When mammals are constrained to hypogravity, their neuromuscular apparatus undergoes modifications which rend difficult postural maintenance and muscular activity upon the return to normal gravitational conditions. Muscle atrophy and differetial gene expression are particularly evident in slow-twitch antigravity muscles such as the soleus. During hypogravity, most of the metabolic and contractile properties characteristic of slow-twitch muscles shift toward to those of fast-twitch muscles. For example, the expression of the fast isoforms of both the myosin heavy-chain and the sarcoplasmic reticulum calcium pump increases in slow-twitch muscle during hypogravity. Thus, modifications of the contractile machinery and calcium handling are likely to be involved in the hypogravity-induced slow-twitch muscle impariment. Fast- and slow-twitch muscles differ also in their electrical properties. Resting membrane potential (RMP) is more negative by about 10 mV in fast muscles compared to slow ones. Differences in action potential (AP) shape as well as in the number of elicitable APs have been also observed between both muscle types, which may reslut from the reported differences in chloride conductance and sodium current. Little is known about the potential modification fo muscle electrical properties during hypogravity, apart a negative shift of the RMP in soleus muscle. Thus this study was performed at the aim to compare the excitability parameters and sodium channel behavior of rat fast-twitch and slow-twitch muscle fibers. The characterization of these properties specific for each muscle-type will give us the basis for the study of the effect of hypogravity.
Download full-text PDF |
Source |
---|
Nat Metab
January 2025
Tongji Shanxi Hospital, Shanxi Bethune Hospital, Shanxi Academy of Medical Science, Third Hospital of Shanxi Medical University, the Key Laboratory of Endocrine and Metabolic Diseases of Shanxi Province, Taiyuan, China.
Skeletal muscle is a critical organ in maintaining homoeostasis against metabolic stress, and histone post-translational modifications are pivotal in those processes. However, the intricate nature of histone methylation in skeletal muscle and its impact on metabolic homoeostasis have yet to be elucidated. Here, we report that mitochondria-rich slow-twitch myofibers are characterized by significantly higher levels of H3K36me2 along with repressed expression of Kdm2a, an enzyme that specifically catalyses H3K36me2 demethylation.
View Article and Find Full Text PDFBiomolecules
December 2024
Department of Aerospace Medical Training, School of Aerospace Medicine, Fourth Military Medical University, Xi'an 710032, China.
Skeletal muscle atrophy, which is induced by factors such as disuse, spaceflight, certain medications, neurological disorders, and malnutrition, is a global health issue that lacks effective treatment. Hindlimb unloading is a commonly used model of muscle atrophy. However, the underlying mechanism of muscle atrophy induced by hindlimb unloading remains unclear, particularly from the perspective of the myocyte proteome and metabolism.
View Article and Find Full Text PDFFASEB J
January 2025
Department of Neurology, Songjiang Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai, China.
Skeletal muscle function gradually declines with aging, presenting substantial health and societal challenges. Comparative analysis of how aging affects fast- and slow-twitch muscles remains lacking. We utilized 20-month-old mice to reveal the aging effects on muscle structure and fiber composition, followed by bulk RNA sequencing for fast- and slow-twitch muscles and integration with human single-cell RNA sequencing dataset providing a comparative analysis across species.
View Article and Find Full Text PDFNeuropathol Appl Neurobiol
February 2025
Department of Neurology, Neuromuscular Diseases Unit, Hospital de la Santa Creu i Sant Pau, Institut de Recerca Sant Pau (IR Sant Pau), Barcelona, Spain.
Aims: Sarcoendoplasmic reticulum Ca-ATPase 2 (SERCA2), encoded by ATP2A2, is a key protein involved in intracellular Ca homeostasis. The SERCA2a isoform is predominantly expressed in cardiomyocytes and type I myofibres. Variants in this gene are related to Darier disease, an autosomal dominant dermatologic disorder, but have never been linked to myopathy.
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Institute of Immunology and Physiology, Russian Academy of Sciences, 620049 Yekaterinburg, Russia.
The cardiac myosin binding protein-C (cMyBP-C) regulates cross-bridge formation and controls the duration of systole and diastole at the whole heart level. As known, mutations in cMyBP-C increase the cross-bridge number and rate of their cycling, hypercontractility, and myocardial hypertrophy. We investigated the effects of the mutations D75N and P161S of cMyBP-C related to hypertrophic cardiomyopathy on the mechanism of force generation in isolated slow skeletal muscle fibers.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!