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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
Cites
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“pTet-On, encoding the rtTA transactivator [30, 31], and pTetS, encoding the tS silencer [32], were both obtained from Clontech (Palo Alto, CA, USA).”
MethodA Flexible System of Enzymatic Analysis
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Brain-derived Neurotrophic Factor Is Stored in Human Platelets and Released by Agonist Stimulation
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Cited by
Sorted by citations
Items 301–400 of 713
Aerobic exercise delays retinal ganglion cell death after optic nerve injury
He, Y., Wang, L., Zhang, T., Weng, S.-J., Lü, J., & Zhong, Y. (2020) · Experimental Eye Research · doi:10.1016/j.exer.2020.108240 · Cited by 26
Exerkines and redox homeostasis
Félix‐Soriano, E., & Stanford, K. I. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102748 · Cited by 27
Exercise, Neuroprotective Exerkines, and Parkinson’s Disease: A Narrative Review
Mitchell, A. K., Bliss, R. R., & Church, F. (2024) · Biomolecules · doi:10.3390/biom14101241 · Cited by 33
Paoli, A. (2025) · Nutrients · doi:10.3390/nu17040663 · Cited by 30
“Increased expression of BDNF mRNA has been associated with enhanced fat mediated primarily within skeletal muscle, potentially through autocrine and/or paracrine signaling pathways [137].”
Running to save sight: The effects of exercise on retinal health and function
Chu‐Tan, J. A., Kirkby, M., & Natoli, R. (2021) · Clinical and Experimental Ophthalmology · doi:10.1111/ceo.14023 · Cited by 27
Muñoz, B., & Ruíz, N. C. (2024) · Mental health and physical activity · doi:10.1016/j.mhpa.2024.100578 · Cited by 30
Slusher, A. L., WHITEHURST, M. A., Zoeller, R. F., Mock, J. T., Maharaj, A., & Huang, C. (2015) · Journal of Neuroendocrinology · doi:10.1111/jne.12275 · Cited by 29
Hvid, L. G., Nielsen, M. K. F., Simonsen, C., Andersen, M., & Caserotti, P. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.03.019 · Cited by 28
“Lastly, systemic levels of BDNF may not represent true tissue levels in skeletal muscle, as Matthews and colleagues demonstrated that BDNF produced in muscle cells are not all released into circulation (Matthews et al., 2009).”
BackgroundNon-pharmacological Approaches to Cognitive Enhancement
Kelly, A. M. (2015) · Handbook of experimental pharmacology · doi:10.1007/978-3-319-16522-6_14 · Cited by 25
“2009) although muscle (Matthews et al. 2009), endothelial cells (Nakahashi et al.”
Backgroundder Stede, T. V., de Loock, A. V., Turiel, G., Hansen, C. C., Tamariz‐Ellemann, A., Ullrich, M., Lievens, E., Spaas, J., Yigit, N., Anckaert, J., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2024.12.011 · Cited by 26
Xenos, D., Mancinetti, F., Mecocci, P., & Boccardi, V. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102955 · Cited by 26
Galindo, C. L., Soslow, J. H., Brinkmeyer‐Langford, C., Gupte, M., Smith, H., Sengsayadeth, S., Sawyer, D. B., Benson, D. W., Kornegay, J. N., & Markham, L. W. (2015) · Pediatric Research · doi:10.1038/pr.2015.257 · Cited by 23
Gaydukov, A. E., Bogacheva, P. O., Tarasova, E., Molchanova, А. I., Miteva, A. S., Pravdivceva, E., & Balezina, O. P. (2019) · Cells · doi:10.3390/cells8070762 · Cited by 27
“A well-known neurotrophin BDNF has been recently rediscovered as a myokine [2,4,5].”
