[go: up one dir, main page]
More Web Proxy on the site http://driver.im/
You seem to have javascript disabled. Please note that many of the page functionalities won't work as expected without javascript enabled.
 
 
Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
5.7
3.6
Journals
Biology
Special Issues
Repair and Regeneration of Skeletal Muscle
share announcement

Repair and Regeneration of Skeletal Muscle

A special issue of Biology (ISSN 2079-7737). This special issue belongs to the section "Developmental and Reproductive Biology".

Deadline for manuscript submissions: 31 May 2025 | Viewed by 5367

Special Issue Editor

Prof. Dr. Huili Tong

E-Mail Website
Guest Editor
1. Key Laboratory of Animal Cellular and Genetics Engineering of Heilongjiang Province, Northeast Agricultural University, Harbin 150030, China
2. Laboratory of Cell and Developmental Biology, Northeast Agricultural University, Harbin 150030, China
Interests: muscle post-injury regeneration and repair; muscle nutrition and disease

Special Issue Information

Dear Colleagues,

Skeletal muscle, as one of the most important organs in the human body, plays a variety of important physiological functions in human beings, such as movement and metabolism. Aging, chronic diseases, drug stimulation, physical trauma, and other factors usually cause skeletal muscle sarcopenia, atrophy, or injury. Severe skeletal muscle damage often impairs the function of skeletal-muscle-specific stem cells, muscle satellite cells (MuSCs), making it difficult to repair skeletal muscle injury and seriously affecting normal physiological activities and quality of life. This has always been a hot topic in the fields of life science and regenerative medicine. Therefore, this Special Issue welcomes submissions of research conducted from a wide range of angles, from studies elucidating the roles and developmental mechanisms of MuSCs to those exploring novel methods and strategies such as drug intervention, stem cell therapy, tissue engineering technology, and so on, for effectively promoting skeletal muscle regeneration and repair. We hope that our research will help to promote the regeneration and repair of skeletal muscle injury, maintain the homeostasis of skeletal muscle tissue, and restore the health of skeletal muscle.

Prof. Dr. Huili Tong
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. Biology is an international peer-reviewed open access monthly 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
  • sarcopenia
  • atrophy
  • muscle satellite cells
  • regeneration and repair

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue policies can be found here.

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

14 pages, 15764 KiB  
Article
Puerarin Promotes the Migration and Differentiation of Myoblasts by Activating the FAK and PI3K/AKT Signaling Pathways
by Xiaofeng Fang, Hangjia Xu, Zhaoxin Fan, Hongge Yang, Yan Huang, Lin Xu, Yiwei Rong, Wei Ma, Liubao Pei and Hongsheng Liang
Biology 2025, 14(1), 102; https://doi.org/10.3390/biology14010102 - 20 Jan 2025
Viewed by 827
Abstract
Puerarin, a flavonoid compound present in the roots of radix puerariae, contributes to the development of tissues such as bone and nerve, but its role in skeletal muscle regeneration remains unclear. In this study, we employed C2C12 myoblasts and barium chloride (BaCl [...] Read more.
Puerarin, a flavonoid compound present in the roots of radix puerariae, contributes to the development of tissues such as bone and nerve, but its role in skeletal muscle regeneration remains unclear. In this study, we employed C2C12 myoblasts and barium chloride (BaCl2)-based muscle injury models to investigate the effects of puerarin on myogenesis. Our study showed that puerarin stimulated the migration and differentiation of myoblasts in vitro. For the mechanism study, we found that puerarin’s influence on cell migration was associated with the activation of FAK signaling; additionally, puerarin induced myoblast differentiation by upregulating the PI3K/AKT pathway. We also found that puerarin treatment could improve muscle regeneration following muscle injury. Taken together, our data indicate that puerarin facilitated myogenesis by promoting migration and differentiation, which suggests puerarin as a new candidate drug for the treatment of muscle loss diseases. Full article
(This article belongs to the Special Issue Repair and Regeneration of Skeletal Muscle)
►▼ Show Figures

