Literature DB >> 3264728

Filament lattice of frog striated muscle. Radial forces, lattice stability, and filament compression in the A-band of relaxed and rigor muscle.

B M Millman1, T C Irving.   

Abstract

Repulsive pressure in the A-band filament lattice of relaxed frog skeletal muscle has been measured as a function of interfilament spacing using an osmotic shrinking technique. Much improved chemical skinning was obtained when the muscles were equilibrated in the presence of EGTA before skinning. The lattice shrank with increasing external osmotic pressure. At any specific pressure, the lattice spacing in relaxed muscle was smaller than that of muscle in rigor, except at low pressures where the reverse was found. The lattice spacing was the same in the two states at a spacing close to that found in vivo. The data were consistent with an electrostatic repulsion over most of the pressure range. For relaxed muscle, the data lay close to electrostatic pressure curves for a thick filament charge diameter of approximately 26 nm, suggesting that charges stabilizing the lattice are situated about midway along the thick filament projections (HMM-S1). At low pressures, observed spacings were larger than calculated, consistent with the idea that thick filament projections move away from the filament backbone. Under all conditions studied, relaxed and rigor, at short and very long sarcomere lengths, the filament lattice could be modeled by assuming a repulsive electrostatic pressure, a weak attractive pressure, and a radial stiffness of the thick filaments (projections) that differed between relaxed and rigor conditions. Each thick filament projection could be compressed by approximately 5 or 2.6 nm requiring a force of 1.3 or 80 pN for relaxed and rigor conditions respectively.

Entities:  

Mesh:

Year:  1988        PMID: 3264728      PMCID: PMC1330343          DOI: 10.1016/S0006-3495(88)82977-1

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  35 in total

1.  Liquid-crystalline characteristics of the thick filament lattice of striated muscle.

Authors:  E W April
Journal:  Nature       Date:  1975-09-11       Impact factor: 49.962

2.  A structural study of gels, in the form of threads, of myosin and myosin rod.

Authors:  P H Cooke; E M Bartels; G F Elliott; R A Hughes
Journal:  Biophys J       Date:  1987-06       Impact factor: 4.033

3.  X-ray evidence for radial cross-bridge movement and for the sliding filament model in actively contracting skeletal muscle.

Authors:  J C Haselgrove; H E Huxley
Journal:  J Mol Biol       Date:  1973-07-15       Impact factor: 5.469

Review 4.  The structure of F-actin.

Authors:  E H Egelman
Journal:  J Muscle Res Cell Motil       Date:  1985-04       Impact factor: 2.698

5.  X-ray diffraction observations of chemically skinned frog skeletal muscle processed by an improved method.

Authors:  A Magid; M K Reedy
Journal:  Biophys J       Date:  1980-04       Impact factor: 4.033

6.  Donnan potentials from the A- and I-bands of glycerinated and chemically skinned muscles, relaxed and in rigor.

Authors:  E M Bartels; G F Elliott
Journal:  Biophys J       Date:  1985-07       Impact factor: 4.033

7.  Lateral forces in the filament lattice of vertebrate striated muscle in the rigor state.

Authors:  B M Millman; K Wakabayashi; T J Racey
Journal:  Biophys J       Date:  1983-03       Impact factor: 4.033

8.  Low-angle x-ray diffraction studies of living striated muscle during contraction.

Authors:  G F Elliott; J Lowy; B M Millman
Journal:  J Mol Biol       Date:  1967-04-14       Impact factor: 5.469

9.  Critical dependence of calcium-activated force on width in highly compressed skinned fibers of the frog.

Authors:  J Gulati; A Babu
Journal:  Biophys J       Date:  1985-11       Impact factor: 4.033

10.  Role of calcium in triggering rapid ultrastructural damage in muscle: a study with chemically skinned fibres.

Authors:  C J Duncan
Journal:  J Cell Sci       Date:  1987-05       Impact factor: 5.285

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  17 in total

1.  Thermodynamic features of myosin filament suspensions: implications for the modeling of muscle contraction.

Authors:  E Grazi; O Cintio
Journal:  Biophys J       Date:  2001-07       Impact factor: 4.033

2.  Troponin I in the murine myocardium: influence on length-dependent activation and interfilament spacing.

Authors:  John P Konhilas; Thomas C Irving; Beata M Wolska; Eias E Jweied; Anne F Martin; R John Solaro; Pieter P de Tombe
Journal:  J Physiol       Date:  2003-01-24       Impact factor: 5.182

3.  Diffraction ellipsometry studies of osmotically compressed muscle fibers.

Authors:  W L Kerr; R J Baskin; Y Yeh
Journal:  Pflugers Arch       Date:  1990-08       Impact factor: 3.657

4.  Z-line/I-band and A-band lattices of intact frog sartorius muscle at altered interfilament spacing.

Authors:  T C Irving; B M Millman
Journal:  J Muscle Res Cell Motil       Date:  1992-02       Impact factor: 2.698

5.  Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.

Authors:  Daisuke Miyashiro; Jun'ichi Wakayama; Nao Akiyama; Yuki Kunioka; Takenori Yamada
Journal:  J Physiol Sci       Date:  2013-05-21       Impact factor: 2.781

6.  Z/I and A-band lattice spacings in frog skeletal muscle: effects of contraction and osmolarity.

Authors:  T C Irving; Q Li; B A Williams; B M Millman
Journal:  J Muscle Res Cell Motil       Date:  1998-10       Impact factor: 2.698

7.  An electrostatic model with weak actin-myosin attachment resolves problems with the lattice stability of skeletal muscle.

Authors:  D A Smith; D G Stephenson
Journal:  Biophys J       Date:  2011-06-08       Impact factor: 4.033

8.  Cross-bridge movement in rat slow skeletal muscle as a function of calcium concentration.

Authors:  H Honda; Y Koiwa; N Yagi; I Matsubara
Journal:  Pflugers Arch       Date:  1996-09       Impact factor: 3.657

9.  Radial equilibrium lengths of actomyosin cross-bridges in muscle.

Authors:  B Brenner; S Xu; J M Chalovich; L C Yu
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

10.  Changes in myofibrillar structure and function produced by N-terminal deletion of the regulatory light chain in Drosophila.

Authors:  T Irving; S Bhattacharya; I Tesic; J Moore; G Farman; A Simcox; J Vigoreaux; D Maughan
Journal:  J Muscle Res Cell Motil       Date:  2001       Impact factor: 2.698

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