BackgroundNeuromuscular Performance and Hormonal Responses to Military Operational Stress in Men and Women
Conkright, W. R., Beckner, M. E., Sinnott, A. M., Eagle, S. R., Martin, B. J., LaGoy, A. D., Proessl, F., Lovalekar, M. T., Doyle, T. L. A., Agostinelli, P. J., et al. (2021) · The Journal of Strength and Conditioning Research · doi:10.1519/jsc.0000000000004013 · Cited by 25
“Primarily known for its function as a mediator of neuroplasticity and neurogenesis, BDNF also mediates energy metabolism by decreasing appetite and enhancing lipid oxidation during glucose deprivation through activation of the AMP-activated protein kinase—a master regulator of cellular energy metabolism (21).”
BackgroundExercise and Metabolic Health: The Emerging Roles of Novel Exerkines
Yazgan, B., Türkel, İ., Özerkliğ, B., ATAKAN, M. M., Aktitiz, S., & Koşar, Ş. N. (2022) · Current Protein and Peptide Science · doi:10.2174/1389203723666220629163524 · Cited by 25
With a little help from my friends: Androgens tap BDNF signaling pathways to alter neural circuits
Ottem, E. N., Bailey, D. J., Jordan, C. L., & Breedlove, S. M. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.12.019 · Cited by 24
“This notion is supported by studies that indicate skeletal muscle expresses both BDNF mRNA and protein (Koliatsos et al., 1993; Kust et al., 2002; Saka et al., 2007; Matthews et al., 2009; Garcia et al., 2010; Ogborn and Gardiner, 2010).”
ResultMammalian Target of Rapamycin at the Crossroad Between Alzheimer’s Disease and Diabetes
Liang, H., Nie, J., Skike, C. E. V., Valentine, J. M., & Orr, M. E. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-3540-2_10 · Cited by 24
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Yu, J., Laybutt, D. R., Kim, L.-J., Quek, L.-E., Wu, L. E., Morris, M. J., & Youngson, N. A. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00446.2020 · Cited by 24
Enhanced pro-BDNF-p75NTR pathway activity in denervated skeletal muscle
Aby, K., Antony, R. M., Eichholz, M., Srinivasan, R., & Li, Y. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.120067 · Cited by 28
Chalimoniuk, M., Chrapusta, S. J., Lukáčová, N., & Langfort, J. (2015) · Brain Research · doi:10.1016/j.brainres.2015.05.020 · Cited by 25
Muskelaktivität: Prägung des ZNS und endokrine Funktion
Laube, W. (2013) · Manuelle Medizin · doi:10.1007/s00337-012-0989-1 · Cited by 23
“Zugleich wird der Proteinstoffwechsel der Muskelfasern angeregt und dessen Abbau reduziert.”
BackgroundInfluential- Invited Review - Physiological Roles of Adipokines, Hepatokines, and Myokines in Ruminants
Roh, S., Suzuki, Y., Gotoh, T., Tatsumi, R., & Katoh, K. (2015) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.16.0001r · Cited by 24
“Although BNDF was thought to be a neuron-related factor, induction of BNDF expression in the muscle was observed following both exercise and electrical stimulation (and contraction) of skeletal muscle (Seidl et al., 1998; Copray et al., 2000; Gómez-Pinilla et al., 2002; Matthews et al., 2009).”
