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Cells
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Skeletal Muscle Extracellular Matrix: Composition, Structure and Function
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Skeletal Muscle Extracellular Matrix: Composition, Structure and Function

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Motility and Adhesion".

Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 15024

Special Issue Editors

Prof. Dr. Inho Choi

E-Mail Website
Guest Editor
Professor, Department of Medical Biotechnology Director, YU-Research Institute of Cell Culture (YU-RICC), Yeungnam University, Gyeongsan, Republic of Korea
Interests: skeletal muscle; cell culture technology; extracellular matrix biology; in silico drug design and screening
Special Issues, Collections and Topics in MDPI journals
Dr. Khurshid Ahmad

E-Mail Website
Guest Editor
Department of Medical Biotechnology, Yeungnam University, Gyeongsan 38541, Republic of Korea
Interests: bioinformatics; extracellular matrix biology; muscle biology; drug designing; virtual screening
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Skeletal muscle is the largest component in humans, accounting for over almost 40% of body mass, and it is predominantly composed of myofiber, providing mobility, protecting and supporting the skeleton, and controlling body temperature and glucose homeostasis. Since the skeletal muscle regulates the whole body’s homeostasis, disturbances of its function result in multiple diseases, including metabolic disorders, cachexia, and sarcopenia, as well as cardiac and renal failures. Muscle fibers reside in a three-dimensional and highly organized scaffolding known as the extracellular matrix (ECM). ECM provides structural support for surrounding cells and serves mechano-biochemical roles in cells. It consists of a range of structural molecules, including many fibrillar and non-fibrillar molecules. In addition to being essential structural elements, ECM molecules have important functional roles in the regulation of key cellular events viz. proliferation, adhesion, migration, differentiation, and survival. Any type of disruption (structural or metabolic) in the ECM or dysfunction of the ECM components may result in several pathological conditions, including metabolic disorders and cancers. Several drugs have been documented to modulate ECM assemblies, including physiological changes, beyond their key targets and ECM metabolism.

This Special Issue will highlight new research on ECM skeletal muscle, its modes of action, and its function in various diseases using state-of-the-art research techniques. Novel therapeutic approaches including in silico, in vitro, and in vivo experiments to target potential ECM components, are also encouraged. Original research papers, review articles, communications, perspectives, and commentaries are welcome.

We look forward to your contributions to this Special Issue.

Prof. Inho Choi
Dr. Khurshid Ahmad
Guest Editors

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

  • Skeletal muscle
  • Extracellular matrix
  • Collagen
  • Metabolic disorders
  • Sarcopenia
  • Cachexia
  • Drug design

Published Papers (4 papers)

