bims-moremu Biomed News
on Molecular regulators of muscle mass
Issue of 2025–05–04
33 papers selected by
Anna Vainshtein, Craft Science Inc.



  1. Scand J Med Sci Sports. 2025 May;35(5): e70059
      Skeletal muscle is a key determinant of sports performance. It is a highly specialized, yet complex and heterogeneous tissue, comprising multiple cell types. Muscle fibers are the main functional cell type responsible for converting energy into mechanical work. They exhibit a remarkable ability to adapt in response to stressors, such as exercise training. But while it is recognized that human skeletal muscle fibers have distinct contractile and metabolic features, classified as slow/oxidative (type 1) or fast/glycolytic (type 2a/x), less attention has been directed to the adaptability of the different fiber types. Methodological advancements in mass spectrometry-based proteomics allow researchers to quantify thousands of proteins with only a small amount of muscle tissue-even in a single muscle fiber. By exploiting this technology, studies are emerging highlighting that muscle fiber subpopulations adapt differently to exercise training. This review provides a contemporary perspective on the fiber type-specific adaptability to exercise training in humans. A key aim of our review is to facilitate further advancements within exercise physiology by harnessing mass spectrometry proteomics.
    Keywords:  athletes; exercise; muscle adaptations; physical activity; proteomics; training
    DOI:  https://doi.org/10.1111/sms.70059
  2. Exerc Sport Sci Rev. 2025 May 01.
       ABSTRACT: Our Perspective for Progress highlights sex differences in skeletal muscle mitochondrial function that evolve with aging, with an influence of denervation emerging in advanced age. Gaps include knowledge about mitochondrial alterations in microdomains of muscle fibers, plasticity of the mitochondrial reticulum to acute muscle contractions, and advanced age of both sexes.
    Keywords:  Mitochondria; aging; denervation; heterogeneity; skeletal muscle
    DOI:  https://doi.org/10.1249/JES.0000000000000364
  3. Am J Physiol Cell Physiol. 2025 May 02.
      Radiation therapy causes long-term skeletal muscle atrophy and fibrosis in juvenile cancer survivors. The mechanisms responsible for the skeletal muscle late effects of radiation therapy are not well-understood and have prevented the development of effective treatments. Using single-cell RNA sequencing (scRNA-seq), we characterize cellular dynamics and communication in a murine model of therapeutic radiation at 24-hours and 56-days post-irradiation (post-IR). We detected changes in muscle stem (satellite) cells (MuSCs) characterized by an acute preservation of committed MuSCs and long-term relative depletion of deep quiescent MuSCs. A conserved senescence Cdkn1a signature was observed in all muscle-resident cells post-IR. Genes related to fibroblast proliferation were up-regulated and a fibrotic and senescent transcriptome persisted in Fibro-adipogenic progenitors (FAPs) post-IR. Intercellular communication analysis revealed FAPs as the primary contributor of extracellular matrix (ECM) and target of monocyte/macrophage-derived TGF-β signalling post-IR through TGF-βR2 on FAPs. Together, our findings provide insights into the potential mechanisms and intercellular communication responsible for radiation-induced muscle atrophy and fibrosis.
    Keywords:  cancer cachexia; fibro-adipogenic progenitors; fibrosis; pediatric cancer; single-cell RNA sequencing
    DOI:  https://doi.org/10.1152/ajpcell.00115.2025
  4. Sci Rep. 2025 Apr 28. 15(1): 14865
      The neuromuscular junction (NMJ) is the unique interface between lower motor neurons and skeletal muscle fibers and is indispensable for muscle function. Tight control of its localized formation at the center of every muscle fiber, and maintenance throughout lifetime are sustained by muscle-specific kinase (MuSK). MuSK acts as central regulator of acetylcholine receptor clustering at the postsynapse. Localized and temporally controlled signaling of MuSK is primarily achieved by tyrosine autophosphorylation and inhibition thereof. Previous investigations suggested serine phosphorylation of the activation domain as an additional modulator of MuSK activation. Here we identified calcium/calmodulin dependent protein kinase II (CaMK2) and in particular CaMK2β as novel catalyst of MuSK activation and confirmed its capability to phosphorylate MuSK in heterologous cells. However, whereas CaMK2β absence in muscle cells reduced AChR clustering, MuSK phosphorylation was unchanged. Accordingly, we ruled out MuSK phosphorylation as the cause of synapse fragmentation in a mouse model for myotonic dystrophy type 1, in which the muscle-specific splice-variant of CaMK2β is missing, or as the cause of ataxia or delayed muscle development in CaMK2β knockout animals. Histological characterization of muscles of CaMK2β knockout mice indicated specific roles of CaMK2β in fast glycolytic versus slow oxidative muscle. Taken together, our data shows that MuSK can be phosphorylated by CaMK2β, but loss of CaMK2β is likely compensated by other CaMK2 paralogs at the NMJ.
    DOI:  https://doi.org/10.1038/s41598-025-95053-3
  5. Cell Metab. 2025 Apr 24. pii: S1550-4131(25)00212-8. [Epub ahead of print]
      Nicotinamide adenine dinucleotide (NAD) is a ubiquitous electron carrier essential for energy metabolism and post-translational modification of numerous regulatory proteins. Dysregulations of NAD metabolism are widely regarded as detrimental to health, with NAD depletion commonly implicated in aging. However, the extent to which cellular NAD concentration can decline without adverse consequences remains unclear. To investigate this, we generated a mouse model in which nicotinamide phosphoribosyltransferase (NAMPT)-mediated NAD+ biosynthesis was disrupted in adult skeletal muscle. The intervention resulted in an 85% reduction in muscle NAD+ abundance while maintaining tissue integrity and functionality, as demonstrated by preserved muscle morphology, contractility, and exercise tolerance. This absence of functional impairments was further supported by intact mitochondrial respiratory capacity and unaltered muscle transcriptomic and proteomic profiles. Furthermore, lifelong NAD depletion did not accelerate muscle aging or impair whole-body metabolism. Collectively, these findings suggest that NAD depletion does not contribute to age-related decline in skeletal muscle function.
    Keywords:  NAD metabolism; NAD(+) biosynthesis; NAMPT; aging; epigenetic clock; exercise; mitochondrial supercomplexes; nicotinamide; reactive oxygen species; skeletal muscle
    DOI:  https://doi.org/10.1016/j.cmet.2025.04.002
  6. Front Biosci (Landmark Ed). 2025 Apr 22. 30(4): 36233
       BACKGROUND: Skeletal muscle atrophy is a common musculoskeletal disorder that significantly reduces patient quality of life. Long non-coding RNA (lncRNA) XLOC_015548 has been identified as a pivotal regulator of C2C12 myoblast proliferation and differentiation. However, its role in mitigating denervation-induced muscle atrophy and the underlying mechanisms remain unclear.
    METHODS: We employed lentiviral-mediated stable expression of XLOC_015548 in C2C12 myoblasts and skeletal muscle-specific XLOC_015548-edited mouse models to investigate the function of this lncRNA. Muscle atrophy models were established in vitro by glucocorticoid-induced atrophy with dexamethasone (DEX) and in vivo by sciatic nerve transection-induced denervation. The MEK inhibitor U0126 was used to assess the role of the growth arrest and DNA damage-inducible 45 gamma/mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (Gadd45g/MEK/ERK) signaling pathway.