BackgroundWalsh, J. J., Bentley, R. F., Gurd, B. J., & Tschakovsky, M. E. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00746 · Cited by 23
“…shown a return to baseline within 30min of exercise cessation for both platelets (Brunelli et al., 2012) and serum BDNF (Rojas Vega et al., 2006; Matthews et al., 2009; Gilder et al., 2014), a response that is likely the result of splenic reuptake of platelets due to sympathetic withdrawal…”
BackgroundInfluentialBrain‐derived neutrophic factor in adolescents smoking waterpipe: The Irbid TRY
Alomari, M. A., Al‐Sheyab, N., Khabour, O. F., & Alzoubi, K. H. (2018) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2018.03.007 · Cited by 25
Sharifi, M., Hamedinia, M. R., & Hosseini-Kakhak, S. A. (2018) · Physical Education of Students · doi:10.15561/20755279.2018.0507 · Cited by 23
Legaard, G. E., & Pedersen, B. K. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-814593-7.00013-x · Cited by 24
Self-citationDeveloping Insulin and BDNF Mimetics for Diabetes Therapy
Chan, C. B., Ahuja, P., & Ye, K. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666191010160643 · Cited by 24
The role of the brain-derived neurotrophic factor (BDNF) in anorexia nervosa
Trinh, S., Keller, L., Herpertz‐Dahlmann, B., & Seitz, J. (2023) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2023.106069 · Cited by 22
ETHNOPHARMACOLOGY, PHYTOCHEMISTRY AND BIOLOGICAL ACTIVITY OF INULA RACEMOSA HOOK. F: A REVIEW
Firdous, Q., Bhat, M. F., & Hussain, M. M. (2018) · International Journal of Research in Ayurveda and Pharmacy · doi:10.7897/2277-4343.09120 · Cited by 22
Bélanger, J.-C., Bouchard, V., Blanc, J. L., Starnino, L., Welman, M., Chabot-Blanchet, M., Busseuil, D., Chertkow, H. M., D’Antono, B., & Lordkipanidzé, M. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.739045 · Cited by 20
“The studies involving human participants were reviewed and approved by Research Ethics Committee of the Montreal Heart Institute [2011-202 (11-1313)].”
BackgroundMethodBrain-derived neurotrophic factor (BDNF): a multifaceted marker in chronic kidney disease
Afşar, B., & Afşar, R. E. (2022) · Clinical and Experimental Nephrology · doi:10.1007/s10157-022-02268-z · Cited by 22
“Exercise has been reported to increase BDNF in skeletal muscle [21, 72, 73] and BDNF is correlated with higher handgrip strength [74].”
BackgroundBazarian, J. J., Abar, B. W., Merchant‐Borna, K., Pham, D. L., Rozen, E., Mannix, R., Kawata, K., Chou, Y., Stephen, S. J., & Gill, J. (2022) · Journal of Neurotrauma · doi:10.1089/neu.2022.0267 · Cited by 22
Vints, W. A. J., Gökçe, E., Langeard, A., Павлова, Ю., Çevik, Ö. S., Ziaaldini, M. M., Todri, J., Lena, O., Sakkas, G. K., Jak, S., et al. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1213057 · Cited by 29
Hyatt, H. W., Toedebusch, R. G., Ruegsegger, G. N., Mobley, C. B., Fox, C. D., McGinnis, G. R., Quindry, J. C., Booth, F. W., Roberts, M. D., & Kavazis, A. N. (2015) · Physiological Reports · doi:10.14814/phy2.12619 · Cited by 22
“BDNF can increase lipid oxidation (Matthews et al. 2009).”
Alomari, M. A., Khabour, O. F., Alawneh, K. M., Alzoubi, K. H., & Maikano, A. B. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03490 · Cited by 23
Physical Activity, Exerkines, and Their Role in Cancer Cachexia
Bilski, J., Szlachcic, A., Ptak‐Belowska, A., & Brzozowski, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26168011 · Cited by 24
Hansen, S. L., Lorentzen, J., Pedersen, L. T., Hendrich, F. L., Jorsal, M., Pingel, J., Nielsen, J. B., & Kiens, B. (2019) · Nutrients · doi:10.3390/nu11030620 · Cited by 22
“However, although the major production of BDNF is in the brain, peripheral tissue such as skeletal muscle [68] and brown and white adipose tissue [69] can also produce BDNF and may add to the concentration of circulating BDNF.”