Figure 1

Figure 1
<p>The proliferative effect of puerarin on C2C12 myoblasts. C2C12 cells were cultured in proliferation medium supplemented with puerarin (0, 5, 10, 20, 40, and 100 µM) for 24 h. (<b>A</b>) The EDU incorporation assay was employed to evaluate the cell proliferation ability. Scale bar = 100 µm. (<b>B</b>) Percentage of EDU-positive cells in panel (<b>A</b>). Data are displayed as the means ± SDs of three independent experiments. (<b>C</b>) Cell viability tested by the CCK8 assay. * <span class="html-italic">p</span> &lt; 0.05 compared with the control group.</p> Full article ">Figure 2
<p>Puerarin promoted the migration of C2C12 myoblasts. C2C12 cells were incubated with DMEM for 24 h with varying concentrations of puerarin (0, 5, 10, 20, and 40 µM). (<b>A</b>) The wound healing assay was conducted to assess cell migration by introducing a scratch in a confluent monolayer and monitoring it for 24 h. Scale bar = 100 µm. (<b>B</b>) The data of cell migration ratio based on (<b>A</b>). (<b>C</b>) The transwell assay was conducted to measure the C2C12 cell movement capacity. Scale bar = 100 µm. (<b>D</b>) Quantitative analysis of crystal violet’s optical density at 570 nm in panel C. Data are displayed as the means ± SDs of three independent experiments. * <span class="html-italic">p</span> &lt; 0.05 and ** <span class="html-italic">p</span> &lt; 0.01 compared with the control group.</p> Full article ">Figure 3
<p>Puerarin-induced myoblast migration through FAK signaling. C2C12 myoblasts were treated with puerarin (20 µM), PF-573228 (10 µM), or both in DMEM for 24 h. (<b>A</b>,<b>C</b>) The protein expression of p-FAK (Tyr397) was analyzed by Western blot. β-Tubulin was employed as the loading control. (<b>B</b>,<b>D</b>) Quantitative analysis of protein expression of p-FAK (Tyr397). (<b>E</b>) The wound healing assay was performed to evaluate cell migration by making a scratch in a confluent monolayer and monitoring it for 24 h. Scale bar = 100 µm. (<b>F</b>) The migration ratio based on the scratch wound assay. (<b>G</b>) The transwell assay was performed to assess the migration ability of C2C12 cells. Scale bar = 100 µm. (<b>H</b>) Quantitative analysis of crystal violet’s optical density at 570 nm in panel (<b>G</b>). Data are displayed as the means ± SDs of three independent experiments. * <span class="html-italic">p</span> &lt; 0.05 and ** <span class="html-italic">p</span> &lt; 0.01 compared with the control group.</p> Full article ">Figure 4
<p>Puerarin stimulated the differentiation of C2C12 myoblasts. C2C12 cells were cultured in differentiation medium for 4 days with varying concentrations of puerarin (0, 5, 10, 20, and 40 µM). (<b>A</b>) Representative optical images showing myotubes after 4 days of differentiation. Scale bar = 50 µm. (<b>B</b>) Immunofluorescence staining of MyHC (green) and DAPI (blue) in myotubes. Scale bar = 100 µm. (<b>C</b>) Fusion index (the proportion of nuclei in cells expressing MHC) in figure (<b>B</b>). (<b>D</b>) The protein expression levels of MyHC, MyoD, and MyoG were analyzed by Western blot. β-Tubulin or GAPDH was used as the loading control. (<b>E</b>) Quantitative analysis of protein expression of MyHC, MyoD, and MyoG. Data are displayed as the means ± SDs of three independent experiments. * <span class="html-italic">p</span> &lt; 0.05 and ** <span class="html-italic">p</span> &lt; 0.01 compared with the control group.</p> Full article ">Figure 5