    RESULTS: Overexpression of XLOC_015548 significantly activated the MEK/ERK signaling pathway (p < 0.05) by downregulating Gadd45g expression (p < 0.05) and promoting its cytoplasmic localization, thereby enhancing cell proliferation and myotube formation. Furthermore, XLOC_015548 reduced the level of reactive oxygen species (ROS) (p < 0.01), stabilized the mitochondrial membrane potential, and alleviated DEX-induced oxidative stress. These protective effects were partially reversed by U0126, confirming the involvement of the MEK/ERK pathway. Skeletal muscle-specific overexpression of XLOC_015548 in vivo significantly reduced denervation-induced muscle atrophy (q < 0.05) and increased the muscle fiber cross-sectional area.
    CONCLUSION: XLOC_015548 plays a critical role in promoting myogenic differentiation and protecting against muscle atrophy by regulating Gadd45g expression, activating the MEK/ERK signaling pathway, and reducing oxidative stress. These findings underscore the therapeutic potential of XLOC_015548 in skeletal muscle atrophy, and provide a foundation for lncRNA-based treatment strategies.
    Keywords:  XLOC_015548; long non-coding RNA; myogenic differentiation; oxidative stress; skeletal muscle atrophy
    DOI:  https://doi.org/10.31083/FBL36233
  7. J Mol Med (Berl). 2025 May 03.
      Muscle fatty infiltration (MFI) was characterized by the pathological accumulation of fat within skeletal muscle tissue. Previous studies have found that the progress of this pathological phenomenon in aging, acute muscle injury, and other conditions was triggered by the activation and adipogenic differentiation of the key cell population, fibro/adipogenic progenitors (FAPs), but there were few studies on the fat infiltration caused by disused skeletal muscle atrophy, and the regulatory role of FAPs in this situation has not been deeply explored, leaving the related molecular mechanisms still unknown. In this study, we conducted single-cell RNA sequencing on the disused skeletal muscle. The aberrant proliferation of FAPs in this state was found by subsequent analysis, along with the high expression of the ferroptosis inhibitory gene in the activated FAPs. By immunofluorescence staining, we verified the proliferation and adipogenic differentiation of FAPs, which proved the role of FAPs in fat infiltration of disused skeletal muscle. In order to further verify the relationship between ferroptosis inhibition and FAPs activation/adipogenic differentiation, we used ferrostatin-1, a commonly used ferroptosis inhibitor, to treat skeletal muscle fibroblasts and FAPs in vitro, and verified the enhancement of ferroptosis inhibition on their adipogenic/fibrogenic ability. Our study pinpointed the effect of aberrant activation of FAPs on MFI in disused skeletal muscle, and preliminarily recognized the potential effect of ferroptosis on the adipogenic differentiation of FAPs. KEY MESSAGES: • Muscle fatty infiltration (MFI) was characterized by the pathological accumulation of fat within skeletal muscle. Fibro/adipogenic progenitors (FAPs) were thought to be crucial regulators of MFI, but their correlations in disused skeletal muscle were unspecified. • In this study, we conducted single-cell RNA sequencing on the disused skeletal muscle and recognized the aberrant proliferation of FAPs along with the upregulated ferroptosis inhibition genes in this status. • Subsequently, we used ferrostatin-1 (ferroptosis inhibitor) to treat skeletal muscle fibroblasts in vitro, and verified the enhancement of ferroptosis inhibition on their adipogenic/fibrogenic ability. • Our study pinpointed the effect of aberrant activation of FAPs on MFI in disused skeletal muscle, and preliminarily recognized the potential effect of ferroptosis on the adipogenic differentiation of FAPs.
    Keywords:  Disused muscle atrophy; Ferroptosis; Fibro/adipogenic progenitors; Muscle fatty infiltration
    DOI:  https://doi.org/10.1007/s00109-025-02548-7
  8. bioRxiv. 2025 Apr 11. pii: 2025.04.11.648330. [Epub ahead of print]
      Fibro-Adipogenic Progenitors (FAPs) are mesenchymal stem cells that are vital for muscle homeostasis and regeneration but produce fibrosis and intramuscular fat under pathological conditions. Insulin-like Growth Factor-I (IGF-I) is a key regulator of muscle repair, satellite cell activity, macrophage polarization, and extracellular matrix (ECM) remodeling. We generated inducible FAP-specific Igf1 deficient (FID) mice to determine the necessity of FAP IGF-I. After BaCl 2 injury, FID mice exhibited impaired muscle regeneration, with fewer Pax7+ cells, increased macrophage accumulation, smaller fibers, reduced ECM, and depressed FAP proliferation. Following glycerol injury, FID muscles exhibited reduced adipocyte accumulation. Primary FAPs isolated from injured FID muscles had blunted growth, upregulation of immune-regulatory genes and downregulation of ECM and cell proliferation genes, with delayed responses to fibrogenic and to adipogenic media. FAP property alterations were already present in homeostatic muscle, indicated by scRNASeq, with decreased indices of protein translation and ECM production as well as increased markers of senescence, confirmed in vivo and in vitro . Overall, FAP IGF-I is a critical autocrine factor, with further paracrine consequences for muscle regenerative capacity.
    DOI:  https://doi.org/10.1101/2025.04.11.648330
  9. Aging Cell. 2025 Apr 25. e70054
      Age-related skeletal muscle atrophy, known as sarcopenia, is characterized by loss of muscle mass, strength, endurance, and oxidative capacity. Although exercise has been shown to mitigate sarcopenia, the underlying governing mechanisms are poorly understood. Mitochondrial dysfunction is implicated in aging and sarcopenia; however, few studies explore how mitochondrial structure contributes to this dysfunction. In this study, we sought to understand how aging impacts mitochondrial three-dimensional (3D) structure and its regulators in skeletal muscle. We hypothesized that aging leads to remodeling of mitochondrial 3D architecture permissive to dysfunction and is ameliorated by exercise. Using serial block-face scanning electron microscopy (SBF-SEM) and Amira software, mitochondrial 3D reconstructions from patient biopsies were generated and analyzed. Across five human cohorts, we correlate differences in magnetic resonance imaging, mitochondria 3D structure, exercise parameters, and plasma immune markers between young (under 50 years) and old (over 50 years) individuals. We found that mitochondria are less spherical and more complex, indicating age-related declines in contact site capacity. Additionally, aged samples showed a larger volume phenotype in both female and male humans, indicating potential mitochondrial swelling. Concomitantly, muscle area, exercise capacity, and mitochondrial dynamic proteins showed age-related losses. Exercise stimulation restored mitofusin 2 (MFN2), one such of these mitochondrial dynamic proteins, which we show is required for the integrity of mitochondrial structure. Furthermore, we show that this pathway is evolutionarily conserved, as Marf, the MFN2 ortholog in Drosophila, knockdown alters mitochondrial morphology and leads to the downregulation of genes regulating mitochondrial processes. Our results define age-related structural changes in mitochondria and further suggest that exercise may mitigate age-related structural decline through modulation of mitofusin 2.
    Keywords:  3D reconstruction; MFN‐2; aging; exercise; human skeletal muscle; mitochondria
    DOI:  https://doi.org/10.1111/acel.70054
  10. J Clin Invest. 2025 May 01. pii: e173354. [Epub ahead of print]135(9):
      Collagen VI-related disorders (COL6-RDs) are a group of rare muscular dystrophies caused by pathogenic variants in collagen VI genes (COL6A1, COL6A2, and COL6A3). Collagen type VI is a heterotrimeric, microfibrillar component of the muscle extracellular matrix (ECM), predominantly secreted by resident fibroadipogenic precursor cells in skeletal muscle. The absence or mislocalization of collagen VI in the ECM underlies the noncell-autonomous dysfunction and dystrophic changes in skeletal muscle with a yet elusive direct mechanistic link between the ECM and myofiber dysfunction. Here, we conducted a comprehensive natural history and outcome study in a mouse model of COL6-RDs (Col6a2-/- mice) using standardized (TREAT-NMD) functional, histological, and physiological parameters. Notably, we identify a conspicuous dysregulation of the TGF-β pathway early in the disease process and propose that the collagen VI-deficient matrix is not capable of regulating the dynamic TGF-β bioavailability both at baseline and in response to muscle injury. Thus, we propose a new mechanism for pathogenesis of the disease that links the ECM regulation of TGF-β with downstream skeletal muscle abnormalities, paving the way for the development and validation of therapeutics that target this pathway.
