ArticleThe Journal of cell biology1998
Myosin heavy chains IIa and IId are functionally distinct in the mouse.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
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- Post-translational modifications of vertebrate striated muscle myosin heavy chains.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Homologous mutations in human β, embryonic, and perinatal muscle myosins have divergent effects on molecular power generation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Musculoskeletal defects associated with myosin heavy chain-embryonic loss of function are mediated by the YAP signaling pathway.EMBO molecular medicine · 2023Article
- Normal muscle fiber type distribution is recapitulated in aged ephrin-A3American journal of physiology. Cell physiology · 2023Article
- Postnatal Protein Intake as a Determinant of Skeletal Muscle Structure and Function in Mice-A Pilot Study.International journal of molecular sciences · 2022Article
- Effects of Low-Intensity and Long-Term Aerobic Exercise on the Psoas Muscle ofInternational journal of molecular sciences · 2022Article
- Aging-related metabolic changes in the extensor digitorum longus muscle of senescence-accelerated mouse-prone 8.Geriatrics & gerontology international · 2022Article
- Super-relaxed state of myosin in human skeletal muscle is fiber-type dependent.American journal of physiology. Cell physiology · 2020Article
- Vaccination mitigates influenza-induced muscular declines in aged mice.GeroScience · 2020Article
- Comparative analysis of the transcriptomes of EDL, psoas, and soleus muscles from mice.BMC genomics · 2020Article
- Myosin heavy chain-embryonic regulates skeletal muscle differentiation during mammalian development.Development (Cambridge, England) · 2020Article
- Mitochondrial ultrastructural adaptations in fast muscles of mice lacking IL15RA.Journal of cell science · 2018Article
- Morphological classification and comparison of suboccipital muscle fiber characteristics.Anatomy & cell biology · 2017Article
- Functional redundancy and nonredundancy between two Troponin C isoforms inMolecular biology of the cell · 2017Article
- Sarcolipin overexpression improves muscle energetics and reduces fatigue.Journal of applied physiology (Bethesda, Md. : 1985) · 2015Article
- Expression of the Troponin C at 41C Gene in Adult Drosophila Tubular Muscles Depends upon Both Positive and Negative Regulatory Inputs.PloS one · 2015Article
- Developmental MYH3 Myopathy Associated with Expression of Mutant Protein and Reduced Expression Levels of Embryonic MyHC.PloS one · 2015Article
- Role of cyclic AMP sensor Epac1 in masseter muscle hypertrophy and myosin heavy chain transition induced by β2-adrenoceptor stimulation.The Journal of physiology · 2014Article
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Authors and funding
6 authors.
Funding
Abstract
Myosin in adult murine skeletal muscle is composed primarily of three adult fast myosin heavy chain (MyHC) isoforms. These isoforms, MyHC-IIa, -IId, and -IIb, are >93% identical at the amino acid level and are broadly expressed in numerous muscles, and their genes are tightly linked. Mice with a null mutation in the MyHC-IId gene have phenotypes that include growth inhibition, muscle weakness, histological abnormalities, kyphosis (spinal curvature), and aberrant kinetics of muscle contraction and relaxation. Despite the lack of MyHC-IId, IId null mice have normal amounts of myosin in their muscles because of compensation by the MyHC-IIa gene. In each muscle examined from IId null mice, there was an increase in MyHC-IIa- containing fibers. MyHC-IIb content was unaffected in all muscles except the masseter, where its expression was extinguished in the IId null mice. Cross-sectional fiber areas, total muscle cross-sectional area, and total fiber number were affected in ways particular to each muscle. Developmental expression of adult MyHC genes remained unchanged in IId null mice. Despite this universal compensation of MyHC-IIa expression, IId null mice have severe phenotypes. We conclude that despite the similarity in sequence, MyHC-IIa and -IId have unique roles in the development and function of skeletal muscle.
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