<p>Puerarin-induced myoblast differentiation through the PI3K/AKT pathway. C2C12 myoblasts were treated with puerarin (20 µM), LY294002 (10 µM), or both in differentiation medium for 4 days. (<b>A</b>,<b>C</b>) The protein expression levels of p-PI3K (Tyr317) and p-AKT (T308) were analyzed by Western blot. GAPDH was employed as the loading control. (<b>B</b>,<b>D</b>) Quantitative analysis of protein expression of p-PI3K (Tyr317) and p-AKT (T308). (<b>E</b>) Representative optical images of myotubes following 4 days of differentiation. Scale bar = 50 µm. (<b>F</b>) Myotubes were stained for MHC (green) and DAPI (blue). Scale bar = 100 µm. (<b>G</b>) Fusion index (the proportion of nuclei in cells expressing MHC) in figure (<b>F</b>). (<b>H</b>) The protein levels of MyHC, MyoD, and MyoG were tested by Western blot. β-Tubulin or GAPDH was used as the loading control. (<b>I</b>) Quantitative analysis of protein levels of MyHC, MyoD, and MyoG. Data are displayed as the means ± SDs of three independent experiments. * <span class="html-italic">p</span> &lt; 0.05 and ** <span class="html-italic">p</span> &lt; 0.01 compared with the control group.</p> Full article ">Figure 6
<p>Puerarin promotes muscle regeneration after muscle damage. After injecting 1.2% BaCl<sub>2</sub> in the middle of the TA muscle, the muscle was collected following continuous oral administration of puerarin (100 mg/kg/day) for 5 days. (<b>A</b>) H&amp;E staining of the TA muscle 5 days post-injury. Scale bar = 50 µm. (<b>B</b>) Quantitative analysis of myofiber area in figure (<b>A</b>). (<b>C</b>) The protein expression of MyHC was analyzed by Western blot. β-Tubulin was used as the loading control. (<b>D</b>) Quantitative analysis of protein expression of MyHC. Data are displayed as the means ± SDs of six independent experiments. ** <span class="html-italic">p</span> &lt; 0.01 compared with the control group. ## <span class="html-italic">p</span> &lt; 0.01 compared with the injury group.</p> Full article ">
16 pages, 4478 KiB  
Article
PEAR1 Promotes Myoblast Proliferation Through Notch Signaling Pathway
by Yahao Zhao, Lu Zhang, Ruotong Hao, Shuang Li, Shufeng Li, Shuai Shi, Huili Tong and Bingchen Liu
Biology 2024, 13(12), 1063; https://doi.org/10.3390/biology13121063 - 19 Dec 2024
Viewed by 827
Abstract
PEAR1, also known as platelet endothelial aggregation receptor 1, is known to play a crucial role in the migration and differentiation of muscle satellite cells (MuSCs). However, its specific effects on skeletal muscle development and regeneration require further exploration. In this study, the [...] Read more.
PEAR1, also known as platelet endothelial aggregation receptor 1, is known to play a crucial role in the migration and differentiation of muscle satellite cells (MuSCs). However, its specific effects on skeletal muscle development and regeneration require further exploration. In this study, the expression of PEAR1; the proliferation marker proteins of Pax7, CCNB1, and PCNA; and the key molecules of N1-ICD, N2-ICD, and Hes1 were all increased gradually during the process of C2C12 cell proliferation. Furthermore, Western blotting and EdU results showed that when PEAR1 was over-expressed or inhibited, the proliferation status of C2C12 cell was increased or reduced respectively. This implied that PEAR1 could regulate myoblast proliferation and might be relate to Notch cell signaling pathway. A subsequent immunoprecipitation experiment result showed that the interaction between PEAR1 and Notch1 or Notch2, respectively. Then Western blotting and EdU results showed that the proliferation of C2C12 cell was inhibited under the treatment of Notch signaling pathway inhibitor RIN1. Meanwhile, the proliferation capacity of C2C12 cell could not be improved by treatment with RIN1 even though PEAR1 was over-expressed. These results showed that PEAR1 may regulated C2C12 cell proliferation though Notch signaling pathway. Additionally, a mouse model of muscle injury repair injected with bupivacaine hydrochloride was established in this study. Immunohistochemistry results exhibited that PEAR1 may regulate skeletal muscle post-injury regeneration relevant to Notch1 and Notch2 in different patterns. These findings provide valuable insights into the potential involvement of PEAR1 in skeletal muscle development and post-injury regeneration. Full article
(This article belongs to the Special Issue Repair and Regeneration of Skeletal Muscle)
►▼ Show Figures

