ArticleThe Journal of cell biology1992
Direct visualization of the dystrophin network on skeletal muscle fiber membrane.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Mechanotransduction and Skeletal Muscle Atrophy: The Interplay Between Focal Adhesions and Oxidative Stress.International journal of molecular sciences · 2025Review
- Duchenne muscular dystrophy: disease mechanism and therapeutic strategies.Frontiers in physiology · 2023Review
- Evolution and developmental functions of the dystrophin-associated protein complex: beyond the idea of a muscle-specific cell adhesion complex.Frontiers in cell and developmental biology · 2023Review
- Dystrophin missense mutations alter focal adhesion tension and mechanotransduction.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PDE10A Inhibition Reduces the Manifestation of Pathology in DMD Zebrafish and Represses the Genetic Modifier PITPNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2021Article
- Microutrophin expression in dystrophic mice displays myofiber type differences in therapeutic effects.PLoS genetics · 2020Article
- Multi-Compartment, Early Disruption of cGMP and cAMP Signalling in Cardiac Myocytes from theInternational journal of molecular sciences · 2020Article
- Pericytes in Muscular Dystrophies.Advances in experimental medicine and biology · 2019Article
- Dystrophin As a Molecular Shock Absorber.ACS nano · 2018Article
- Predictive model identifies key network regulators of cardiomyocyte mechano-signaling.PLoS computational biology · 2017Article
- Dystrophic Cardiomyopathy-Potential Role of Calcium in Pathogenesis, Treatment and Novel Therapies.Genes · 2017Review
- Filamentous structures in skeletal muscle: anchors for the subsarcolemmal space.Medical molecular morphology · 2015Article
- Article
- The carboxy-terminal third of dystrophin enhances actin binding activity.Journal of molecular biology · 2012Article
- Aquaporin 4 Expression in the mdx Mouse Diaphragm.Acta histochemica et cytochemica · 2011Article
- Biomechanics of the sarcolemma and costameres in single skeletal muscle fibers from normal and dystrophin-null mice.Journal of muscle research and cell motility · 2011Article
- Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic instability and protein aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Dystrophin and utrophin have distinct effects on the structural dynamics of actin.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Article
- Challenges and opportunities in dystrophin-deficient cardiomyopathy gene therapy.Human molecular genetics · 2006Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dystrophin, the protein product of the Duchenne muscular dystrophy (DMD) gene locus, is expressed on the muscle fiber surface. One key to further understanding of the cellular function of dystrophin would be extended knowledge about its subcellular organization. We have shown that dystrophin molecules are not uniformly distributed over the humen, rat, and mouse skeletal muscle fiber surface using three independent methods. Incubation of single-teased muscle fibers with antibodies to dystrophin revealed a network of denser transversal rings (costameres) and finer longitudinal interconnections. Double staining of longitudinal semithin cryosections for dystrophin and alpha-actinin showed spatial juxtaposition of the costameres to the Z bands. Where peripheral myonuclei precluded direct contact of dystrophin to the Z bands the organization of dystrophin was altered into lacunae harboring the myonucleus. These lacunae were surrounded by a dystrophin ring and covered by a more uniform dystrophin veil. Mechanical skinning of single-teased fibers revealed tighter mechanical connection of dystrophin to the plasma membrane than to the underlying internal domain of the muscle fiber. The entire dystrophin network remained preserved in its structure on isolated muscle sarcolemma and identical in appearance to the pattern observed on teased fibers. Therefore, connection of defined areas of plasma membrane or its constituents such as ion channels to single sarcomeres might be a potential function exerted by dystrophin alone or in conjunction with other submembrane cytoskeletal proteins.
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