    Keywords:  Extracellular matrix; Genetic diseases; Genetics; Growth factors; Muscle biology
    DOI:  https://doi.org/10.1172/JCI173354
  11. Front Physiol. 2025 ;16 1554222
      Exercise and physical activity confer health advantages, in part, by enhancing skeletal muscle mitochondrial respiratory function. The objective of this study is to analyze the impacts of high-intensity interval training (HIIT) and moderate-intensity continuous training (MICT) on the dynamics and functionality of the mitochondrial network within skeletal muscle. 20 young male participants were assigned to either HIIT or MICT group. Initial assessments of exercise-related indicators were conducted, followed by skeletal muscle biopsies from the vastus lateralis before, 1 day after, and 6 weeks post-experiment. We utilized multi-dimensional myofiber imaging to analyze mitochondrial morphology and arrangement, and assessed citrate synthase activity, complex I activity, and dynamics-related mRNA. Both training modalities increased VO2max, Wmax, citrate synthase and complex I activities, mitochondrial content, and volume density, though the changes differed between the two groups. 6 weeks training induced remodeling of the mitochondrial network within skeletal muscle. Before training, the network appeared sparse and punctate. After MICT, it adopted a grid-like structure with partially robust longitudinal connections. In contrast, HIIT resulted in a less obvious grid structure but showed a stronger longitudinally oriented network. Training also increased mRNA expression of mitochondrial fusion proteins and decreased fission protein expression, with these effects being more pronounced in HIIT. Similarly, peroxisome proliferator-activated receptor γ coactivator 1-alpha mRNA expression showed a comparable trend, though the changes differed between 1 day and 6 weeks of training. In conclusion, HIIT and MICT induce distinct mitochondrial adaptation in skeletal muscle, reflected in different network remodeling and molecular pathways. These findings may be due to HIIT's more pronounced effect on mitochondrial dynamics or respiratory function, but the study has only conducted preliminary observational experiments and further evidence is required for confirmation.
    Keywords:  high-intensity interval training; mitochondrial dynamics; mitochondrial network remodeling; moderate-intensity interval training; skeletal muscle
    DOI:  https://doi.org/10.3389/fphys.2025.1554222
  12. Cell Mol Life Sci. 2025 Apr 28. 82(1): 178
      Balanced mTOR activity and iron levels are crucial for muscle integrity, with evidence suggesting mTOR regulates cellular iron homeostasis. In this study, we investigated iron metabolism in muscle-specific mTOR knockout mice (mTORmKO) and its relation to their myopathy. The mTORmKO mice exhibited distinct iron content patterns across muscle types and ages. Slow-twitch soleus muscles initially showed reduced iron levels in young mice, which increased with the dystrophy progression but remained within control ranges. In contrast, the less affected fast-twitch muscles maintained near-normal iron levels from a young age. Interestingly, both mTORmKO muscle types exhibited iron metabolism markers indicative of iron excess, including decreased transferrin receptor 1 (TFR1) and increased levels of ferritin (FTL) and ferroportin (FPN) proteins. Paradoxically, these changes were accompanied by downregulated Ftl and Fpn mRNA levels, indicating post-transcriptional regulation. This discordant regulation resulted from disruption of key iron metabolism pathways, including NRF2/NFE2L2, HIFs, and AKT/PKB signaling. Mechanistically, mTOR deficiency impaired transcriptional regulation of iron-related genes mediated by NRF2 and HIFs. Furthermore, it triggered ferritin accumulation through two NRF2 mechanisms: (1) derepression of ferritin translation via suppression of the FBXL5-IRP axis, and (2) autophagosomal sequestration driven by NCOA4-dependent ferritin targeting to autophagosomes, coupled with age-related impairments of autophagy linked to chronic AKT/PKB activation. Three-week spermidine supplementation in older mTORmKO mice was associated with normalized AKT/PKB-FOXO signaling, increased endolysosomal FTL and reduced total FTL levels in the dystrophic soleus muscle. These findings underscore mTOR's crucial role in skeletal muscle iron metabolism and suggest spermidine as a potential strategy to address impaired ferritinophagy due to autophagy blockade in dystrophic muscle.
    Keywords:  Autophagy; Dystrophy; Glycogen; Iron-sulfur cluster; Myoglobin; Oxidative stress
    DOI:  https://doi.org/10.1007/s00018-025-05695-9
  13. Cell Mol Biol Lett. 2025 Apr 30. 30(1): 53
       BACKGROUND: Sarcopenia, characterized by a progressive loss of skeletal muscle mass and function, is associated with the accumulation of senescent muscle stem cells, which impair muscle regeneration and contributes to the decline in muscle health. Cdkn1a, which encodes p21, is a well-known marker of cellular senescence. However, it remains unclear whether p21 inhibition eliminates senescent myoblasts and restores the differentiation capacity.
    METHODS: We performed transcriptomic analysis to identify genes related to aging-induced sarcopenia using 21 month-old Sprague-Dawley rats. To investigate the specific role of Cdkn1a gene in muscle aging, we used an in vitro model of ceramide-induced senescence in myoblasts, which was verified by the upregulation of p21 and increased senescence-associated beta-galactosidase (SA-β-gal) staining. To inhibit p21, we treated myoblasts with small interfering RNA (siRNA) targeting Cdkn1a. Using fluorescence-activated cell sorting, we separated subpopulations of cells with high or low caspase 3/7 activity. Protein expression related to myogenesis, muscle atrophy, protein synthesis, and apoptosis were quantified by western blotting.
    RESULTS: In our transcriptomic analysis, we identified Cdkn1a as an upregulated gene in both the soleus and white gastrocnemius muscles of aged rats, among 36 commonly upregulated genes. The upregulation of Cdkn1a appears to be linked to mitochondrial dysfunction and cellular senescence, underscoring its significance in sarcopenia pathogenesis. C2-ceramide treatment effectively induced senescence, as evidenced by increased p21 expression, enhanced SA-β-gal staining, decreased myogenesis, and increased apoptosis. Knockdown of p21 in ceramide-treated myoblasts significantly reduced SA-β-gal-positive cells, restored cell proliferation, reduced the expression of senescence-associated cytokines (i.e., interleukin (IL)-6 and tumor necrosis factor (TNF)-α), and selectively induced apoptosis in the senescent cell population, demonstrating a senolytic effect. Notably, p21 inhibition also improved differentiation of myoblasts into myotubes, as indicated by increased myosin heavy chain expression and improvements in myotube diameter and fusion index.
    CONCLUSIONS: Our data suggest that p21 inhibition selectively eliminates senescent cells while simultaneously enhancing the regenerative capacity of healthy myoblasts, which may combine to improve muscle regeneration and promote myogenesis, ultimately improving muscle health and function in aged individuals.
