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
- Obesity and diabetes impair the ability of the muscle to regenerate, repair and remodel, resulting in a gradual decrease in muscle mass and function. However, the underlying mechanisms and effective therapeutic strategies remain poorly understood. M2 macrophages within skeletal muscle play an important role in tissue recovery following injury. This study aims to investigate the role of M2 macrophages derived transforming growth factor-beta 1 (Tgf-β1) in regulation of skeletal muscle function under diet-induced obese conditions. - Source: PubMed
Bilal MuhammadAnh Le DucPhuong Nguyen QuynhKhalid SanaNawaz AllahMemoona Aslam Muhammad RahilKado TomonobuWatanabe YoshiyukiNishimura AyumiIgarashi YoshikoSharif AamirOnogi YasuhiroWada TsutomuHayashi RyujiHirabayashi KenichiYamamoto SeijiNakagawa TakashiMori HisashiUsui IsaoKato MasaruFujisaka ShihoTobe Kazuyuki - Monoalkyldiacylglycerols (MADG), ether-type glycerolipids found in deep-sea fish animals, promote myotube formation in C2C12 myoblasts. In this study, we investigated the effects of MADG on skeletal muscle regeneration in a mouse model of cardiotoxin-induced muscle injury. Male C57BL/6J mice were fed a diet supplemented with 0.5% MADG for 2 weeks, followed by cardiotoxin injection into the tibialis anterior muscle, and maintained on the experimental diets for up to an additional 2 weeks. The MADG diet increased the number and total area of myofibers 7 and 14 days post-injury compared with the normal diet group. mRNA levels of the myogenic regulatory factors MyoD and Myogenin increased, whereas those of inflammatory factors and satellite cell marker, remained unchanged. Immunohistochemical staining for myofiber type markers showed that dietary MADG promoted a shift toward a more fast-type phenotype, characterized by an increase in the number and proportion of MHC4-positive type Ⅱb fibers. In C2C12 myoblasts and mouse satellite cells, treatment with batyl alcohol, a MADG metabolite, increased Myh4 mRNA expression and decreased Myh2 mRNA expression. Overall, MADG promotes skeletal muscle regeneration and has the potential to induce a fast-twitch shift, accompanied by an increased proportion of type IIb myofibers during muscle repair. These results contribute to a better understanding of the regulation of myofiber types underlying skeletal muscle function and homeostasis. - Source: PubMed
Publication date: 2026/06/01
Imamura KyosukeTakatani NaokiHosokawa MasashiBeppu Fumiaki - 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