Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
9.0
6.0
Journals
Cells
Special Issues
Mechanobiology Defects in Muscular Disorders
share announcement

Mechanobiology Defects in Muscular Disorders

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (31 October 2020) | Viewed by 11765

Special Issue Editor

Dr. Catherine Coirault

E-Mail Website
Guest Editor
Center of Research in Myology, Sorbonne University, INSERM 974, 75654 Paris, France
Interests: mechanobiology; mechanotransduction; nuclear envelope; muscular disorders
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Whereas the primary function of muscle is to produce force and movement, a vast body of research has accumulated to illustrate that mechanical forces in turn are critical to controlling muscle cell decisions and tissue homeostasis. It is becoming evident that mechanobiology defects are present in a wide range of muscular disorders, either inherited—such as muscular dystrophy—or acquired—such as age-related muscular diseases. The process of mechanobiology may be altered by changes in the extracellular matrix composition and stiffness, changes in muscle mechanics, or by the deregulation of the molecular mechanisms by which muscle cells and tissues sense and transduce mechanical force into biochemical signals. In a desire to develop new targets for therapeutic interventions, understanding the mechanical cues that regulate muscle development and homeostasis has become an active and fruitful area of research.

This Special Issue aims to provide comprehensible knowledge of mechanobiology defects in muscular disorders, including cell biology, molecular biology, and mechanobiology tools used in the muscle field. We invite the community to submit original articles or reviews in the above-mentioned field.

We look forward to your contributions

Dr. Catherine Coirault
Guest Editor

Manuscript Submission Information

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. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • mechanical stress
  • mechanotransduction
  • mechanosensation
  • mechanoresponse
  • striated muscle
  • muscle homeostasis
  • muscle growth
  • myopathy

Published Papers (3 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

9 pages, 988 KiB  
Article
Myofibre Hyper-Contractility in Horses Expressing the Myosin Heavy Chain Myopathy Mutation, MYH1E321G
by Julien Ochala, Carrie J. Finno and Stephanie J. Valberg
Cells 2021, 10(12), 3428; https://doi.org/10.3390/cells10123428 - 06 Dec 2021
Cited by 9 | Viewed by 3656
Abstract
Myosinopathies are defined as a group of muscle disorders characterized by mutations in genes encoding myosin heavy chains. Their exact molecular and cellular mechanisms remain unclear. In the present study, we have focused our attention on a MYH1-related E321G amino acid substitution [...] Read more.
Myosinopathies are defined as a group of muscle disorders characterized by mutations in genes encoding myosin heavy chains. Their exact molecular and cellular mechanisms remain unclear. In the present study, we have focused our attention on a MYH1-related E321G amino acid substitution within the head region of the type IIx skeletal myosin heavy chain, associated with clinical signs of atrophy, inflammation and/or profound rhabdomyolysis, known as equine myosin heavy chain myopathy. We performed Mant-ATP chase experiments together with force measurements on isolated IIx myofibres from control horses (MYH1E321G−/−) and Quarter Horses homozygous (MYH1E321G+/+) or heterozygous (MYH1E321G+/−) for the E321G mutation. The single residue replacement did not affect the relaxed conformations of myosin molecules. Nevertheless, it significantly increased its active behaviour as proven by the higher maximal force production and Ca2+ sensitivity for MYH1E321G+/+ in comparison with MYH1E321G+/− and MYH1E321G−/− horses. Altogether, these findings indicate that, in the presence of the E321G mutation, a molecular and cellular hyper-contractile phenotype occurs which could contribute to the development of the myosin heavy chain myopathy. Full article
(This article belongs to the Special Issue Mechanobiology Defects in Muscular Disorders)
►▼ Show Figures