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Research

18 pages, 3225 KiB  
Article
IgLON4 Regulates Myogenesis via Promoting Cell Adhesion and Maintaining Myotube Orientation
by Jeong Ho Lim, Khurshid Ahmad, Hee Jin Chun, Ye Chan Hwang, Afsha Fatima Qadri, Shahid Ali, Syed Sayeed Ahmad, Sibhghatulla Shaikh, Jungseok Choi, Jihoe Kim, Jun-O Jin, Myunghee Kim, Sung Soo Han, Inho Choi and Eun Ju Lee
Cells 2022, 11(20), 3265; https://doi.org/10.3390/cells11203265 - 17 Oct 2022
Cited by 5 | Viewed by 1959
Abstract
Immunoglobulin-like cell adhesion molecule (IgLON4) is a glycosylphosphatidylinositol-anchored membrane protein that has been associated with neuronal growth and connectivity, and its deficiency has been linked to increased fat mass and low muscle mass. Adequate information on IgLON4 is lacking, especially in the context [...] Read more.
Immunoglobulin-like cell adhesion molecule (IgLON4) is a glycosylphosphatidylinositol-anchored membrane protein that has been associated with neuronal growth and connectivity, and its deficiency has been linked to increased fat mass and low muscle mass. Adequate information on IgLON4 is lacking, especially in the context of skeletal muscle. In this study, we report that IgLON4 is profusely expressed in mouse muscles and is intensely localized on the cell membrane. IgLON4 expression was elevated in CTX-injected mouse muscles, which confirmed its role during muscle regeneration, and was abundantly expressed at high concentrations at cell-to-cell adhesion and interaction sites during muscle differentiation. IgLON4 inhibition profoundly affected myotube alignment, and directional analysis confirmed this effect. Additionally, results demonstrating a link between IgLON4 and lipid rafts during myogenic differentiation suggest that IgLON4 promotes differentiation by increasing lipid raft accumulation. These findings support the notion that a well-aligned environment promotes myoblast differentiation. Collectively, IgLON4 plays a novel role in myogenesis and regeneration, facilitates myotube orientation, and is involved in lipid raft accumulation. Full article
(This article belongs to the Special Issue Skeletal Muscle Extracellular Matrix: Composition, Structure and Function)
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18 pages, 3074 KiB  
Article
Exploring the Binding Pattern of Geraniol with Acetylcholinesterase through In Silico Docking, Molecular Dynamics Simulation, and In Vitro Enzyme Inhibition Kinetics Studies
by Danish Iqbal, M. Salman Khan, Mohd Waiz, Md Tabish Rehman, Mohammed Alaidarous, Azfar Jamal, Abdulaziz S. Alothaim, Mohamed F AlAjmi, Bader Mohammed Alshehri, Saeed Banawas, Mohammed Alsaweed, Yahya Madkhali, Abdulrahman Algarni, Suliman A. Alsagaby and Wael Alturaiki
Cells 2021, 10(12), 3533; https://doi.org/10.3390/cells10123533 - 14 Dec 2021
Cited by 15 | Viewed by 3544
Abstract
Acetylcholinesterase (AChE) inhibition is a key element in enhancing cholinergic transmission and subsequently relieving major symptoms of several neurological and neuromuscular disorders. Here, the inhibitory potential of geraniol and its mechanism of inhibition against AChE were elucidated in vitro and validated via an [...] Read more.
Acetylcholinesterase (AChE) inhibition is a key element in enhancing cholinergic transmission and subsequently relieving major symptoms of several neurological and neuromuscular disorders. Here, the inhibitory potential of geraniol and its mechanism of inhibition against AChE were elucidated in vitro and validated via an in silico study. Our in vitro enzyme inhibition kinetics results show that at increasing concentrations of geraniol and substrate, Vmax did not change significantly, but Km increased, which indicates that geraniol is a competitive inhibitor against AChE with an IC50 value 98.06 ± 3.92 µM. All the parameters of the ADME study revealed that geraniol is an acceptable drug candidate. A docking study showed that the binding energy of geraniol (−5.6 kcal mol−1) was lower than that of acetylcholine (−4.1 kcal mol−1) with AChE, which exhibited around a 12.58-fold higher binding affinity of geraniol. Furthermore, molecular dynamics simulation revealed that the RMSD of AChE alone or in complex with geraniol fluctuated within acceptable limits throughout the simulation. The mean RMSF value of the complex ensures that the overall conformation of the protein remains conserved. The average values of Rg, MolSA, SASA, and PSA of the complex were 3.16 Å, 204.78, 9.13, and 51.58 Å2, respectively. We found that the total SSE of AChE in the complex was 38.84% (α-helix: 26.57% and β-sheets: 12.27%) and remained consistent throughout the simulation. These findings suggest that geraniol remained inside the binding cavity of AChE in a stable conformation. Further in vivo investigation is required to fully characterize the pharmacokinetic properties, optimization of dose administration, and efficacy of this plant-based natural compound. Full article