    Keywords:   Cdkn1a ; Myogenesis; Sarcopenia; Senescence; Senolysis; p21
    DOI:  https://doi.org/10.1186/s11658-025-00731-9
  14. Pathol Res Pract. 2025 Apr 17. pii: S0344-0338(25)00174-8. [Epub ahead of print]270 155982
      Heart failure (HF) is a structural or functional abnormality of the heart, often accompanied by skeletal muscle atrophy and other complications. Exercise plays an important role in preventing muscle atrophy. However, the underlying molecular mechanisms related to skeletal muscle atrophy in HF still remain poorly understood. In this study, we constructed an HF rat model by abdominal aortic coarctation (AAC) and a C2C12 muscle atrophy cell model induced by angiotensin II (Ang II). The relevant protein expressions were analyzed using western blotting. The damage of myocardial tissue, gastrocnemius tissue and cells were assessed through echocardiography, ELISA, HE staining, and immunofluorescence staining. Findings from this study indicated that moderate exercise has beneficial effects on pathological damage in the myocardial and gastrocnemius tissues of rats, resulting in a reduction of NT-proBNP levels in the blood. Furthermore, it was observed that the expression levels of MAFbx and MuRF1 were downregulated, while MHC and MyoD expressions were elevated, and the expression of endoplasmic reticulum stress (ERS)-related proteins GRP78, p-eIF2α, p-IRE1α, p-PERK, CHOP, ATF6 was inhibited, and finally alleviated HF-induced skeletal muscle atrophy. The mechanism involves moderate exercise working to alleviate ERS by inhibiting the MAPK/SOCS3 signaling pathway, thus alleviating skeletal muscle atrophy induced by HF. Our study elucidates the positive role of moderate exercise in HF-induced skeletal muscle atrophy, reveals its potential molecular mechanism, and provides a new scientific basis for the comprehensive treatment of skeletal muscle atrophy in HF.
    Keywords:  Endoplasmic reticulum stress; Exercise; Heart failure; MAPK signaling pathway; SOCS3; Skeletal muscle atrophy
    DOI:  https://doi.org/10.1016/j.prp.2025.155982
  15. Adv Sci (Weinh). 2025 Apr 26. e2417715
      Skeletal muscle plays a crucial role in maintaining motor function and metabolic homeostasis, with its loss or atrophy leading to significant health consequences. Long non-coding RNAs (lncRNAs) have emerged as key regulators in muscle biology; however, their precise roles in muscle function and pathology remain to be fully elucidated. This study demonstrates that lncRNA maternally expressed gene 3 (MEG3) is preferentially expressed in slow-twitch muscle fibers and dynamically regulated during muscle development, aging, and in the context of Duchenne muscular dystrophy (DMD). Using both loss- and gain-of-function mice models, this study shows that lncRNA-MEG3 is critical for preserving muscle mass and function. Its depletion leads to muscle atrophy, mitochondrial dysfunction, and impaired regenerative capacity, while overexpression enhances muscle mass, increases oxidative muscle fiber content, and improves endurance. Notably, lncRNA-MEG3 overexpression in MDX mice significantly alleviates muscle wasting and adipose tissue infiltration. Mechanistically, this study uncovers a novel interaction between lncRNA-MEG3 and the polycomb repressive complex 2 (PRC2), where lncRNA-MEG3 binds to SUZ12 polycomb repressive complex 2 subunit (Suz12), stabilizes PRC2, facilitates SUZ12 liquid-liquid phase separation (LLPS), and regulates the epigenetic modulation of four and a half lim domains 3 (Fhl3) and ring finger protein 128 (Rnf128). These findings not only highlight the crucial role of lncRNA-MEG3 in muscle homeostasis but also provide new insights into lncRNA-based therapeutic strategies for muscle-related diseases.
    Keywords:  SUZ12 LLPS; fat infiltration; lncRNA‐MEG3; muscle atrophy; oxidative muscle fibers
    DOI:  https://doi.org/10.1002/advs.202417715
  16. J Biol Chem. 2025 Apr 23. pii: S0021-9258(25)00385-0. [Epub ahead of print] 108536
      CAPN3/calpain-3/p94, a muscle-specific Ca2+-dependent cysteine protease, is responsible for limb-girdle muscular dystrophy R1 (LGMDR1), an autosomal recessive muscular dystrophy. However, the activation mechanism and physiological function of CAPN3 in skeletal muscles remain unknown. Here, we capture the in situ activation of CAPN3 in cultured mouse skeletal myotubes. Using our newly developed antibody, which specifically recognizes CAPN3 autolytic processing, we succeeded in differentiating wild-type CAPN3 from a protease-inactive CAPN3 mutant by immunostaining. We further demonstrated that CAPN3 predominantly localized at the M-bands of cultured skeletal myotubes at rest and translocated to the cytoplasm after activation by stimulation with ouabain, a cardiotonic steroid. This event requires a small but long-lasting cytoplasmic increase in Ca2+ levels, which is sufficient for the activation of CAPN3 but not of calpain-1/CAPN1. Activated CAPN3 digests the cytoskeletal proteins spectrin and talin. Thus, we successfully visualized the intracellular dynamics of endogenous CAPN3 in cultured skeletal muscles after activation by ouabain and demonstrated the subsequent processing of endogenous substrates in living cells. Our study will help understand the physiological functions of CAPN3 in skeletal muscles and the pathophysiological mechanisms of LGMDR1.
    Keywords:  calcium; calpain; muscular dystrophy; protein translocation; skeletal muscle
    DOI:  https://doi.org/10.1016/j.jbc.2025.108536
  17. J Cachexia Sarcopenia Muscle. 2025 Jun;16(3): e13818
       BACKGROUND: Skeletal muscle is a major target for ethanol-induced perturbations, leading to sarcopenia in alcohol-related liver disease (ALD). The complex interactions and pathways involved in adaptive and maladaptive responses to ethanol in skeletal muscle are not well understood. Unlike hypothesis-driven experiments, an integrated multiomics-experimental validation approach provides a comprehensive view of these interactions.
    METHODS: We performed multiomics analyses with experimental validation to identify novel regulatory mechanisms of sarcopenia in ALD. Studies were done in a comprehensive array of models including ethanol-treated (ET) murine and human-induced pluripotent stem cell-derived myotubes (hiPSCm), skeletal muscle from a mouse model of ALD (mALD) and human patients with alcohol-related cirrhosis and controls. We generated 13 untargeted datasets, including chromatin accessibility (assay for transposase accessible chromatin), RNA sequencing, proteomics, phosphoproteomics, acetylomics and metabolomics, and conducted integrated multiomics analyses using UpSet plots and feature extraction. Key findings were validated using immunoblots, redox measurements (NAD+/NADH ratio), imaging and senescence-associated molecular phenotype (SAMP) assays. Mechanistic studies included mitochondrial-targeted Lactobacillus brevis NADH oxidase (MitoLbNOX) to increase redox ratio and MitoTempo as a mitochondrial free radical scavenger.
