutaneous needle biopsy technique with suction.Samples were snap frozen before being analysed for BDNF mRNA and protein expression.Serum was obtained at the above mentioned time-points.”
Rated minor: it would not touch a result — a value no result rests on, a p-value that stays on the same side of the significance level, or a conflict that is clerical, resolved elsewhere in the paper, or outside its own findings.
In the paper
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Discussion
“Upon BDNF binding, TrkB is phosphorylated (Tyr 705/706 )”
§ Brain-derived neurotrophic factor is produced by skeletal muscle cells in response to contraction and enhances fat oxidation via activation of AMP-activated protein kinase > Analytical methods
“phospho-TrkB (Tyr 706/707 )”
Citations
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“BDNF mRNA and protein expression levels were also increased in the skeletal muscles of untrained males after acute aerobic exercise [12].”
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“BDNF/NTRK2 signaling increases fat oxidation in skeletal muscle through activation of AMP-activated protein kinase [10].”
Characteristics of Skeletal Muscle as a Secretory Organ
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“Exercise increases circulating and muscle brain-derived neurotrophic factor (BDNF), which is a myokine, in humans and mice (43).”
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“During aerobic exercise, skeletal muscle contractions upregulate BDNF release [33, 34], which can result in BDNF being stored in blood platelets [35].”
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“It enhances lipid oxidation within muscles and improves glucose utilization (Matthews et al. 2009; Yamanaka et al. 2007).”
BackgroundThomas, K. N., Caldwell, H. G., MacLeod, D. B., Abraham, W. C., Carr, J. M. J. R., Gasho, C., Brewster, L. M., Bruce, C. D., Monteleone, J. A., Duffy, J. S., et al. (2025) · The Journal of Physiology · doi:10.1113/jp289261 · Cited by 5
“…2014), other tissues contribute to the circulating pool including endothelial cells (Cefis et al., 2020; Monnier et al., 2017), skeletal muscle (Matthews et al., 2009), astrocytes (Vignoli & Canossa, 2017), lymphocytes (Kerschensteiner et al., 1999), peripheral neurons (Meyer et al., 1992) and…”
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“Also, muscle contraction has been shown to increase levels of brain-derived neurotrophic factor in muscle cells, which may have a role in promoting neuronal growth after nerve injury [133].”
BackgroundBDNF Val66Met Polymorphism, the Allele-Specific Analysis by qRT-PCR - a Novel Protocol
de Assis, G. G., Hoffman, J. R., & Gasanov, E. V. (2020) · International Journal of Medical Sciences · doi:10.7150/ijms.50643 · Cited by 4
“Predominantly expressed in neural and skeletal muscle cells as a protein signaler [7], BDNF synthesis results in the formation of several precursor isoforms in a multistage process involving cleavage and storage [2,8].”
BackgroundUpregulation of brain-derived neurotrophic factor by Shiikuwasha (Citrus depressa Hayata)
Nakajima, K., Okubo, S., Ohta, T., Uto, T., & Oiso, S. (2023) · Journal of Pharmaceutical Health Care and Sciences · doi:10.1186/s40780-023-00309-7 · Cited by 6
“Additionally, BDNF is produced in the skeletal muscles, kidney, thymus, heart, liver, lung, and spleen [25–30].”
BackgroundBrotto, M., Isaacson, J., & de Abreu, E. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-25976-5_4 · Cited by 4
Pedersen, B. K. (2016) · Springer eBooks · doi:10.1007/978-3-319-11251-0_31 · Cited by 4
Self-citationThe Pleiotropic Potential of BDNF beyond Neurons: Implication for a Healthy Mind in a Healthy Body
Rosa, M. C. D., Zimbone, S., Saab, M. W., & Tomasello, M. F. (2022) · Vide Leaf, Hyderabad eBooks · doi:10.37247/pabsc.1.22.35 · Cited by 3
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Türkez, H., Alak, G., Özgeriş, F. B., et al. (2024) · Drug and Chemical Toxicology · doi:10.1080/01480545.2024.2370916 · Cited by 3
“…that BDNF is involved in the immune interactions (Kerschensteiner et al., 1999; Wang & Wang, 2021) and stimulates lipid oxidation in muscle cells (Matthews et al., 2009). the cytokines play vital roles in immunity and cellular development, including growth, homeostasis, tissue repair, tumor…”
Moreira‐Pais, A., Ferreira, R. M., Aires, I., Sousa-Mendes, C., Nogueira‐Ferreira, R., Seixas, F., Leite-Moreira, A. F., Oliveira, P. A., & Duarte, J. A. (2025) · Biogerontology · doi:10.1007/s10522-024-10182-y · Cited by 3
“Muscle-derived BDNF appears not to be released into circulation (Matthews et al. 2009); however, the knowledge is very limited.”
