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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 397

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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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Keywords

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

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Published Papers (1 paper)

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Research

17 pages, 10557 KiB  
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 142
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
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