ArticleProceedings of the National Academy of Sciences of the United States of America1984
Denervated skeletal muscle displays discoordinate regulation for the synthesis of several myofibrillar proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 57 citations in OpenAlex.
- Caveolin-3: A Causative Process of Chicken Muscular Dystrophy.Biomolecules · 2020Review
- Longitudinal Changes in Glucose Metabolism of Denervated Muscle after Complete Peripheral Nerve Injury.Molecular imaging and biology · 2016Article
- Role of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC-1α) in denervation-induced atrophy in aged muscle: facts and hypotheses.Longevity & healthspan · 2013Article
- Targeted ablation of TRAF6 inhibits skeletal muscle wasting in mice.The Journal of cell biology · 2010Article
- Ectopic expression of an embryonic skeletal myosin heavy chain in human fetal and Syrian hamster hearts.Journal of muscle research and cell motility · 2003Article
- Id-1 as a possible transcriptional mediator of muscle disuse atrophy.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Denervated chicken breast muscle displays discoordinate regulation and differential patterns of expression of alpha f and beta tropomyosin genes.Journal of muscle research and cell motility · 1993Article
- Neural regulation of differentiation of rat skeletal muscle cell types.Histochemistry · 1992Article
- Myogenesis and histogenesis of skeletal muscle on flexible membranes in vitro.In vitro cellular & developmental biology : journal of the Tissue Culture Association · 1990Article
- Developmental regulation of the multiple myogenic cell lineages of the avian embryo.The Journal of cell biology · 1986Article
- Neonatal and adult myosin heavy chain isoforms in a nerve-muscle culture system.The Journal of cell biology · 1986Article
- The myosin alkali light chain proteins and their genes.The Biochemical journal · 1985Review
- The presence of two skeletal muscle alpha-actinins correlates with troponin-tropomyosin expression and Z-line width.The Journal of cell biology · 1985Article
- Unusual fast myosin isozyme pattern in the lateral gastrocnemius of the chicken.Journal of muscle research and cell motility · 1985Article
- Denervation of rat adrenal glands markedly increases preproenkephalin mRNA.Proceedings of the National Academy of Sciences of the United States of America · 1984Article
- Activity-dependent regulation of gene expression in muscle and neuronal cells.Molecular neurobiologyReview
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3 authors at 1 institution in 1 country.
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Abstract
Synthesis patterns of myosin heavy- and light-chain isoforms, tropomyosin and troponin, have been studied in chicken fast muscle denervated at both neonatal and adult stages. Denervated neonatal muscle does not synthesize the adult myosin heavy-chain isoform at the time of denervation, but it does synthesize the adult isoform several months after denervation. Thus, innervation does not appear to be necessary for the normal sequential replacement of embryonic and neonatal myosin heavy chain by the adult variant. Nerve is required, however, for the regulation of tropomyosin and troponin expression. Normally the pectoralis major muscle represses synthesis of both beta-tropomyosin and leg-type troponin T during late embryonic development. After denervation, however, the muscle relaxes its ongoing repression of these proteins and significant amounts of both beta-tropomyosin and leg-type troponin T are synthesized by the muscle. Denervation also results in an altered pattern of myosin light-chain synthesis so that the ratio of fast light-chain 3/fast light-chain 1 decreases. Similar results are found in muscle denervated at the adult stage. In denervated muscle, therefore, synthesis of these myofibrillar proteins is not coordinated: ongoing isoform shifts proceed to express an adult pattern of myosin heavy chain while tropomyosin, troponin, and myosin light-chain patterns appear to revert to embryonic configurations.
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