(This article belongs to the Special Issue Skeletal Muscle Extracellular Matrix: Composition, Structure and Function)
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17 pages, 48488 KiB  
Article
Interaction of Fibromodulin and Myostatin to Regulate Skeletal Muscle Aging: An Opposite Regulation in Muscle Aging, Diabetes, and Intracellular Lipid Accumulation
by Eun Ju Lee, Syed Sayeed Ahmad, Jeong Ho Lim, Khurshid Ahmad, Sibhghatulla Shaikh, Yun-Sil Lee, Sang Joon Park, Jun O. Jin, Yong-Ho Lee and Inho Choi
Cells 2021, 10(8), 2083; https://doi.org/10.3390/cells10082083 - 13 Aug 2021
Cited by 18 | Viewed by 3901
Abstract
The objective of this study was to investigate fibromodulin (FMOD) and myostatin (MSTN) gene expressions during skeletal muscle aging and to understand their involvements in this process. The expressions of genes related to muscle aging (Atrogin 1 and Glb1), diabetes (RAGE and CD163), [...] Read more.
The objective of this study was to investigate fibromodulin (FMOD) and myostatin (MSTN) gene expressions during skeletal muscle aging and to understand their involvements in this process. The expressions of genes related to muscle aging (Atrogin 1 and Glb1), diabetes (RAGE and CD163), and lipid accumulation (CD36 and PPARγ) and those of FMOD and MSTN were examined in CTX-injected, aged, MSTN−/−, and high-fat diet (HFD) mice and in C2C12 myoblasts treated with ceramide or grown under adipogenic conditions. Results from CTX-injected mice and gene knockdown experiments in C2C12 cells suggested the involvement of FMOD during muscle regeneration and myoblast proliferation and differentiation. Downregulation of the FMOD gene in MSTN−/− mice, and MSTN upregulation and FMOD downregulation in FMOD and MSTN knockdown C2C12 cells, respectively, during their differentiation, suggested FMOD negatively regulates MSTN gene expression, and MSTN positively regulates FMOD gene expression. The results of our in vivo and in vitro experiments indicate FMOD inhibits muscle aging by negatively regulating MSTN gene expression or by suppressing the action of MSTN protein, and that MSTN promotes muscle aging by positively regulating the expressions of Atrogin1, CD36, and PPARγ genes in muscle. Full article
(This article belongs to the Special Issue Skeletal Muscle Extracellular Matrix: Composition, Structure and Function)
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15 pages, 4071 KiB  
Article
IgLON5 Regulates the Adhesion and Differentiation of Myoblasts
by Jeong Ho Lim, Mirza Masroor Ali Beg, Khurshid Ahmad, Sibhghatulla Shaikh, Syed Sayeed Ahmad, Hee Jin Chun, Dukhwan Choi, Woo-Jong Lee, Jun-O Jin, Jihoe Kim, Arif Tasleem Jan, Eun Ju Lee and Inho Choi
Cells 2021, 10(2), 417; https://doi.org/10.3390/cells10020417 - 17 Feb 2021
Cited by 11 | Viewed by 3293
Abstract
IgLON5 is a cell adhesion protein belonging to the immunoglobulin superfamily and has important cellular functions. The objective of this study was to determine the role played by IgLON5 during myogenesis. We found IgLON5 expression progressively increased in C2C12 myoblasts during transition from [...] Read more.
IgLON5 is a cell adhesion protein belonging to the immunoglobulin superfamily and has important cellular functions. The objective of this study was to determine the role played by IgLON5 during myogenesis. We found IgLON5 expression progressively increased in C2C12 myoblasts during transition from the adhesion to differentiation stage. IgLON5 knockdown (IgLON5kd) cells exhibited reduced cell adhesion, myotube formation, and maturation and reduced expressions of different types of genes, including those coding for extracellular matrix (ECM) components (COL1a1, FMOD, DPT, THBS1), cell membrane proteins (ITM2a, CDH15), and cytoskeletal protein (WASP). Furthermore, decreased IgLON5 expression in FMODkd, DPTkd, COL1a1kd, and ITM2akd cells suggested that IgLON5 and these genes mutually control gene expression during myogenesis. IgLON5 immunoneutralization resulted in significant reduction in the protein level of myogenic markers (MYOD, MYOG, MYL2). IgLON5 expression was higher in the CTX-treated gastrocnemius mice muscles (day 7), which confirmed increase expression of IgLON5 during muscle. Collectively, these results suggest IgLON5 plays an important role in myogenesis, muscle regeneration, and that proteins in ECM and myoblast membranes form an interactive network that establishes an essential microenvironment that ensures muscle stem cell survival. Full article
(This article belongs to the Special Issue Skeletal Muscle Extracellular Matrix: Composition, Structure and Function)
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