BackgroundThivel, D., Julian, V., Miguet, M., Pereira, B., Beaulieu, K., Finlayson, G., Richard, R., & Duclos, M. (2019) · Physiology & Behavior · doi:10.1016/j.physbeh.2019.112744 · Cited by 21
Muscle-brain communication in pain: The key role of myokines
Wang, Y., Wu, Z., Wang, D., Huang, C., Xu, J., Liu, C., & Yang, C. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.11.017 · Cited by 21
Age-related differences in plasma BDNF levels after prolonged bed rest
Soavi, C., Marušič, U., Sanz, J. M., Morieri, M. L., Nora, E. D., Šimunič, B., Pišot, R., Zuliani, G., & Passaro, A. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01111.2015 · Cited by 21
“A massive presence of BDNF in platelets and in skeletal muscle was also described, but whereas platelet release upon activation does not seem to explain the variations in circulating BDNF occurring with aging or exercise (26, 40), skeletal muscle was demonstrated not to be a source of circulating BDNF (31, 37).”
BackgroundSbardelotto, M. L., Pedroso, G. S., Pereira, F. T., Sorato, H. R., Brescianini, S. M. S., Effting, P. S., Thirupathi, A., Nesi, R. T., Silveira, P. C., & Pinho, R. A. (2017) · Aging and Disease · doi:10.14336/ad.2017.0209 · Cited by 21
“BDNF is a neurotrophin related to growth, differentiation, and neuronal plasticity that has many peripheral sources such as epithelial and vascular cells [40], macrophages and leucocytes [41], and muscle cells [42], which all have been shown to synthesize and release BDNF.”
BackgroundBarman, H. A. (2019) · The Anatolian Journal of Cardiology · doi:10.14744/anatoljcardiol.2019.37941 · Cited by 21
Effects of hippotherapy on brain function, BDNF level, and physical fitness in children with ADHD
Lee, N., Park, S., & Kim, J. (2015) · Physical Activity and Nutrition · doi:10.5717/jenb.2015.15061209 · Cited by 21
“These changes particularly pertain to the activated cellular energy metabolism and adenosine monophosphate-activated protein kinase (AMPK) enhancement that improves lipid metabolism in skeletal muscles [28,29].”
BackgroundEmerging Insights into the Role of BDNF on Health and Disease in Periphery
Ichimura‐Shimizu, M., Kurrey, K., Miyata, M., Dezawa, T., Tsuneyama, K., & Kojima, M. (2024) · Biomolecules · doi:10.3390/biom14040444 · Cited by 20
Ceylan, H. İ., Silva, A. F., Ramírez‐Campillo, R., & Murawska‐Ciałowicz, E. (2024) · Biology · doi:10.3390/biology13050323 · Cited by 28
Żebrowska, A., Sikora, M., Konarska-Rawluk, A., Zwierzchowska, A., Kamiński, T., Robins, A., & Hall, B. (2020) · Therapeutic Advances in Endocrinology and Metabolism · doi:10.1177/2042018820925326 · Cited by 24
García‐Suárez, P. C., Rentería, I., Moncada‐Jiménez, J., Fry, A. C., & Jiménez‐Maldonado, A. (2020) · Dose-Response · doi:10.1177/1559325820970818 · Cited by 22
Synaptic retrograde regulation of the PKA-induced SNAP-25 and Synapsin-1 phosphorylation
Polishchuk, A., Cilleros‐Mañé, V., Just‐Borràs, L., Balanyà-Segura, M., Pont, G. V., Simón, C. S., Tomàs, M., García, N., Tomàs, J. M., & Lanuza, M. A. (2023) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-023-00431-2 · Cited by 20
“Muscle contraction enhances BDNF levels in vitro and in vivo [54, 55], and this BDNF/TrkB signaling retrogradely regulates presynaptic isoforms of PKC and the neurotransmission machinery [38, 39, 55].”