Figure 1

Figure 1
<p><b>The expression pattern of PEAR1 and Notch signaling pathway during C2C12 cell proliferation.</b> (<b>A</b>) Western blotting results of PEAR1, Pax7, CCNB1, PCNA and marker proteins related to the Notch signaling pathway. (<b>B</b>–<b>J</b>). Statistical data based on A. Laminb1 is a nuclear reference protein for Western blotting detection. The different letters a, b, c, and d represent significant differences between different groups, while the same letters represent no significant differences between different treatment groups. The original Western Blot images can be found in the <a href="#app1-biology-13-01063" class="html-app">Supplementary File</a>.</p> Full article ">Figure 2
<p>PEAR1 regulates the expression of proliferative marker proteins and Notch cell signaling during C2C12 cell proliferation. (<b>A</b>) Western blotting results of the expression of Pax7, CCNB1, PCNA, and Notch signaling pathway marker proteins after PEAR1 over-expression; ctrl represents the control group (pcDNA3.1+ empty vector); PEAR1-OE represents the PEAR1 over-expression group. Laminb1 is a nuclear reference protein for Western blotting detection. (<b>B</b>) Statistical data based on A. (<b>C</b>) Western blotting results of the expression of Pax7, CCNB1, PCNA, and Notch signaling pathway marker proteins after PEAR1 was inhibited; ctrl represents the shRNA negative control group; shRNA represents the PEAR1 inhibition group. (<b>D</b>) Statistical data based on C. “*” for <span class="html-italic">p</span> &lt; 0.05, indicating significant difference, “**” for <span class="html-italic">p</span> &lt; 0.01, indicating extremely significant difference, and “***” for <span class="html-italic">p</span> &lt; 0.001, indicating extremely significant difference. The original Western Blot images can be found in the <a href="#app1-biology-13-01063" class="html-app">Supplementary File</a>.</p> Full article ">Figure 3
<p><b>PEAR1 regulates C2C12 cell proliferation.</b> (<b>A</b>,<b>C</b>) EdU results after PEAR1 over–expressed or inhibited in C2C12 cells. The blue signal represents for cell nuclei stained by Hoechst 33,342 and red signal represents EdU positive cells. (<b>B</b>,<b>D</b>) Statistical data based on (<b>A</b>,<b>C</b>), respectively. (<b>E</b>,<b>G</b>) Flow cytometry results after PEAR1 over–expressed or inhibited in C2C12 cells. (<b>F</b>,<b>H</b>) Statistical data based on (<b>E</b>,<b>G</b>), respectively. “*” for <span class="html-italic">p</span> &lt; 0.05, indicating significant difference.</p> Full article ">Figure 4
<p><b>Co-IP results of PEAR1 interacting with Notch1 or Notch2, respectively.</b> (<b>A</b>). Co-IP with Notch1 antibody followed by Western blotting using Notch1 and PEAR1 antibody. (<b>B</b>). Co-IP with PEAR1 antibody followed by Western blotting using PEAR1 and Notch1 antibody. (<b>C</b>). Co-IP with Notch2 antibody followed by Western blotting using Notch2 and PEAR1 antibody. (<b>D</b>). Co-IP with PEAR1 antibody followed by Western blotting using PEAR1 and Notch2 antibody. InPut represents positive control group, IgG represents negative control group, IP represents the target group. The original Western Blot images can be found in the <a href="#app1-biology-13-01063" class="html-app">Supplementary File</a>.</p> Full article ">Figure 5
<p><b>PEAR1 regulates C2C12 cell proliferation through the Notch signaling pathway.</b> (<b>A</b>) Western blotting results of Hes1, Pax7, CCNB1, and PCNA. (<b>B</b>–<b>E</b>) Statistical data based on (<b>A</b>). (<b>F</b>) EdU results in C2C12 cells treated by RIN1. The blue signal represents for cell nuclei stained by Hoechst 33,342, and the red signal represents EdU-positive cells. (<b>G</b>). Statistical data based on (<b>F</b>). (<b>H</b>) Western blotting results of PEAR1, Pax7, CCNB1, PCNA, and Hes1. (<b>I</b>–<b>M</b>) Statistical data based on (<b>H</b>). “**” for <span class="html-italic">p</span> &lt; 0.01, indicating extremely significant difference. Different letters of a, b and c represent significant differences between different groups, while the same letters represent no significant differences between different treatment groups. The original Western Blot images can be found in the <a href="#app1-biology-13-01063" class="html-app">Supplementary File</a>.</p> Full article ">Figure 6
<p><b>Expression localization of PEAR1, Pax7, Notch1, and Notch2 during skeletal muscle post-injury regeneration.</b> (<b>A</b>). HE staining was used to identify whether the mouse muscle injury repair model was successfully constructed. The red part is stained with eosin, which gives the cytoplasm a red color. The blue color is hematoxylin staining, which gives the nucleus a blue color. The indicators 0 D, 1 D, 3 D, 5 D, 7 D, and 14 D indicate that muscle injury repair was carried out on Day 0, Day 1, Day 3, Day 5, Day 7, and Day 14. (<b>B</b>). Western blotting results of PEAR1 and Notch signaling pathway molecules in the process of post-injury regeneration. (<b>C</b>–<b>H</b>). The results of the analysis based on (<b>B</b>). The different letters a, b, c, and d represent significant differences between different groups, while the same letters represent no significant differences between different treatment groups. The original Western Blot images can be found in the <a href="#app1-biology-13-01063" class="html-app">Supplementary File</a>.</p> Full article ">Figure 7
<p><b>Immunohistochemistry staining for PEAR1, Pax7, Notch1, and Notch2.</b> (<b>A</b>). Immunohistochemistry was used to detect the expression patterns of PEAR1, Pax7, Notch1, and Notch2 the skeletal muscle post-injury process. Regeneration brown signal refers to the staining of the target molecule by DAB, and blue refers to the staining of nucleus. The indicators 0 D, 1 D, 3 D, 5 D, 7 D, and 14 D indicate that skeletal muscle post-injury regeneration was carried out on Day 0, Day 1, Day 3, Day 5, Day 7, and Day 14. (<b>B</b>–<b>E</b>). The results of the analysis based on A.F. Immunohistochemistry was used to detect the expression and localization of PEAR1, Pax7, Notch1 and Notch2 on Day 3 after the injury. The same parts were photographed, and the picture content in the red box was selected for amplification. (<b>G</b>). Enlarged picture based on (<b>F</b>). Red arrows indicate the positive signals of Notch1, and green arrows indicate the positive signals of Notch2. The different letters a, b, c, d, e and f represent significant differences between different groups, while the same letters represent no significant differences between different treatment groups.</p> Full article ">

