Ask about this productRelated genes to: MYH2 antibody
- Gene:
- MYH2 NIH gene
- Name:
- myosin heavy chain 2
- Previous symbol:
- IBM3
- Synonyms:
- MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-06-22
- Gene:
- MYH4 NIH gene
- Name:
- myosin heavy chain 4
- Previous symbol:
- -
- Synonyms:
- MYH2B, MyHC-2B, MyHC-IIb
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-06-22
Related products to: MYH2 antibody
Related articles to: MYH2 antibody
- To reduce the risk of diseases caused by a reduction in skeletal muscle mass and quality, it is important to understand the molecular mechanisms underlying the maintenance and improvement of skeletal muscle mass and quality. Gα12 and/or Gα13 have been implicated in the regulation of myotube size through the mechanistic target of rapamycin complex 1 (mTORC1) signaling; however, their specific and potentially distinct molecular mechanisms remain unknown. Knockdown and rescue experiments revealed that the loss of Gα12 decreased myotube size, whereas the loss of Gα13 increased it. Gα12 knockdown reduced the phosphorylation levels of mTORC1 signaling components (Akt, mTOR, and p70S6K) and the levels of puromycin-labeled proteins, whereas Gα13 knockdown increased these levels. Loss of Gα12 or Gα13 suppressed SRF-RE-dependent transcriptional activity. While expression of a constitutively active form of RhoA (RhoA-CA) activated SRF-RE activity, notably, RhoA-CA expression did not affect myotube size, nor did it alter myotube atrophy induced by Gα12 knockdown or hypertrophy induced by Gα13 knockdown. Depletion of Gα12 increased the mRNA expression of oxidative myosin heavy chain (MyHC) isoforms Myh7 and Myh2 and decreased the mRNA expression of Myh1 and Myh4, whereas depletion of Gα13 increased the mRNA expression of Myh7, Myh2, Myh1, and Myh4. These results indicate that loss of Gα12 induces myotube atrophy by suppressing mTORC1 signaling and protein synthesis, whereas loss of Gα13 induces myotube hypertrophy by enhancing these processes, likely independent of SRF-RE-mediated transcription. Notably, Gα12 and Gα13 oppositely regulated the mRNA expression of MyHC isoforms, particularly Myh1 and Myh4. - Source: PubMed
Publication date: 2026/01/21
Kubota MaiFujita ShuheiKamata RyoheiTamura KazumaSugimoto KeiichiroKitakaze TomoyaHarada NaokiYamaji Ryoichi - Skeletal muscle is a dynamic tissue capable of structural and metabolic remodeling in response to physiological and pathological stimuli. These adaptations are central to understanding the mechanisms underlying conditions such as genetic myopathies, cancer, aging, and recovery from injury. Muscle fiber characterization-assessing fiber type, size, and metabolic profile-is essential for such studies. However, conventional histological methods often rely on serial tissue sections and multiple staining protocols, which are time-consuming, require significant biological material, and introduce methodological bias. - Source: PubMed
Publication date: 2025/11/21
Di Gallo MaximeGuilbert ThomasPereira DorianeCepella ZoéBraud-Mussi RaphaëlJauliac EdgarMacaux GaspardBritto Florian AlexisLaunay Thierry - Skeletal muscle tissue consists of not only myofibers, i.e., muscle cells, but also intramuscular adipocytes. Our previous study demonstrated that adipocytes produce secretory factors during differentiation, leading us to hypothesize that soluble factors derived from adipocytes regulate gene expression and cellular function in muscle cells. Yet the mechanism by which coexisting adipocytes influence muscle cells remains unclear. Here, microarray analysis was used to examine transcriptional changes in muscle cells under two co-culture conditions: myoblasts co-cultured with differentiated adipocytes and myotubes co-cultured with preadipocytes. Gene Ontology terms related to cell adhesion, extracellular matrix (ECM) organization, and metabolic processes were significantly enriched in both conditions. We also assessed the influence of adipocyte co-culture on myogenic differentiation and fiber type-specific gene expression. In myoblasts, co-culture with differentiated adipocytes had no significant effect on the expression of myogenic regulatory factors, whereas Myh2 and Myh4 expression was markedly increased in myotubes co-cultured with preadipocytes. These results indicate that adipocyte-derived soluble factors alter the transcriptional landscape of muscle cells, especially genes involved in ECM remodeling and metabolic regulation. This intercellular communication likely contributes to structural and metabolic adaptations in skeletal muscle tissue in vivo. - Source: PubMed
Publication date: 2025/11/17
Ojima KoichiMuroya SusumuOe MikaNishimura Takanori - Capsaicin and menthol, agonists of transient receptor potential channels, are known to influence energy metabolism. However, their roles in skeletal muscle function are unclear. Therefore, this study aimed to investigate the effects of capsaicin and menthol on skeletal muscle differentiation and muscle quality. In vitro, capsaicin and menthol increased myosin heavy chain (MYH)4 expression, while menthol upregulated MYH1. Both compounds reduced MYH2 and MYH7 levels. Additionally, capsaicin enhanced uncoupling protein (UCP)3 expression, and menthol increased UCP2, UCP3, and M-type creatine kinase. In vivo, topical application during voluntary running did not affect body or muscle mass, but capsaicin reduced fat mass and increased locomotor activity. Menthol enhanced light-phase activity. Both treatments elevated MYH4, UCP2, and UCP3 in muscle, and suppressed myostatin expression. These findings suggest capsaicin and menthol modulate skeletal muscle phenotype and metabolism through both direct cellular effects and increased physical activity. - Source: PubMed
Yamamoto HiroyukiKojima KotaKasai ShutoTakimoto YusukeKato AyaYamamoto KaichiMoriya YunaKoida AyakaAgata Umon - The process of skeletal muscle regeneration entails alterations in the relative composition of muscle fiber types, yet the regulatory mechanisms remain incompletely understood. This study aimed to investigate the role of melatonin in regulating the regeneration of slow muscle fibers during skeletal muscle repair and its underlying mechanisms. Using a tibialis anterior muscle frostbite model in 6-8-week-old male C57BL/6J mice, in vivo experiments revealed that intraperitoneal melatonin administration significantly increased Myh7/Myh2 protein expression while reducing Myh1/Myh4 levels. In vitro, melatonin-treated C2C12 myoblasts exhibited elevated oxygen consumption, mitochondrial mass, mitochondrial respiratory chain complexes activity, ATP production, mtDNA content, and membrane potential, alongside reduced LDH activity and ROS levels. Transcriptional upregulation of genes linked to mitochondrial complexes assembly, oxidative phosphorylation, and ATP synthesis was observed. Mechanistically, melatonin activated the AMPK/PGC-1α pathway, as evidenced by Compound C (AMPK inhibitor) pretreatment reversing these effects, decreasing p-AMPK/AMPK ratios, PGC-1α, and slow fiber markers (Myh7/Myh2), while increasing ROS and fast fiber marker (Myh4). The results indicate that melatonin facilitates the formation of slow-twitch fibers during muscle repair by augmenting mitochondrial function through the AMPK/PGC-1α signaling pathway. Consequently, these findings imply that melatonin improves mitochondrial function via AMPK/PGC-1α signaling, thereby promoting the regeneration of slow muscle fibers and facilitating the repair of skeletal muscle damage. - Source: PubMed
Xie WeiHong ZhengchaoXie YuxinHou KangyanLi SonghanFang MingxinGuan YupengZhang ZhixuanZhang Miao