BackgroundIda, S., Murata, K., Nakai, M., Ito, S., Malmstrom, T. K., Ishihara, Y., Imataka, K., Uchida, A., Monguchi, K., Kaneko, R., et al. (2018) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.13461 · Cited by 21
Neurotrophic factor BDNF is upregulated in soft palate muscles of snorers and sleep apnea patients
Shah, F. K., Forsgren, S., Holmlund, T., Jäghagen, E. L., Berggren, D., Franklin, K. A., & Stål, P. (2018) · Laryngoscope Investigative Otolaryngology · doi:10.1002/lio2.225 · Cited by 20
Effect of exercise training on the FNDC5/BDNF pathway in spontaneously hypertensive rats
Wang, T., Maltez, M. T., Lee, H. W., Ahmad, M., Wang, H., & Leenen, F. H. H. (2019) · Physiological Reports · doi:10.14814/phy2.14323 · Cited by 22
“In skeletal muscle, it contributes to muscle regeneration (Yu, Chang, Gao, Li, & Zhao, 2017) and fat metabolism (Matthews et al., 2009).”
BackgroundMarconcin, P., Peralta, M., Ferrari, G., de Matos, M. G., Espanha, M., Murawska‐Ciałowicz, E., & Marques, A. (2020) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph17196942 · Cited by 21
“BDNF could be considered as a novel contraction-induced myokine [53].”
BackgroundClos, P., Lepers, R., & Garnier, Y. M. (2021) · European Journal of Applied Physiology · doi:10.1007/s00421-020-04575-3 · Cited by 19
The Potential Roles of Myokines in Adipose Tissue Metabolism with Exercise and Cold Exposure
Jiang, S., Bae, J. H., Wang, Y., & Song, W. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911523 · Cited by 20
“Although mainly released from the brain, known as a factor improving cognitive function, BDNF was also identified as a contraction-regulated myokine capable of enhancing AMPK activation and, hence, lipid oxidation [74].”
BackgroundGanse, B., Bosutti, A., Drey, M., & Degens, H. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112463 · Cited by 23
Dubé, C., Aguer, C., Adamo, K. B., & Bainbridge, S. A. (2017) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2016-0446 · Cited by 20
Brandli, A. A., Johnstone, D. M., & Stone, J. (2016) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.16-19361 · Cited by 18
A Physiologically Based Approach to Prescribing Exercise Following a Sport-Related Concussion
Worts, P. R., Burkhart, S. O., & Kim, J. (2019) · Sports Medicine · doi:10.1007/s40279-019-01065-1 · Cited by 21
Malczynska-Sims, P., Chalimoniuk, M., & Sułek, A. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.578981 · Cited by 19
Goldfield, G. S., Walsh, J. J., Sigal, R. J., Kenny, G. P., Hadjiyannakis, S., Lisio, M. D., Ngu, M., Prud’homme, D., Alberga, A. S., Doucette, S. P., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.715330 · Cited by 18
Gaggi, G., Credico, A. D., Guarnieri, S., Mariggiò, M. A., Baldassarre, A. D., & Ghinassi, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.936990 · Cited by 19
“In this scenario, the hypothesis that the myotubes may produce some molecules, such as neurotropic factors, cytokines, exosomes or microparticles (Matthews et al., 2009; Di Credico et al., 2020; Di Credico et al., 2021b; Saini et al., 2021), that might increase the support the maturation of hAFSC-derived MNs cannot be…”
BackgroundDeng, C., & Chen, H. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106377 · Cited by 18
Behnoush, A. H., Khalaji, A., Naghibi, A. F., Bagheri, K. H., Goshtasbi, P., Mohseni, G., Kanty, A. E. E., Vinciguerra, C., & Cannavò, A. (2024) · ESC Heart Failure · doi:10.1002/ehf2.14916 · Cited by 19
“27,55 Therefore, assessing BDNF levels may represent an important diagnostic and prognostic tool for cardiovascular disease and HF and this is a central fi nding of our study.”
