ArticleBiophysical journal1994
Lattice spacing changes accompanying isometric tension development in intact single muscle fibers.
Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A mechanism for sarcomere breathing: volume change and advective flow within the myofilament lattice.Biophysical journal · 2021Article
- Effect of Active Lengthening and Shortening on Small-Angle X-ray Reflections in Skinned Skeletal Muscle Fibres.International journal of molecular sciences · 2021Article
- Article
- Nanometer-scale structure differences in the myofilament lattice spacing of two cockroach leg muscles correspond to their different functions.The Journal of experimental biology · 2020Article
- Structural and functional impact of troponin C-mediated CaJournal of molecular and cellular cardiology · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Multiscale and Multiaxial Mechanics of Vascular Smooth Muscle.Biophysical journal · 2017Article
- Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Biophysical journal · 2016Article
- Axial and radial forces of cross-bridges depend on lattice spacing.PLoS computational biology · 2010Article
- Nonlinear force-length relationship in the ADP-induced contraction of skeletal myofibrils.Biophysical journal · 2007Article
- Sarcomere-length dependence of lattice volume and radial mass transfer of myosin cross-bridges in rat papillary muscle.Pflugers Archiv : European journal of physiology · 2004Article
- Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.The Journal of physiology · 2003Article
- Length-dependent activation in three striated muscle types of the rat.The Journal of physiology · 2002Article
- Time-resolved X-ray diffraction by skinned skeletal muscle fibers during activation and shortening.Biophysical journal · 2001Article
- Z-line structural diversity in frog single muscle fiber in the passive state.Journal of muscle research and cell motility · 1999Article
- Volume changes of the myosin lattice resulting from repetitive stimulation of single muscle fibers.Biophysical journal · 1998Article
- Z/I and A-band lattice spacings in frog skeletal muscle: effects of contraction and osmolarity.Journal of muscle research and cell motility · 1998Article
- The stiffness of skeletal muscle in isometric contraction and rigor: the fraction of myosin heads bound to actin.Biophysical journal · 1998Article
- Diffusion of fluorescently labeled macromolecules in cultured muscle cells.Biophysical journal · 1996Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The myosin lattice spacing of single intact muscle fibers of the frog, Rana temporaria, was studied in Ringer's solution (standard osmolarity 230 mOsm) and hyper- and hypotonic salines (1.4 and 0.8 times standard osmolarity respectively) in the relaxed state, during "fixed end" tetani, and during shortening, using synchrotron radiation. At standard tonicity, a tetanus was associated with an initial brief lattice expansion (and a small amount of sarcomere shortening), followed by a slow compression (unaccompanied by sarcomere length changes). In hypertonic saline (myosin lattice compressed by 8.1%), these spacing changes were suppressed, in hypotonic saline (lattice spacing increased by 7.5%), they were enhanced. During unloaded shortening of activated fibers, a rapid lattice expansion occurred at all tonicities, but became larger as tonicity was reduced. This expansion was caused in part by the change in length of the preparation, but also by a recoil of a stressed radial compliance associated with axial force. The lattice spacing during unloaded shortening was equal to or occasionally greater than predicted for a relaxed fiber at that sarcomere length, indicating that the lattice compression associated with activation is rapidly reversed upon loss of axial force. Lattice recompression occurred upon termination of shortening under standard and hypotonic conditions, but was almost absent under hypertonic conditions. These observations indicate that axial cross-bridge tension is associated with a compressive radial force in intact muscle fibers at full overlap; however, this radial force exhibits a much greater sensitivity to lattice spacing than does the axial force.
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