    RESULTS: Multiomics analyses revealed enrichment in mitochondrial oxidative function, protein synthesis and senescence pathways consistent with the known effects of hypoxia-inducible factor 1α (HIF1α) during normoxia. Across preclinical and clinical models, HIF1α targets (n = 32 genes) and signalling genes (n > 100 genes) (n = 3 ATACseq, n = 65 phosphoproteomics, n = 10 acetylomics, n = 6 C2C12 proteomics, n = 106 C2C12 RNAseq, n = 64 hiPSC RNAseq, n = 30 hiPSC proteomics, n = 3 mouse proteomics, n = 25 mouse RNAseq, n = 8 human RNAseq, n = 3 human proteomics) were increased. Stabilization of HIF1α (C2C12, 6hEtOH 0.24 ± 0.09; p = 0.043; mALD 0.32 ± 0.074; p = 0.005; data shown as mean difference ± standard error mean) was accompanied by enrichment in the early transient and late change clusters, -log(p-value) = 1.5-3.8, of the HIF1α signalling pathway. Redox ratio was reduced in ET myotubes (C2C12: 15512 ± 872.1, p < 0.001) and mALD muscle, with decreased expression of electron transport chain components (CI-V, p < 0.05) and Sirt3 (C2C12: 0.067 ± 0.023, p = 0.025; mALD: 0.41 ± 0.12, p = 0.013). Acetylation of mitochondrial proteins was increased in both models (C2C12: 107364 ± 4558, p = 0.03; mALD: 40036 ± 18 987, p = 0.049). Ethanol-induced SAMP was observed across models (P16: C2C12: 0.2845 ± 0.1145, p < 0.05; hiPSCm: 0.2591, p = 0.041). MitoLbNOX treatment reversed redox imbalance, HIF1α stabilization, global acetylation and myostatin expression (p < 0.05).
    CONCLUSIONS: An integrated multiomics approach, combined with experimental validation, identifies HIF1α stabilization and accelerated post-mitotic senescence as novel mechanisms of sarcopenia in ALD. These findings show the complex molecular interactions leading to mitochondrial dysfunction and progressive sarcopenia in ALD.
    Keywords:  alcohol‐related liver disease; hypoxia‐inducible factor‐1‐alpha; mitochondrial oxidative dysfunction; protein acetylation; redox ratio; sarcopenia; senescence; sirtuins
    DOI:  https://doi.org/10.1002/jcsm.13818
  18. Med Sci Sports Exerc. 2025 May 01.
       INTRODUCTION: Mitochondrial dynamics involve two distinct and opposing processes, fusion and fission. Traditionally we assess fusion and fission by snapshots of protein markers at distinct time points or in vitro models to infer outcomes in vivo. Recent technological advancements enable visualization of mitochondrial dynamics in vivo using fluorescent microscopy.
    METHODS: Our study modified this technique to evaluate mitochondrial dynamics in skeletal muscle, comparing young (6mo) and old (24mo) mice in vivo and contrasting this to ex vivo and in vitro models. We hypothesized that in vitro and ex vivo models would have higher rates of dynamics than in vivo models and that young animals would have higher rates than old animals. We electroporated mitochondrial matrix-targeted photo-activatable GFP into the tibialis anterior (TA) of young and old C57Bl6 mice and imaged using multiphoton microscopy. We also measured rates of mitochondrial dynamics using single fibers isolated from the TA of the electroporated mice, as well as C2C12 myotubes transfected with the same plasmids.
    RESULTS: We found that the rates of dynamic events in vivo are slower than previously indicated, with the C2C12 myoblasts having the fastest rates of dynamic events across all models. We also observed that dynamic rates are slower in old animals compared to young animals. Finally, we found that rates of dynamic events were higher in old animals after an acute bout of exercise.
    CONCLUSIONS: Our data demonstrate it is possible to directly measure rates of mitochondrial dynamics in vivo. This technique provides a powerful tool to answer experimental questions about mitochondrial dynamics of skeletal muscle.
    Keywords:  FISSION; FUSION; MITOCHONDRIAL DYNAMICS; SKELETAL MUSCLE
    DOI:  https://doi.org/10.1249/MSS.0000000000003748
  19. Mol Ther. 2025 Apr 29. pii: S1525-0016(25)00315-6. [Epub ahead of print]
      Centronuclear myopathies (CNM) are severe genetic disorders characterized by generalized muscle weakness associated with organelle mispositioning in myofibers. Most CNM cases are caused by mutations in proteins involved in membrane remodeling, including amphiphysin 2 (BIN1). There is no treatment and the pathological mechanisms are not understood. Here, we aimed to cure the Bin1-CNM mouse model (Bin1mck-/-) via an adeno-associated virus (AAV)-based gene replacement strategy. Early systemic exogenous BIN1 expression efficiently prevented disease progression. Moreover, BIN1 expression after disease onset reverted all disease signs four weeks after treatment, including motor defects, muscle weakness, muscle and myofibers hypotrophy, kyphosis, nuclei and mitochondria misposition, and altered T-tubules network. We then validated the most efficient construct combining a myotropic AAV serotype with the muscle BIN1 isoform. The rescue correlated with normalization of autophagy and excitation-contraction coupling markers. Cellular and in vivo investigations revealed that different BIN1 natural isoforms shared similar beneficial effects. Artificial constructs coding for separated protein domains rescued different CNM hallmarks. Only the muscle-specific BIN1 isoform combined the different cellular functions of BIN1 on membrane tubulation and dynamin (DNM2) regulation necessary for a full rescue. Overall, this study validates BIN1 gene replacement as a promising strategy to cure BIN1-related centronuclear myopathy.
    DOI:  https://doi.org/10.1016/j.ymthe.2025.04.036
  20. Bio Protoc. 2025 Apr 20. 15(8): e5281
      Skeletal muscle-specific stem cells are responsible for regenerating damaged muscle tissue following strenuous physical activity. These muscle stem cells, also known as satellite cells (SCs), can activate, proliferate, and differentiate to form new skeletal muscle cells. SCs can be identified and visualized utilizing optical and electron microscopy techniques. However, studies identifying SCs using fluorescent imaging techniques vary significantly within their methodology and lack fundamental aspects of the guidelines for rigor and reproducibility that must be included within immunohistochemical studies. Therefore, a standardized method for identifying human skeletal muscle stem cells is warranted, which will improve the reproducibility of future studies investigating satellite activity. Additionally, although it has been suggested that SC shape can change after exercise, there are currently no methods for examining SC morphology. Thus, we present an integrated workflow for three-dimensional visualization of satellite cell nuclei, validated by the spatial context of the fluorescent labeling and multichannel signal overlap. Our protocol includes, from start to finish, post-biopsy extraction and embedding, tissue sectioning, immunofluorescence, imaging steps and acquisition, and three-dimensional data post-processing. Because of the depth volume generated from the confocal microscope z-stacks, this will allow future studies to investigate the morphology of SC nuclei and their activity, instead of traditionally observing them in two-dimensional space (x, y). Key features • Detailed instructions on post-biopsy extraction and embedding, tissue sectioning, immunofluorescence, imaging steps and acquisition, and three-dimensional data post-processing of muscle stem cells. • Builds upon the validated method developed by Feng et al. [1], which was optimized for mouse tissue and fills critical gaps in existing literature. • Allows qualitative and quantitative morphological assessment of muscle stem cell nuclei in three-dimensional space. Graphical overview Graphical overview of integrated workflow for three-dimensional visualization of human skeletal muscle stem cells. After the percutaneous muscle biopsy, cut ~25-100 mg of the sample and arrange it according to the desired orientation → Mount sample for sectioning, embed in mounting medium, and freeze in liquid nitrogen-cooled isopentane → Using a cryostat, generate tissue cross-sections in an alternating collection method of 20 μm intervals and place on subbed glass slides → Fix and block sections before incubating in a cocktail of primary antibodies specific for satellite cell nuclei (anti-Pax7) and muscle membrane (anti-laminin) overnight. The following day, incubate sections in the appropriate secondary antibodies (Pax7: goat anti-mouse IgG1 biotin conjugated; laminin: goat anti-rabbit Alexa Fluor 488), apply signal amplification using streptavidin-horseradish peroxidase and tyramide 594 conjugate before counterstaining with DAPI, add mounting media, and coverslip → Using a confocal microscope, search for Pax7 signal, confirm overlap with DAPI adjacent to laminin labeling, apply appropriate laser channels, determine z-stack size, and acquire images in high-pixel-resolution format → For image post-processing, in the software's three-dimensional viewer, modify individual channel histograms to optimize image quality and save as a TIFF.