Bloch‐Ibenfeldt, M., Demnitz, N., Gates, A. T., Garde, E., Siebner, H. R., Kjær, M., & Boraxbekk, C. (2025) · BMC Geriatrics · doi:10.1186/s12877-025-05778-z · Cited by 4
“One key myokine for brain plasticity is brain-derived neurotrophic factor (BDNF), which is produced by skeletal muscle during contraction [48].”
Madjedi, K. M., Stuart, K. V., Yin, G. S., Luben, R., Sun, Z., Biradar, M. I., Hu, R., Foster, P. J., Khaw, P. T., Bell, K. C., et al. (2025) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.66.6.66 · Cited by 3
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“It is also proposed that BDNF is produced within the skeletal muscle bed in response to muscle contraction during exercise (Matthews et al. 2009).”
Jäger, A., Pieper, A., Priebe, K., Hellweg, R., Meyer, K., Herrmann, S., Wolfarth, B., Grummt, M., Ströhle, A., & Schoofs, N. (2024) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2024.11.009 · Cited by 3
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Role of brain-derived neurotrophic factor in frailty: From mechanisms to interventions
Xu, Y., Liu, Z., Xu, J., Xu, L., He, Z., Liu, F., & Wang, Y. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118016 · Cited by 4
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“Furthermore, high shear stress (the force exerted on blood vessel walls) has been associated with the release of 32% of total bound platelet BDNF, which may have also contributed to the reported increase in BDNF levels seen (Matthews et al., 2009).”
Roles of myokines in osteoporosis under physiological and diabetic conditions
Ji, X., Hu, X., Xu, T., & Yang, W.-L. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1600218 · Cited by 5
Exercise is medicine: Die Rolle von Zytokinen und Myokinen für Gesundheit und Krankheit
Wahl, P. (2018) · Sportphysio · doi:10.1055/a-0642-8160 · Cited by 3
“[44] Matthews VB, Astrom MB, Chan MH et al.”
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Alcohol and Brain-Derived Neurotrophic Factor (BDNF)
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Sarcopenia: Pathophysiology and Treatment Strategies
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Skrzep-Poloczek, B., Idzik, M., Michalczyk, K., Chełmecka, E., Kukla, M., Zalejska–Fiolka, J., Poloczek, J., Bogielski, B., Jochem, J., Nowak, D., et al. (2023) · Journal of Clinical Medicine · doi:10.3390/jcm12154881 · Cited by 3
“Peripherally, it is expressed by skeletal [15], adipose [16], and endothelial cells [17], and stored in a form bound to platelets in the blood, liver, and spleen [18].”
BackgroundUpregulation Effect of Citrus Species on Brain-Derived Neurotrophic Factor
NAKAJIMA, K., Ahreum, H. A. N., KAYANO, A., & Oiso, S. (2024) · Journal of Nutritional Science and Vitaminology · doi:10.3177/jnsv.70.61 · Cited by 3
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Chronic Exercise and Cognition in Humans
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Apoptotic Effects of Reduced Brain Derived Neurotrophic Factor (BDNF) on Mouse Liver and Kidney
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Serum brain‐derived neurotrophic factor in the diagnosis of febrile seizure
Çokyaman, T., Kasap, T., & Şehitoğlu, H. (2020) · Pediatrics International · doi:10.1111/ped.14567 · Cited by 3
Effects of hippotherapy on brain function, BDNF level, and physical fitness in children with ADHD
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Acevedo, O. G., Aragón‐Vela, J., Márquez, J. C. D. L. C., Marín, M. M., Casuso, R. A., & Huertas, J. R. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19159581 · Cited by 3
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“Physical exercise stimulates platelet activation, which triggers the release of BDNF into the bloodstream [23].”
Exercise Suppresses Appetite in Obesity: A Biochemical, Metabolic, and Molecular Approach
Razi, O., Zamani, N., de Moraes, C., Laher, I., & Hadjicharalambous, M. (2025) · Applied Sciences · doi:10.3390/app15116191 · Cited by 4
Jost, Z., Rozynkowska, A., Głąb, M., Sitkiewicz, A., Goiko, M., Laskowski, R., Herold, F., Radak, Z. O., & Kujach, S. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2025.1733269 · Cited by 2
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“Given the well-established role of skeletal muscle ECs as a major source of pro-regenerative factors such as brain-derived neurotrophic factor (BDNF), 66–68 their loss in both conditions is unlikely to be incidental.”