BackgroundGaede, G., Hellweg, R., Zimmermann, H. G., Brandt, A. U., Dörr, J., Bellmann–Strobl, J., Zangen, A., Paul, F., & Pfueller, C. F. (2014) · Neuropsychobiology · doi:10.1159/000358088 · Cited by 18
Colitti, M., & Montanari, T. (2020) · Tissue and Cell · doi:10.1016/j.tice.2020.101388 · Cited by 18
Motor activity affects adult skeletal muscle re‐innervation acting via tyrosine kinase receptors
Sartini, S., Bartolini, F., Ambrogini, P., Betti, M., Ciuffoli, S., Lattanzi, D., Palma, M. D., & Cuppini, R. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12130 · Cited by 18
Himmerich, H., Keeler, J. L., King, J. A., Ehrlich, S., Kaufmann, L., Bulik, C. M., Cohen‐Woods, S., Wade, T. D., Steiger, H., Booij, L., et al. (2026) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2026.2626934 · Cited by 24
Cerebral Benefits Induced by Electrical Muscle Stimulation: Evidence from a Human and Rat Study
Chaney, R., Leger, C., Wirtz, J., Fontanier, E., Méloux, A., Quirié, A., Martin, A., Prigent‐Tessier, A., & Garnier, P. E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031883 · Cited by 19
“Indeed, BDNF is produced in skeletal muscle by various cell types [32,61] and was reported to play a role in muscle regeneration and metabolism [62–64].”
BackgroundAdipocytokines, gut hormones and growth factors in anorexia nervosa
Kowalska, I., Karczewska‐Kupczewska, M., & Strączkowski, M. (2011) · Clinica Chimica Acta · doi:10.1016/j.cca.2011.06.007 · Cited by 18
Jiménez‐Maldonado, A., Cortés, J. C., Castro-Rodríguez, E. M., Montero, S., Muñı́z, J., Rodríguez‐Hernández, A., Lemus, M., & de Álvarez-Buylla, E. R. (2015) · Muscle & Nerve · doi:10.1002/mus.24757 · Cited by 17
Kim, H.-J., So, B., Son, J. S., Song, H. S., Oh, S. L., Seong, J. K., Lee, H., & Song, W. J. (2015) · Physical Activity and Nutrition · doi:10.5717/jenb.2015.15112402 · Cited by 18
“Also, BDNF is thought to be a regulator of metabolism in skeletal muscles [9] and an enhancer of glucose utilization in diabetic skeletal muscles [10].”
BackgroundArvidsson, D., Johannesson, E., Andersen, L. B., Karlsson, M. K., Wollmer, P., Thorsson, O., & Dencker, M. (2018) · Journal of Physical Activity and Health · doi:10.1123/jpah.2017-0483 · Cited by 17
Pereira, E. S., Neto, W. K., Calefi, A. S., Georgetti, M., Guerreiro, L., Zocoler, C. A. S., & Gama, E. F. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00823 · Cited by 19
Colitti, M., Boschi, F., & Montanari, T. (2018) · European Journal of Histochemistry · doi:10.4081/ejh.2018.2984 · Cited by 17
de Assis, G. G., Hoffman, J. R., Bojakowski, J., Murawska‐Ciałowicz, E., Cięszczyk, P., & Gasanov, E. V. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.638176 · Cited by 17
Passaro, A., Soavi, C., Marušič, U., Rejc, E., Sanz, J. M., Morieri, M. L., Nora, E. D., Kavcic, V., Narici, M. V., Reggiani, C., et al. (2017) · Aging · doi:10.18632/aging.101166 · Cited by 16
“At muscular level, muscle BDNF can increase fatty acid oxidation, ameliorating energy afflux in an autocrine/ paracrine manner [17].”
