ArticleThe Journal of cell biology1990
Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 146 citations in OpenAlex.
- Evaluating the effect of two-dimensional molecular layout on DNA origami-based transporters.Nanoscale advances · 2023Article
- Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC).Scientific reports · 2020Article
- An historical perspective of the discovery of titin filaments -Part 2.Biophysical reviews · 2018Review
- The multiple roles of titin in muscle contraction and force production.Biophysical reviews · 2018Review
- Structure of isolated Z-disks from honeybee flight muscle.Journal of muscle research and cell motility · 2017Article
- Spontaneous oscillatory contraction (SPOC) in cardiomyocytes.Biophysical reviews · 2015Article
- Impaired embryonic motility in dusp27 mutants reveals a developmental defect in myofibril structure.Disease models & mechanisms · 2014Article
- Individual globular domains and domain unfolding visualized in overstretched titin molecules with atomic force microscopy.PloS one · 2014Article
- Rbm20 regulates titin alternative splicing as a splicing repressor.Nucleic acids research · 2013Article
- Comprehensive analysis of titin protein isoform and alternative splicing in normal and mutant rats.Journal of cellular biochemistry · 2012Article
- Non-uniform distribution of strain during stretch of relaxed skeletal muscle fibers from rat soleus muscle.Journal of muscle research and cell motility · 2011Article
- SPontaneous Oscillatory Contraction (SPOC): auto-oscillations observed in striated muscle at partial activation.Biophysical reviews · 2011Review
- Thin filament-reconstituted skinned muscle fibers for the study of muscle physiology.Journal of biomedicine & biotechnology · 2011Review
- Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos.PloS one · 2010Article
- Inhibition of calpain prevents muscle weakness and disruption of sarcomere structure during hindlimb suspension.Journal of applied physiology (Bethesda, Md. : 1985) · 2010Article
- Dynamic strength of titin's Z-disk end.Journal of biomedicine & biotechnology · 2010Article
- Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation.Journal of muscle research and cell motility · 2006Review
- Isoform diversity of giant proteins in relation to passive and active contractile properties of rabbit skeletal muscles.The Journal of general physiology · 2005Article
- Viscoelastic properties of short calf muscle-tendon units of older women: effects of slow and fast passive dorsiflexion stretches in vivo.European journal of applied physiology · 2005Article
- A new muscle contractile system composed of a thick filament lattice and a single actin filament.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle needs an elastic framework to maintain its mechanical stability. Removal of thin filaments in rabbit skeletal muscle with plasma gelsolin has revealed the essential features of elastic filaments. The selective removal of thin filaments was confirmed by staining with phalloidin-rhodamine for fluorescence microscopy, examination of arrowhead formation with myosin subfragment 1 by electron microscopy, and analysis by SDS-PAGE. Thin section electron microscopy revealed the elastic fine filaments (approximately 4 nm in diameter) connecting thick filaments and the Z line. After removal of thin filaments, both rigor stiffness and active tension generation were lost, but the resting tension remained. These observations indicate that the thin filament-free fibers maintain a framework composed of the serial connections of thick filaments, the elastic filaments, and the Z line, which gives passive elasticity to the contractile system of skeletal muscle. The resting tension that remained in the thin filament-free fibers was decreased by mild trypsin treatment. The only protein component that was digested in parallel with the decrease in the resting tension and the disappearance of the elastic filaments was alpha-connectin (also called titin 1), which was transformed from the alpha to the beta form (from titin 1 to 2, respectively). Thus, we conclude that the main protein component of the elastic filaments is alpha-connectin (titin 1).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.