    Keywords:  Fluorescent microscopy; Immunohistochemistry; Muscle damage; Muscle regeneration; Myofiber cross-sectional area; Satellite cells
    DOI:  https://doi.org/10.21769/BioProtoc.5281
  21. Am J Physiol Endocrinol Metab. 2025 Apr 29.
      We investigated how short-term muscle disuse altered the skeletal muscle metabolome, lipidome and transcriptome in middle-aged adults. We report that the energy metabolism pathways: Nicotinate and nicotinamide metabolism, glycolysis and TCA cycle, were reduced after 7 days of muscle disuse. These changes in the metabolome were reflected by changes in the transcriptome where multiple genes involved in the glycolysis and TCA pathways were reduced after short term disuse. Phenylalanine, tyrosine and tryptophan metabolism pathways showed the same response and were reduced after short-term disuse. The skeletal muscle lipidome showed a decrease in phosphatidylinositols but an increase in phosphatidylglycerols and diacylglycerols after short term muscle disuse. We conclude that short-term muscle disuse in humans has profound and negative effects on the muscle metabolome and lipidome. These include significant downregulation of muscle glycolytic, amino acid, and TCA cycle intermediates. In contrast skeletal muscle lipids had a divergent response to disuse (e.g., increased phosphatidylglycerols and diacylglycerols, but reduced phosphatidylinositols).
    Keywords:  Skeletal muscle; atrophy; disuse; lipidomics; metabolomics; transcriptomics
    DOI:  https://doi.org/10.1152/ajpendo.00012.2025
  22. Brain. 2025 Apr 29. pii: awaf153. [Epub ahead of print]
      Idiopathic immune myopathies (IIM) represent a heterogeneous group of diseases, in which muscle lesions result from deregulated immune reactions. Typical histological features include myofibre necrosis, leukocyte infiltration, and aberrant myofibre Major Histocompatibility Complex (MHC) expression. To investigate the link between MHC expression, inflammation, and muscle lesions, muscle biopsies from IIM patients were analysed by transcriptomics. Both, anti-synthetase syndrome (ASS) and inclusion body myositis (IBM) displayed the upregulation of IFNγ and senescence signalling pathways. Notably, IFNγ expression significantly correlated with myofibre atrophy in ASS and IBM muscle biopsies. In addition to MHC-II expression at the myofibre sarcolemma in IBM, we observed a marked overexpression in the muscle stem cells (MuSC) population, suggesting that resident satellite cells respond to IFNγ in this condition. To examine the link between IFNγ and muscle atrophy via MuSCs, we implanted an osmotic pump chronically releasing recombinant mouse IFNγ in wild-type mice subjected to acute muscle injury. Under IFNγ exposure, post-injury muscle repair was associated with significantly reduced muscle weight and myofibre diameter, while promoting interstitial fibrosis and fat deposition. The mechanism of action of the IFNγ-induced myofibre atrophy was further investigated in vitro using cultured human MuSCs. IFNγ stimulation dramatically impaired MuSCs proliferation, fusion, and promoted cell senescence. Isolated myofibres from IFNγ-treated wild-type mice displayed a significant decrease of MyoD expression and cell cycling, suggesting that IFNγ also prevents MuSC activation. In vitro, ruxolitinib, a commercially available JAK1/2 antagonist, blocked IFNγ-induced expression of MHC-II, restored normal MuSC proliferation, and reduced β-Galactosidase activity, a marker of cell senescence. In vivo, oral delivery of ruxolitinib improved myofibre size and biomarkers of muscle atrophy. Our study provides multiple lines of evidence that IFNγ may mediate muscle atrophy in IBM patients. The identified mechanism of action involves JAK1/2 pathways, which impair MuSC function by preventing post-lesion myogenesis and promoting cell senescence. Our data suggest that repurposing JAK1/2 inhibitors may offer a new therapeutic option for treating IBM, a condition known for its resistance to classical immunosuppressant drugs, despite their effectiveness in other IIM.
    Keywords:  IFNγ; JAK-STAT; inclusion body myositis (IBM); inflammatory myopathies; myogenesis; satellite cells
    DOI:  https://doi.org/10.1093/brain/awaf153
  23. Neural Regen Res. 2025 Apr 29.
       ABSTRACT: Mitochondrial dysfunction and oxidative stress are widely regarded as primary drivers of aging and are associated with several neurodegenerative diseases. The degeneration of motor neurons during aging is a critical pathological factor contributing to the progression of sarcopenia. However, the morphological and functional changes in mitochondria and their interplay in the degeneration of the neuromuscular junction during aging remain poorly understood. A defined systematic search of the PubMed, Web of Science and Embase databases (last accessed on October 30, 2024) was conducted with search terms including 'mitochondria', 'aging' and 'NMJ'. Clinical and preclinical studies of mitochondrial dysfunction and neuromuscular junction degeneration during aging. Twentyseven studies were included in this systematic review. This systematic review provides a summary of morphological, functional and biological changes in neuromuscular junction, mitochondrial morphology, biosynthesis, respiratory chain function, and mitophagy during aging. We focus on the interactions and mechanisms underlying the relationship between mitochondria and neuromuscular junctions during aging. Aging is characterized by significant reductions in mitochondrial fusion/fission cycles, biosynthesis, and mitochondrial quality control, which may lead to neuromuscular junction dysfunction, denervation and poor physical performance. Motor nerve terminals that exhibit redox sensitivity are among the first to exhibit abnormalities, ultimately leading to an early decline in muscle strength through impaired neuromuscular junction transmission function. Parg coactivator 1 alpha is a crucial molecule that regulates mitochondrial biogenesis and modulates various pathways, including the mitochondrial respiratory chain, energy deficiency, oxidative stress, and inflammation. Mitochondrial dysfunction is correlated with neuromuscular junction denervation and acetylcholine receptor fragmentation, resulting in muscle atrophy and a decrease in strength during aging. Physical therapy, pharmacotherapy, and gene therapy can alleviate the structural degeneration and functional deterioration of neuromuscular junction by restoring mitochondrial function. Therefore, mitochondria are considered potential targets for preserving neuromuscular junction morphology and function during aging to treat sarcopenia.
    Keywords:  aging; mitochondrial dysfunction; neuromuscular junction; oxidative stress; sarcopenia; systematic review
    DOI:  https://doi.org/10.4103/NRR.NRR-D-24-01338
  24. Diabetologia. 2025 Apr 28.
       AIMS/HYPOTHESIS: Disrupted energy balance is critical for the onset and development of type 2 diabetes mellitus. Understanding of the exact underlying metabolic mechanisms remains incomplete, but skeletal muscle is thought to play an important pathogenic role. As the super-relaxed state of its most abundant protein, myosin, regulates cellular energetics, we aimed to investigate whether it is altered in individuals with type 2 diabetes.
    METHODS: We used vastus lateralis biopsy specimens (obtained from patients with type 2 diabetes and control participants with similar characteristics), and ran a combination of structural and functional assays consisting of loaded 2'- (or 3')-O-(N-methylanthraniloyl)-ATP (Mant-ATP) chase experiments, x-ray diffraction and LC-MS/MS proteomics in isolated muscle fibres.
    RESULTS: Our studies revealed a greater muscle myosin super-relaxation and decreased ATP demand in male participants with type 2 diabetes than in control participants. Subsequent proteomic analyses indicated that these (mal)adaptations probably originated from remodelled sarcomeric proteins and greater myosin glycation levels in patients than in control participants.