Therapeutic potential of exerkines in neurodegenerative and mental disorders: a narrative review
Yang, S., Sang, H.-W., Kim, S., Cho, E., Choi, Y., Kang, D., Jang, Y. C., Park, D.-H., Kwak, H., & Yook, J. S. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1793043 · Cited by 2
“In skeletal muscles, contraction induces BDNF expression, which mainly acts in an autocrine/paracrine manner to coordinate metabolic adaptation and muscle repair (Matthews et al., 2009).”
Exercise-induced myokines in metabolic regulation: mechanisms, mimetics, and translational potential
Aslam, M. A., Lee, J., Bowen, T. S., & Huh, J. Y. (2026) · Archives of Pharmacal Research · doi:10.1007/s12272-026-01624-x · Cited by 7
“In cell models, muscle contraction induces BDNF expression, and BDNF enhances fatty acid oxidation through AMPK activation, consistent with this local metabolic role (Matthews et al. 2009).”
Khandekar, P., Shenoy, S., & Sathe, A. (2022) · Neuroscience Research Notes · doi:10.31117/neuroscirn.v5i2.146 · Cited by 2
“The expression of BDNF mRNA is increased in the muscle cells after acute exercise (Matthews et al., 2009).”
BackgroundAzusa, M. I. K. I., AIHARA, M., KAWAGUCHI, H., Hirose, N., & Hagiwara, H. (2024) · Biomedical Research · doi:10.2220/biomedres.45.163 · Cited by 3
Giannopoulos, A. J., Mohammad, A., Retsidou, M. I., Tucker, J. A. L., Bornath, D. P. D., McCarthy, S. F., MacPherson, R. E. K., Hazell, T. J., & Klentrou, P. (2024) · Endocrines · doi:10.3390/endocrines5030021 · Cited by 3
“Given this, the reduction in BDNF with menopause likely contributes to the increased risk of several age-related metabolic diseases—thus, it is important to find interventions that can maintain or increase BDNF levels throughout menopause [58].”
BackgroundLevels of biomarkers associated with subconcussive head hits in mixed martial arts fighters
Filho, N. M. D. L., Fernandes, S. G. G., Costa, V., Araújo, D. F. D. S., Godeiro-Junior, C. D. O., Guerra, G. C. B., Guerra, R. O., & Ribeiro, K. M. O. B. D. F. (2024) · PeerJ · doi:10.7717/peerj.17752 · Cited by 2
“Moreover, despite being exercise-induced, serum BDNF quantification corresponds to cerebral production, since muscle-produced BDNF does not appear to be released into the bloodstream ( Matthews VB et al., 2009 ).”
BackgroundKalantarhormozi, M., Afshar, A., Hajeb, F., Bahreini, R., & Afshari, N. (2024) · Медицинский журнал Западного Казахстана · doi:10.18502/wkmj.v66i3.16629 · Cited by 2
“Ultimately, it contributes to muscle atrophy [65, 67].”
BackgroundKrishnamurthy, R., Krishnamoorthy, C., Dietsch, A. M., & Natarajan, S. K. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149287 · Cited by 2
Lactate infusion increases circulating pro-brain-derived neurotrophic factor levels in humans
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Effect of Exercise on Oxidative Stress in Neurological Disorders
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POSSIBLE INVOLVEMENT OF BRAIN-DERIVED NEUROTROPHIC FACTOR IN MALE INFERTILITY
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Alcohol and Brain-Derived Neurotrophic Factor (BDNF)
Martín‐González, C., González‐Arnay, E., Fernández-Rodríguez, C. M., Rodríguez, A. G., & González‐Reimers, E. (2022) · Springer eBooks · doi:10.1007/978-3-030-92392-1_182 · Cited by 2
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-031-40116-9_56 · Cited by 2
Humoral Factors in Humans Participating in Different Types of Exercise and Training
Vega, S. R., Hollmann, W., & Strüder, H. K. (2012) · Springer eBooks · doi:10.1007/978-1-4614-3293-7_8 · Cited by 3
The association between polymorphism of theBDNFgene and cigarette smoking in the Iranian population
Rajabi, A., Khosravi, P., Motevalian, S. A., et al. (2018) · The Journal of Gene Medicine · doi:10.1002/jgm.3052 · Cited by 2
Fatigue and depression improvements on breast cancer survivors practitioners of strength training
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The Impact of Aerobic Fitness on Cognition and Molecular Intermediates
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The effectiveness of physical activity in cardiorehabilitation
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Rogalska, M., Ławicki, S., Błachnio-Zabielska, A. U., Zabielski, P., Roszczyc-Owsiejczuk, K., Janica, J. R., Bogdanowska-Charkiewicz, D., Andrzejuk, A., Dâbrowski, A., Flisiak, R., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26157142 · Cited by 1
“Beyond its well-established role in the central nervous system, BDNF has been increasingly recognized as a regulator of energy balance, glucose metabolism, and inflammatory responses [16–18].”