Figure 1

16 pages, 2466 KiB  
Article
Perlecan Facilitates Neuronal Nitric Oxide Synthase Delocalization in Denervation-Induced Muscle Atrophy
by Satoshi Nakada, Yuri Yamashita, Shuichi Machida, Yuko Miyagoe-Suzuki and Eri Arikawa-Hirasawa
Cells 2020, 9(11), 2524; https://doi.org/10.3390/cells9112524 - 23 Nov 2020
Cited by 3 | Viewed by 2821
Abstract
Perlecan is an extracellular matrix molecule anchored to the sarcolemma by a dystrophin–glycoprotein complex. Perlecan-deficient mice are tolerant to muscle atrophy, suggesting that perlecan negatively regulates mechanical stress-dependent skeletal muscle mass. Delocalization of neuronal nitric oxide synthase (nNOS) from the sarcolemma to the [...] Read more.
Perlecan is an extracellular matrix molecule anchored to the sarcolemma by a dystrophin–glycoprotein complex. Perlecan-deficient mice are tolerant to muscle atrophy, suggesting that perlecan negatively regulates mechanical stress-dependent skeletal muscle mass. Delocalization of neuronal nitric oxide synthase (nNOS) from the sarcolemma to the cytosol triggers protein degradation, thereby initiating skeletal muscle atrophy. We hypothesized that perlecan regulates nNOS delocalization and activates protein degradation during this process. To determine the role of perlecan in nNOS-mediated mechanotransduction, we used sciatic nerve transection as a denervation model of gastrocnemius muscles. Gastrocnemius muscle atrophy was significantly lower in perinatal lethality-rescued perlecan-knockout (Hspg2−/−-Tg) mice than controls (WT-Tg) on days 4 and 14 following surgery. Immunofluorescence microscopy showed that cell membrane nNOS expression was reduced by denervation in WT-Tg mice, with marginal effects in Hspg2−/−-Tg mice. Moreover, levels of atrophy-related proteins—i.e., FoxO1a, FoxO3a, atrogin-1, and Lys48-polyubiquitinated proteins—increased in the denervated muscles of WT-Tg mice but not in Hspg2−/−-Tg mice. These findings suggest that during denervation, perlecan promotes nNOS delocalization from the membrane and stimulates protein degradation and muscle atrophy by activating FoxO signaling and the ubiquitin–proteasome system. Full article
(This article belongs to the Special Issue Mechanobiology Defects in Muscular Disorders)
►▼ Show Figures

Figure 1

Review

Jump to: Research

18 pages, 1789 KiB  
Review
Nuclear Mechanotransduction in Skeletal Muscle
by Saline Jabre, Walid Hleihel and Catherine Coirault
Cells 2021, 10(2), 318; https://doi.org/10.3390/cells10020318 - 04 Feb 2021
Cited by 13 | Viewed by 4574
Abstract
Skeletal muscle is composed of multinucleated, mature muscle cells (myofibers) responsible for contraction, and a resident pool of mononucleated muscle cell precursors (MCPs), that are maintained in a quiescent state in homeostatic conditions. Skeletal muscle is remarkable in its ability to adapt to [...] Read more.
Skeletal muscle is composed of multinucleated, mature muscle cells (myofibers) responsible for contraction, and a resident pool of mononucleated muscle cell precursors (MCPs), that are maintained in a quiescent state in homeostatic conditions. Skeletal muscle is remarkable in its ability to adapt to mechanical constraints, a property referred as muscle plasticity and mediated by both MCPs and myofibers. An emerging body of literature supports the notion that muscle plasticity is critically dependent upon nuclear mechanotransduction, which is transduction of exterior physical forces into the nucleus to generate a biological response. Mechanical loading induces nuclear deformation, changes in the nuclear lamina organization, chromatin condensation state, and cell signaling, which ultimately impacts myogenic cell fate decisions. This review summarizes contemporary insights into the mechanisms underlying nuclear force transmission in MCPs and myofibers. We discuss how the cytoskeleton and nuclear reorganizations during myogenic differentiation may affect force transmission and nuclear mechanotransduction. We also discuss how to apply these findings in the context of muscular disorders. Finally, we highlight current gaps in knowledge and opportunities for further research in the field. Full article
(This article belongs to the Special Issue Mechanobiology Defects in Muscular Disorders)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-3
Back to TopTop