Besser, R. R., Bowles, A. C., Alassaf, A., Carbonero, D., Maciel, R., Saporta, M. D. C., & Agarwal, A. (2020) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-020-00624-1 · Cited by 14
Nayasista, A. H., Tinduh, D., Pawana, I. P. A., Wulan, S. M. M., Utomo, D. N., & Melaniani, S. (2022) · Annals of Medicine and Surgery · doi:10.1016/j.amsu.2022.103800 · Cited by 16
Rehabilitation and the Neural Network After Stroke
Shimamura, N., Katagai, T., Kakuta, K., Matsuda, N., Katayama, K., Fujiwara, N., Watanabe, Y., Naraoka, M., & Ohkuma, H. (2017) · Translational Stroke Research · doi:10.1007/s12975-017-0550-6 · Cited by 16
Identification of CCL5/RANTES as a novel contraction-reducible myokine in mouse skeletal muscle
Ishiuchi, Y., Sato, H., Komatsu, N., Kawaguchi, H., Matsuwaki, T., Yamanouchi, K., Nishihara, M., & Nedachi, T. (2018) · Cytokine · doi:10.1016/j.cyto.2018.03.012 · Cited by 17
Copeland, E. N., LeBlanc, P. J., Duarte‐Guterman, P., Fajardo, V. A., & MacPherson, R. E. K. (2025) · The Journal of Physiology · doi:10.1113/jp288032 · Cited by 16
“Previous work concluded that BDNF is not secreted into circulation by skeletal muscle (Matthews et al., 2009); however, there is new evidence suggesting that muscle is capable of releasing BDNF into circulation.”
Histone Deacetylases as Modulators of the Crosstalk Between Skeletal Muscle and Other Organs
Renzini, A., D’Onghia, M., Coletti, D., & Moresi, V. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.706003 · Cited by 15
Polishchuk, A., Cilleros‐Mañé, V., Balanyà-Segura, M., Just‐Borràs, L., Forniés-Mariné, A., Silvera-Simón, C., Tomàs, M., Jami-ElHirchi, M., Hurtado, E., Tomàs, J. M., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01735-2 · Cited by 15
“In the peripheral nervous system, BDNF is a contraction-inducible molecule [10, 11] that, by binding to TrkB in the nerve terminal membrane, contributes to the retrograde neuroprotective control done by muscles, which is necessary for the proper function of motor neurons [12, 50].”
BackgroundRunning and Swimming Differently Adapt the BDNF/TrkB Pathway to a Slow Molecular Pattern at the NMJ
Just‐Borràs, L., Cilleros‐Mañé, V., Hurtado, E., Biondi, O., Charbonnier, F., Tomàs, M., García, N., Tomàs, J. M., & Lanuza, M. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094577 · Cited by 17
“BDNF is strongly expressed in skeletal muscle in response to muscle contraction [3,38].”
BackgroundResultInfluentialCosta, H. S., Lima, M. M. O., Figueiredo, P. H. S., Martinelli, P. M., Camargos, E. R. S., Chaves, A. T., Nunes, M. C. P., & Rocha, M. O. D. C. (2018) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/0074-02760180224 · Cited by 15
“Both skeletal(22) and cardiac muscles(23) are important sources of BDNF.”
BackgroundGoldfield, G. S., Cameron, J. D., Sigal, R. J., Kenny, G. P., Holčı́k, M., Prud’homme, D., Guérin, E., Alberga, A. S., D’Angiulli, A., Tremblay, M. S., et al. (2021) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2020-0756 · Cited by 17
Goulet, N., McCormick, J. J., King, K. E., Notley, S. R., Goldfield, G. S., Fujii, N., Amano, T., & Kenny, G. P. (2023) · Temperature · doi:10.1080/23328940.2023.2176107 · Cited by 14
“Additionally, previous observations on the acute effects of prolonged exercise are limited to healthy young adults [19,20].”
BackgroundCao, J., Gorwood, P. A. P. M., Ramoz, N., & Viltart, O. (2024) · Nutrients · doi:10.3390/nu16162617 · Cited by 17
“Adipose tissue-derived BDNF also plays a crucial role in metabolism by regulating local processes in white adipose tissue, such as sympathetic innervation, mitochondrial function, and susceptibility to obesity-related challenges [136,140,141].”