Brain-derived neurotrophic factor in human cerebrospinal fluid is elevated after exercise
Carr, J. M. J. R., Koep, J. L., Duffy, J. S., Brewster, L. M., Bird, J. D., Monteleone, J. A., Monaghan, T. D. R., Islam, H., Steele, A. R., Howe, C. A., et al. (2026) · Journal of Neurophysiology · doi:10.1152/jn.00068.2026 · Cited by 1
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“The muscle–brain axis is mediated by several exercise-responsive signals, including BDNF, irisin/FNDC5-related pathways and cathepsin B. Skeletal muscle cells can produce BDNF in response to contraction, and BDNF has been linked to AMPK-mediated fat oxidation in muscle [67].”
Excercised Muscles and the Brain
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“Yu Nofuji (Fukuoka, Japan) presented findings showing that physical activity altered serum BDNF levels (15) as well as appreciated the recent data of BDNF as a myokine, that is, a cytokine secreted by skeletal muscles (16).”
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“최근 BDNF의 역할을 보면, 체중과 에너지 항 상성 조절[28]과 골격근의 지방산화대사에도 주요한 역할을 하는 것으 로 나타났다[29].”
Muskelaktivität – Muskelinaktivität: anti-nozizeptive oder pro-nozizeptive Körperstrukur
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Metadata
- Authors
- Matthews, V. B., Åström, M.-B., Chan, M. H. S., Bruce, C. R., Krabbe, K. S., Prelovsek, O., Åkerström, T., Yfanti, C., Broholm, C., Mortensen, O. H., Penkowa, M., Hojman, P., Zankari, A., Watt, M. J., Bruunsgaard, H., Pedersen, B. K., & Febbraio, M. A.
- Affiliations
- Baker Heart and Diabetes Institute (AU)
- University of Copenhagen (DK)
- Monash University (AU)
- Corresponding author
- Pedersen, B. K.
- Febbraio, M. A.
- Venue
- Diabetologia
- Published
- 2009-04-22
- Volume
- 52
- Issue
- 7
- Pages
- 1409-1418
- ISSN
- 0012-186X (ISSN-L)
- 1432-0428
- OpenAlex
- W2083119172
- Semantic Scholar
- 4a8929d0be521f621ff5750ab854a4eab70f134f
- Cited by
- 722
- References
- 45
- Citations by year
- 2026: 33 · 2025: 56 · 2024: 57 · 2023: 48 · 2022: 67 · 2021: 54 · 2020: 54 · 2019: 54 · 2018: 44 · 2017: 45 · 2016: 29 · 2015: 45 · 2014: 29 · 2013: 38 · 2012: 22
- FWCI
- 8.98
- Type
- journal article
- Language
- en
- Update notices
- correction (2015-02-19)
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Diabetologia (publishedVersion)
- PubMed (publishedVersion)
- RMIT Research Repository (RMIT University Library) (submittedVersion)
- Own your potential (DEAKIN) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- Diabetes Australia Research Trust
- Diabetes Australia
- National Research Foundation
- Danmarks Grundforskningsfond (02-512-555, DG 02–512‐555, LSHM-CT-2004-005272, 504–14, LSHM-CT-2004-005272 EXGENESIS)
- Lundbeckfonden
- Novo Nordisk
- Novo Nordisk Fonden
- H. Lundbeck A/S
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- brain-derived neurotrophic factor, skeletal muscle, muscle contraction, fatty acid oxidation, AMPK, physical activity, TrkB, ERK, muscle lipid metabolism
- MeSH terms
- Acetyl-CoA Carboxylase, Animals, Cell Line, Exercise Test, Fats, Humans, Male, Mice, Inbred C57BL, Muscle Contraction, Oxidation-Reduction, Phosphorylation, Signal Transduction, Gene Expression, Muscle, Skeletal, Muscle Fibers, Skeletal, Brain-Derived Neurotrophic Factor, Receptor, trkB, Extracellular Signal-Regulated MAP Kinases, Lipid Metabolism, Mice, Rats, AMP-Activated Protein Kinases
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