    CONCLUSIONS/INTERPRETATION: Overall, our findings indicate a complex molecular dysregulation of myosin super-relaxed state and energy consumption in male participants with type 2 diabetes. Ultimately, pharmacological targeting of myosin could benefit skeletal muscle and whole-body metabolic health through enhancement of ATP consumption.
    DATA AVAILABILITY: The raw MS data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD053022.
    Keywords:  Diabetes; Metabolism; Myosin; Skeletal muscle
    DOI:  https://doi.org/10.1007/s00125-025-06436-0
  25. Front Endocrinol (Lausanne). 2025 ;16 1560396
      Type 2 diabetes mellitus-related sarcopenia (T2DMRS) is a common complication in elderly and advanced diabetes patients that affects long-term prognosis and quality of life. Skeletal muscle is the main unit of glucose metabolism, and it is surrounded by extracellular matrix (ECM), which is a microenvironment that acts as an efficient highway system. The ECM is essential for cellular communication and nutrient transport and supports muscle cell growth and repair. When this "ECM highway" fails to function effectively because of damage or blockage, the development of T2DMRS can be triggered or exacerbated. In recent years, the ECM has been widely demonstrated to play a critical role in insulin resistance and skeletal muscle regeneration. However, how the remodeling of skeletal muscle ECM components specifically affects the T2DMRS mechanism of action has not been scientifically described in detail. In this review, we comprehensively summarize the T2DMRS-related mechanisms of ECM remodeling, suggesting that collagen and integrins may be potential therapeutic targets.
    Keywords:  collagen; extracellular matrix; integrins; sarcopenia; skeletal muscle regeneration; type 2 diabetes
    DOI:  https://doi.org/10.3389/fendo.2025.1560396
  26. Pharmaceuticals (Basel). 2025 Mar 21. pii: 445. [Epub ahead of print]18(4):
      Background/Objectives: Cancer cachexia (CC) is a prevalent and debilitating syndrome in cancer patients, characterized by severe muscle and weight loss, leading to increased mortality and reduced quality of life. Despite the significant impact, effective treatments are lacking due to an incomplete understanding of its underlying mechanisms. In this study, we aim to develop drugs that ameliorate the inhibition of muscle differentiation induced by CC. We established an advanced, high-content phenotypic screening system using the serum of cancer patients and identified potential compounds. Methods: We used cancer patients' sera as pathophysiological stimuli in our screening system to evaluate their effects on muscle atrophy and differentiation. Various histone deacetylase (HDAC) inhibitors were tested for their efficacy. The system's translational relevance was validated by comparing results with clinical data and in vivo cachexia models. Results: Using our screening system, we evaluated several cancer patients' sera and found that they reflect clinical features of cancer cachexia. In addition, HDAC inhibitors, particularly those with broad-spectrum inhibition, showed promise as agents to ameliorate the inhibition of muscle differentiation induced by CC sera. This system's findings were consistent with clinical and in vivo data, highlighting its potential for identifying new drugs. Conclusions: The high-content phenotypic screening system effectively mimics some key aspects of CC pathophysiology on skeletal muscle, providing a valuable tool for drug discovery and understanding CC mechanisms. The translational relevance of our system offers a promising avenue for therapeutic advancements in the management of cancer cachexia, with the potential to improve patient outcomes and quality of life.
    Keywords:  HDAC inhibitors; cancer cachexia; high-content phenotypic screening; muscle differentiation
    DOI:  https://doi.org/10.3390/ph18040445
  27. J Cachexia Sarcopenia Muscle. 2025 Jun;16(3): e13775
       BACKGROUND: We recently demonstrated that following a 10-day exposure to inactivity/simulated microgravity impairments of oxidative metabolism were located 'upstream' of mitochondrial function, as evaluated by maximal ADP-stimulated mitochondrial respiration (JO2max) determined ex vivo. The aim of this study was to evaluate mitochondrial sensitivity to submaximal [ADP] by an alternative approach aimed at identifying responses associated with fibre type composition.
    METHODS: Isolated permeabilized vastus lateralis fibres were analysed by high-resolution respirometry in 9 young males before and after a 10-day horizontal bed rest. Eleven submaximal titrations of ADP (from 12.5 to 10 000 μM) were utilized to assess complex I + II-linked ADP sensitivity. We applied to JO2 versus [ADP] data a traditional Michaelis-Menten kinetics equation, with the calculation of the apparent Km and maximal respiration (Vmax), and two 'sequential' hyperbolic equations, yielding two Km and Vmax values. The two-hyperbolic equations were solved and the [ADP] value corresponding to 50% of JO2max was calculated. Isoform expression of myosin heavy chains (MyHC) 1, 2A and 2X was also determined. Control experiments were also carried out on rat skeletal muscle samples with different percentages of MyHC isoforms.
    RESULTS: The two hyperbolic equations provided an alternative fitting of data and identified two distinct phases of the JO2 versus [ADP] response: a first phase characterized by low Vmax (Vmax1, 28 ± 10 pmol s-1 mg-1) and apparent Km (Km1, 62 ± 54 μM) and a second phase characterized by higher Vmax (Vmax2, 61 ± 16 pmol s-1 mg-1) and Km (Km2, 1784 ± 833 μM). Data were confirmed in control experiments carried out in rat muscle samples with different percentages of MyHC isoforms. Correlation and receiver operating characteristics analyses suggest that the two phases of the response were related to the % of MyHC isoforms.
    CONCLUSIONS: A novel mathematical approach (two sequential hyperbolic functions) for the fitting of JO2 versus [ADP] data obtained by high-resolution respirometry on permeabilized skeletal muscle fibres, obtained in humans and rats, provided an alternative fitting of the experimental data compared to the traditional Michaelis-Menten kinetics equation. This alternative model allowed the identification of two distinct phases in the responses, which were related to fibre type composition. A first phase, characterized by low apparent Km and Vmax values, was correlated with the percentage of less oxidative (Type 2A + 2X) MyHC isoforms. A second phase, characterized by high apparent Km and Vmax, was related to more oxidative (Type 1) MyHC isoforms.
    Keywords:  ADP; bed rest; mitochondrial sensitivity; myosin heavy chains; skeletal muscle mitochondria
    DOI:  https://doi.org/10.1002/jcsm.13775
  28. Geroscience. 2025 Apr 28.
      Aging is a universal biological process that impacts all tissues, leading to functional decline and increased susceptibility to age-related diseases, particularly cardiometabolic disorders. While aging is characterized by hallmarks such as mitochondrial dysfunction, chronic inflammation, and dysregulated metabolism, the molecular mechanisms driving these processes remain incompletely understood, particularly in a tissue-specific context. To address this gap, we conducted a comprehensive transcriptomic analysis across 40 human tissues using data from the Genotype-Tissue Expression (GTEx) project, comparing individuals younger than 40 years with those older than 65 years. We identified over 17,000 differentially expressed genes (DEGs) across tissues, with distinct patterns of up- and down-regulation. Enrichment analyses revealed that up-regulated DEGs were associated with inflammation, immune responses, and apoptosis, while down-regulated DEGs were linked to mitochondrial function, oxidative phosphorylation, and metabolic processes. Using gene co-expression network (GCN) analyses, we identified 1,099 genes as dysregulated nodes (DNs) shared across tissues, reflecting global aging-associated transcriptional shifts. Integrating machine learning approaches, we pinpointed key aging biomarkers, including GDF15 and EDA2R, which demonstrated strong predictive power for aging and were particularly relevant in cardiometabolic tissues such as the heart, liver, skeletal muscle, and adipose tissue. These genes were also validated in plasma proteomics studies and exhibited significant correlations with clinical cardiometabolic health indicators. This study provides a multi-tissue, integrative perspective on aging, uncovering both systemic and tissue-specific molecular signatures. Our findings advance understanding of the molecular underpinnings of aging and identify novel biomarkers that may serve as therapeutic targets for promoting healthy aging and mitigating age-related diseases.