BackgroundBrinza, I., Boiangiu, R. Ş., Mihăşan, M., Gorgan, L., Stache, A. B., Abd-Alkhalek, A. M., El‐Nashar, H. A. S., Ayoub, I. M., Mostafa, N. M., Eldahshan, O. A., et al. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.177013 · Cited by 16
Pang, B. P. S., Iu, E. C. Y., Hang, M., Chan, W. S., Tse, M. C. L., Yeung, C. T. Y., Wang, M., Siu, P. M., Lee, C. W., Ye, K., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103418 · Cited by 17
“Nevertheless, several fragmented studies have shown that BDNF promotes muscle regeneration and myofiber differentiation [20,21], enhances intramyocellular lipid catabolism [22,23], and controls systemic glucose metabolism via triggering insulin synthesis [24].”
Lee, S. Y., Chen, S., Chang, Y., Chen, P.-S., Huang, S., Tzeng, N., Wang, C.-L., Wang, L.-J., Lee, I., Wang, T., et al. (2014) · Acta Psychiatrica Scandinavica · doi:10.1111/acps.12324 · Cited by 14
“BDNF is stored in circulating platelets; found in muscles, the heart, and the gonads; and found in the central and peripheral nervous systems (52, 53).”
BackgroundUrinary Brain-Derived Neurotrophic Factor as a Biomarker of Executive Functioning
Koven, N. S., & Collins, L. R. (2014) · Neuropsychobiology · doi:10.1159/000362242 · Cited by 14
Brass, E. P., Peters, M. A., Hinchcliff, K. W., He, Y. D., & Ulrich, R. G. (2009) · Journal of Applied Physiology · doi:10.1152/japplphysiol.91347.2008 · Cited by 14
“The muscle biopsies used contain a number of different cell types, and muscle BDNF has been suggested to arise from nerves (15), vasculature (23), satellite cells (31), as well as myocytes (29).”
BackgroundThermogenesis and Related Metabolic Targets in Anti-Diabetic Therapy
Arch, J. R. S. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-17214-4_10 · Cited by 14
Jiménez‐Maldonado, A., Virgen‐Ortiz, A., Melnikov, V., et al. (2016) · Islets · doi:10.1080/19382014.2016.1260796 · Cited by 14
“Finally, previous reports have indicated that the BDNF participates in the functional regulation of the liver,(37) and skeletal muscle.(38) The present work indicates that besides to liver and skeletal muscle, the BDNF also regulates the Langerhans islet morphometry.”
ResultLauretta, G., Ravalli, S., Maugeri, G., D’Agata, V., Rosa, M. D., & Musumeci, G. (2021) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201022666210405142611 · Cited by 15
Koito, Y., Yanishi, M., Kimura, Y., Tsukaguchi, H., Kinoshita, H., & Matsuda, T. (2021) · Transplantation Proceedings · doi:10.1016/j.transproceed.2021.04.021 · Cited by 15
Hashida, R., Nakano, D., Yamamura, S., Kawaguchi, T., Tsutsumi, T., Matsuse, H., Takahashi, H., Gerber, L. H., Younossi, Z. M., & Torimura, T. (2021) · Life · doi:10.3390/life11080799 · Cited by 13
“BDNF is a myokine that increases in the muscles in response to exercise, and it promotes fatty acid oxidation [19,20].”
BackgroundExerkines and myokines in aging sarcopenia
Wang, H., He, W., Chen, P., Wang, H., Wang, H., Zhu, L., & Liu, X. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1592491 · Cited by 20
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
A language model drew the claims from the paper on 2026-10-09, under version 3 of the claim definition (model deepseek-v4.1-flash, prompt extract-v3).
A second model labelled each claim on 2026-10-09 (model jev-1.13-20260917, definition revision gold-guideline-v0.2).
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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