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Molecular and Neuromuscular Mechanisms in Skeletal Muscle Aging, 2nd Edition
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Molecular and Neuromuscular Mechanisms in Skeletal Muscle Aging, 2nd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 February 2026 | Viewed by 1011

Special Issue Editor

Dr. Rosa Mancinelli

E-Mail Website
Guest Editor
Department of Neuroscience, Imaging and Clinical Sciences, University ”G. d’Annunzio” Chieti-Pescara, 66100 Chieti, Italy
Interests: muscle; skeletal; myochines; neuromuscular junction; aging; human muscle senescence
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

It is known that in humans, skeletal muscles account for about 40% of the body weight and are essential for overall health. With increasing age, muscle function declines, causing reduced mobility, thus leading to reduced independence and an increase in morbidity and mortality in the elderly. This age-related decline in muscle function is known as sarcopenia. Sarcopenia is a multifactorial disease that is defined as a progressive loss of muscle mass, strength, and function. It has attracted great research efforts to clarify its underlying mechanisms and potential treatments.

When aiming to discover hallmarks of aging, looking at shared age- and disease-related changes in cellular and muscular pathways such as apoptosis, cell cycle regulation, calcium handling, myokines, and catabolism can be helpful.

The aim of this Special Issue is essentially to present new discoveries and study approaches to aging processes, mainly at the molecular and neuromuscular levels. For this Special Issue, we invite researchers to provide original research articles and review articles regarding results in the field of the new frontiers that can contribute to the understanding of the aging muscle process.

Dr. Rosa Mancinelli
Guest Editor

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Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

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Keywords

  • aging
  • sarcopenia
  • neuromuscular junction
  • molecular muscle modifications
  • myokines

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Published Papers (3 papers)