    Keywords:  Aging biomarkers; Cardiometabolic health; Gene co-expression networks; Inflammation; Machine learning; Mitochondrial dysfunction; Transcriptomics
    DOI:  https://doi.org/10.1007/s11357-025-01672-z
  29. J Cachexia Sarcopenia Muscle. 2025 Jun;16(3): e13786
       BACKGROUND: To date, most research investigating the influence of circulating sex hormones on ageing female skeletal muscle has been cross-sectional and focused only on dichotomised young and old, or pre- versus post-menopausal groups. This excludes an important transitional period from high to low circulating oestrogen. Using secondary data from the Baltimore Longitudinal Study of Aging, this study aimed to investigate cross-sectional and longitudinal associations between circulating sex hormones and skeletal muscle mass and function across a continuum of ages.
    METHODS: Multiple and binomial linear regression was used to map cross-sectional (n = 319) and longitudinal (n = 83) associations between circulating sex hormones (oestradiol (E2), free oestradiol index (FEI), total (TT) and bioavailable (BioT), testosterone, testosterone/oestradiol ratio (TT/E2)) and skeletal muscle mass and function in healthy females. Cross-sectional models analysed females across an ageing continuum (24-89 years) and longitudinal associations were tested across 4-6 years of ageing in females over 50 years old. Models were adjusted for age, height, physical activity, comorbidities, ethnicity, and follow-up time.
    RESULTS: Cross-sectionally, serum E2 and FEI were positively associated with relative appendicular lean mass (ALM; β = 0.28 and 0.20, respectively, p < 0.05) and thigh muscle percentage (β = 0.19 and 0.15, respectively, p < 0.05). E2 and FEI were negatively associated with total body fat percentage (β = -0.30 and -0.21, respectively, p < 0.05). BioT was positively associated with absolute ALM (β = 0.13, p < 0.05) and total body fat percentage (β = 0.18, p < 0.05). TT was negatively associated with total body fat percentage (β = -0.14, p < 0.05). The TT/E2 ratio was negatively associated with thigh muscle CSA (β = -0.08, p < 0.05) and hamstring strength (β = -0.12, p < 0.05). Across 4-6 years, decreases in E2 and FEI were associated with a decrease in ALM (β = 0.27 and 0.41, respectively, p < 0.05), and a decrease in FEI was associated with a decrease in handgrip strength (β = 0.21, p < 0.05). Decreases in TT and BioT were associated with an increase in total body fat (β = -0.25 for both, p < 0.05) and a decrease in TT was associated with an increase in hamstring specific force (β = -0.11, p < 0.05).
    CONCLUSION: This study demonstrates novel associations between sex hormone levels and skeletal muscle in females across a wide continuum of ages. We also demonstrate that longitudinal fluctuations in circulating sex hormones must be considered to gain a comprehensive understanding of female muscle ageing.
    Keywords:  ageing; oestrogen; ovarian hormones; skeletal muscle
    DOI:  https://doi.org/10.1002/jcsm.13786
  30. FEBS Lett. 2025 Apr 28.
      The neuromuscular junction (NMJ) performs the crucial function of controlling skeletal muscle contraction. NMJ formation depends on the Agrin/Lrp4/MuSK/Dok-7 signaling pathway. However, signaling downstream of Dok-7 remains incompletely understood. Here we used the phosphorylated iTRAQ technique to identify downstream molecules of Dok-7 in muscle cells. We found 16 Agrin/Dok-7-mediated serine/threonine phosphorylated proteins, and we validated the role of one phosphorylated protein, JPH2, in regulating AChR clustering. Our phosphoproteomics analysis sheds light on the underappreciated signaling network downstream of Agrin/Dok-7, thus providing new clues for understanding pathogenesis and developing treatment methods for neuromuscular diseases.
    Keywords:  AChR clustering; Dok‐7; JPH2; neuromuscular junction; phosphorylation
    DOI:  https://doi.org/10.1002/1873-3468.70050
  31. Front Sports Act Living. 2025 ;7 1601326
      
    Keywords:  anabolic resistance; gender-specific barriers; gut-muscle axis; middle-aged adults; muscle protein synthesis; resistance training; sarcopenia; ultra-processed foods
    DOI:  https://doi.org/10.3389/fspor.2025.1601326
  32. Sci Rep. 2025 May 02. 15(1): 15319
      To investigate the role of gut microbiota and bile acids metabolism on skeletal muscle strength in low density lipoprotein receptor (LDLR) knockdown aging mice. Forty-eight male C57BL/6J mice were employed in the experiment, twelve adult mice and twelve old mice were separately knocked down skeletal muscle LDLR (ALKd group, OLKd group). Other adult mice and old mice were injected with empty vectors as control (Acon group, Ocon group). After eight weeks of injection, each mouse was tested for skeletal muscle strength. The serum glycolipid biomarkers, the gut microbiota composition, the ileum apical sodium-dependent bile acid transporter (ASBT), farnesoid X receptor (FXR), fibroblast growth factor 15 (FGF15), and gastrocnemius fibroblast growth factor receptor 4 (FGFR4) were detected. When compared to the Ocon group, increased grip strength, and the relative abundance of Akkermansia and Ileibacterium were found in the OLKd group. The FGF15 protein of the ileum and FGFR4 protein of the gastrocnemius were found to increase in the OLKd group than those of the Ocon group. The gut microbiota and bile acid metabolism both play an important role in the partially improved skeletal muscle strength of LDLR knockdown aging mice.
    Keywords:  Aging; FGF15; Gut microbiota; LDLR knockdown; Metabolism; Skeletal muscle strength
    DOI:  https://doi.org/10.1038/s41598-025-00059-6
  33. Sci Rep. 2025 Apr 29. 15(1): 14936
      Muscle ultrasound has high utility in clinical practice and research; however, the main challenges are the training and time required for manual analysis to achieve objective quantification of muscle size and quality. We aimed to develop and validate a software tool powered by artificial intelligence (AI) by measuring its consistency and comparability of expert manual analysis quantifying lower limb muscle ultrasound images. Quadriceps complex (QC) and tibialis anterior (TA) muscle images of healthy, intensive care unit, and/or lung cancer participants were captured with portable devices. Manual analyses of muscle size and quality were performed by experienced physiotherapists taking approximately 24 h to analyze all 180 images, while automated analyses were performed using a custom-built deep-learning model (MyoVision-US), taking 247 s (saving time = 99.8%). Consistency between the manual and automated analyses was good to excellent for all QC (ICC = 0.85-0.99) and TA (ICC = 0.93-0.99) measurements, even for critically ill (ICC = 0.91-0.98) and lung cancer (ICC = 0.85-0.99) images. The comparability of MyoVision-US was moderate to strong for QC (adj. R2 = 0.56-0.94) and TA parameters (adj. R2 = 0.81-0.97). The application of AI automating lower limb muscle ultrasound analyses showed excellent consistency and strong comparability compared with human analysis across healthy, acute, and chronic population.
    Keywords:  Artificial intelligence; Automation software; Medical image analysis; Skeletal muscle; Ultrasound
    DOI:  https://doi.org/10.1038/s41598-025-99522-7