Review

Jump to: Research

26 pages, 1328 KiB  
Review
From Brain to Muscle: The Role of Muscle Tissue in Neurodegenerative Disorders
by Elisa Duranti and Chiara Villa
Biology 2024, 13(9), 719; https://doi.org/10.3390/biology13090719 - 12 Sep 2024
Cited by 4 | Viewed by 3202
Abstract
Neurodegenerative diseases (NDs), like amyotrophic lateral sclerosis (ALS), Alzheimer’s disease (AD), and Parkinson’s disease (PD), primarily affect the central nervous system, leading to progressive neuronal loss and motor and cognitive dysfunction. However, recent studies have revealed that muscle tissue also plays a significant [...] Read more.
Neurodegenerative diseases (NDs), like amyotrophic lateral sclerosis (ALS), Alzheimer’s disease (AD), and Parkinson’s disease (PD), primarily affect the central nervous system, leading to progressive neuronal loss and motor and cognitive dysfunction. However, recent studies have revealed that muscle tissue also plays a significant role in these diseases. ALS is characterized by severe muscle wasting as a result of motor neuron degeneration, as well as alterations in gene expression, protein aggregation, and oxidative stress. Muscle atrophy and mitochondrial dysfunction are also observed in AD, which may exacerbate cognitive decline due to systemic metabolic dysregulation. PD patients exhibit muscle fiber atrophy, altered muscle composition, and α-synuclein aggregation within muscle cells, contributing to motor symptoms and disease progression. Systemic inflammation and impaired protein degradation pathways are common among these disorders, highlighting muscle tissue as a key player in disease progression. Understanding these muscle-related changes offers potential therapeutic avenues, such as targeting mitochondrial function, reducing inflammation, and promoting muscle regeneration with exercise and pharmacological interventions. This review emphasizes the importance of considering an integrative approach to neurodegenerative disease research, considering both central and peripheral pathological mechanisms, in order to develop more effective treatments and improve patient outcomes. Full article
(This article belongs to the Special Issue Repair and Regeneration of Skeletal Muscle)
►▼ Show Figures

Figure 1

Figure 1
<p>A schematic representation of skeletal muscle structure. The image was created with the use of Servier Medical Art modified templates, licensed under a Creative Common Attribution 3.0 Unported License (<a href="https://smart.servier.com" target="_blank">https://smart.servier.com</a>, accessed on 28 August 2024).</p> Full article ">Figure 2
<p>A schematic representation of the accumulation of ROS leading to mitochondrial dysfunction and cellular damage. This cascade of events results in muscle atrophy and weakness. The image was created with the use of Servier Medical Art modified templates, licensed under a Creative Common Attribution 3.0 Unported License (<a href="https://smart.servier.com" target="_blank">https://smart.servier.com</a>, accessed on 28 August 2024).</p> Full article ">Figure 3
<p>The aggregates of α-synuclein caused by alterations in protein degradation pathways promote the muscle cell alterations typically found in PD patients. The image was created with the use of Servier Medical Art modified templates, licensed under a Creative Common Attribution 3.0 Unported License (<a href="https://smart.servier.com" target="_blank">https://smart.servier.com</a>, accessed on 28 August 2024).</p> Full article ">
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