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Research

15 pages, 2872 KB  
Article
Biglycan Alleviates Age-Related Muscle Atrophy and Hepatocellular Senescence
by Da Som Lee, Joo Hyun Lim and Yoo Jeong Lee
Int. J. Mol. Sci. 2025, 26(17), 8286; https://doi.org/10.3390/ijms26178286 - 26 Aug 2025
Abstract
Myokines are secreted by muscle and play crucial roles in muscle repair and regeneration and also impact diverse physiological effects through crosstalk with other metabolic organs. However, aging is associated with a progressive decline in muscle mass, which in turn leads to reduced [...] Read more.
Myokines are secreted by muscle and play crucial roles in muscle repair and regeneration and also impact diverse physiological effects through crosstalk with other metabolic organs. However, aging is associated with a progressive decline in muscle mass, which in turn leads to reduced myokine secretion. This decline may contribute to the development of sarcopenia, leading to an increased risk of metabolic disorders such as type 2 diabetes. Accordingly, interest in identifying novel myokines and elucidating their biological functions is increasing. In this study, we explored the function of biglycan (BGN), a novel myokine, in aging-related metabolic tissues. BGN levels decreased in the muscle tissue and plasma of older adults and aged mice, whereas exercise intervention restored BGN expression in aged mice. BGN counteracted the expression of atrophy-related genes involved in muscle degradation and mitigated muscle mass loss by regulating AKT/mTOR signaling pathway. Notably, BGN decreased the expression of the senescence marker p21 and senescence-associated secretory phenotype (SASP)-related genes in hepatocytes. Additionally, BGN attenuated senescence-induced lipid accumulation and ROS generation. Our results suggest that BGN has beneficial effects against muscle atrophy and hepatocellular senescence, indicating its potential as a protective factor for age-related diseases. Full article
(This article belongs to the Special Issue Molecular and Neuromuscular Mechanisms in Skeletal Muscle Aging, 2nd Edition)
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20 pages, 4912 KB  
Article
Klotho Deficiency Promotes Skeletal Muscle Weakness and Is Associated with Impaired Motor Unit Connectivity
by Linda A. Bean, Connor Thomas, Juan F. Villa, Alexander J. Fitt, Areli Jannes S. Javier, Akanksha Agrawal, Hanna Whitney, Guilherme Nascimento Dos Santos, Kenneth E. White, Joshua R. Huot and Steven S. Welc
Int. J. Mol. Sci. 2025, 26(16), 7986; https://doi.org/10.3390/ijms26167986 - 19 Aug 2025
Viewed by 197
Abstract
Muscle wasting and weakness are critical clinical problems that limit mobility and independence, reduce health span, and increase the risk of physical disability. The molecular basis for this has not been fully determined. Klotho expression is downregulated in conditions associated with muscle wasting, [...] Read more.
Muscle wasting and weakness are critical clinical problems that limit mobility and independence, reduce health span, and increase the risk of physical disability. The molecular basis for this has not been fully determined. Klotho expression is downregulated in conditions associated with muscle wasting, including aging, chronic kidney disease, and myopathy. The objective of this study was to investigate a mechanistic role for Klotho in regulating muscle wasting and weakness. Body weight, lean mass, muscle mass, and myofiber caliber were reduced in Klotho-deficient mice. In the tibialis anterior muscle of Klotho-null mice, type IIa myofibers were resistant to changes in size, and muscle composition differed with a higher concentration of type IIb fibers to the detriment of type IIx fibers. Glycolytic GPDH enzymatic activity also increased. Klotho-deficient mice showed impaired muscle contractility, with reduced twitch force, torque, and contraction–relaxation rates. RNA sequencing revealed upregulation of synaptic and fetal sarcomeric genes, prompting us to examine muscle innervation. Klotho deficiency led to neuromuscular junction remodeling, myofiber denervation, and functional motor unit loss. Loss of motor units correlated with absolute torque. Collectively, these findings reveal a novel mechanism through which systemic Klotho deficiency disrupts muscle synapses and motor unit connectivity, potentially contributing to muscle wasting and weakness. Full article
(This article belongs to the Special Issue Molecular and Neuromuscular Mechanisms in Skeletal Muscle Aging, 2nd Edition)
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17 pages, 10557 KB  
Article
Formation of an Amyloid-like Structure During In Vitro Interaction of Titin and Myosin-Binding Protein C
by Tatiana A. Uryupina, Liya G. Bobyleva, Nikita V. Penkov, Maria A. Timchenko, Azat G. Gabdulkhakov, Anna V. Glyakina, Vadim V. Rogachevsky, Alexey K. Surin, Oxana V. Galzitskaya, Ivan M. Vikhlyantsev and Alexander G. Bobylev
Int. J. Mol. Sci. 2025, 26(14), 6910; https://doi.org/10.3390/ijms26146910 - 18 Jul 2025
Viewed by 350
Abstract
Protein association and aggregation are fundamental processes that play critical roles in a variety of biological phenomena from cell signaling to the development of incurable diseases, including amyloidoses. Understanding the basic biophysical principles governing protein aggregation processes is of crucial importance for developing [...] Read more.
Protein association and aggregation are fundamental processes that play critical roles in a variety of biological phenomena from cell signaling to the development of incurable diseases, including amyloidoses. Understanding the basic biophysical principles governing protein aggregation processes is of crucial importance for developing treatment strategies for diseases associated with protein aggregation, including sarcopenia, as well as for the treatment of pathological processes associated with the disruption of functional protein complexes. This work, using a set of methods such as atomic force microscopy (AFM), transmission electron microscopy (TEM), Fourier transform infrared spectroscopy (FTIR), and X-ray diffraction, as well as bioinformatics analysis, investigated the structures of complexes formed by titin and myosin-binding protein C (MyBP-C). TEM revealed the formation of morphologically ordered aggregates in the form of beads during co-incubation of titin and MyBP-C under close-to-physiological conditions (175 mM KCl, pH 7.0). AFM showed the formation of a relatively homogeneous film with local areas of relief change. Fluorimetry with thioflavin T, as well as FTIR spectroscopy, revealed signs of an amyloid-like structure, including a signal in the cross-β region. X-ray diffraction showed the presence of a cross-β structure characteristic of amyloid aggregates. Such structural features were not observed in the control samples of the investigated proteins separately. In sarcomeres, these proteins are associated with each other, and this interaction plays a partial role in the formation of a strong sarcomeric cytoskeleton. We found that under physiological ionic-strength conditions titin and MyBP-C form complexes in which an amyloid-like structure is present. The possible functional significance of amyloid-like aggregation of these proteins in muscle cells in vivo is discussed. Full article
(This article belongs to the Special Issue Molecular and Neuromuscular Mechanisms in Skeletal Muscle Aging, 2nd Edition)
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