Low-angle X-ray diffraction studies of living striated muscle during contraction

Elliott, G.F.; Lowy, J.; Millman, B. M.

doi:10.1016/0022-2836(67)90277-x

Cited by 164 publications

(73 citation statements)

References 23 publications

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“…There is evidence for the existence of electrostatic repulsive forces acting transversely between the filaments (Elliott, 1967;Rome, 1967). The constant-volume behaviour of the filament lattice during stretch (Huxley, 1953;Elliott, Lowy & Worthington, 1963) requires that the filaments move nearer together when a relaxed muscle is stretched, and if there is an electrostatic repulsion between them the force necessary to move them together must appear as a resting tension.…”

Section: Discussionmentioning

confidence: 99%

Tension due to interaction between the sliding filaments in resting striated muscle. the effect of stimulation

Hill¹

1968

The Journal of Physiology

391

296

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SUMAARY1. A resting sartorius muscle of the frog or toad possesses a special kind of elasticity which is shown to be due to a component lying between the two sets of filaments. The elastic effect is seen only for very small length changes, up to about 0-2 % of the muscle length, and the 'elastic limit' is then reached. If the length change then continues at a constant velocity the tension developed is maintained at a fixed level, producing a sort of frictional resistance. The component responsible is called the 'short-range elastic component', or SREC.2. It is also shown that a small part of the permanent tension of a resting muscle is probably due to 'active' interaction between the filaments. This is called the 'filamentary resting tension', or FRT. For a sarcomere length of 2-0 ,u the FRT amounts to about 150 mg in a muscle weighing 100 mg.3. The stiffness of the SREC and the magnitude of the FRT are shown to be related to one another. They are both increased, and may rise to high values, by making the external solution hypertonic.4. The working hypothesis is as follows. In a resting muscle the crossbridges on the myosin filaments are not entirely inactive, but a very small proportion of them are cross-linked with the actin filaments. The links are very stable and have a long 'life'. The elastic behaviour is due to the flexural rigidity, or spring-like properties of these bridges. The elasticity is 'short-range' because the bridges can be bent, or stretched, only a small way from the steady-state position before the contacts 'slip'. The 'filamentary resting tension' (which is present in the absence of any external length change) is attributed to an 'active process', which operates by imparting 'organized' potential energy to the participating cross-bridges, by potentiating their attachment. against their elastic resistance, to sites on the actin filaments which are displaced towards the Z line.5. It is shown that the ability of the muscle to maintain a 'frictional' resistance to a continuing, slow, length change is suppressed during a maintained tetanic contraction. The process of suppression starts during the period of the latency relaxation.6. It is suggested that the latency relaxation may be due to a reduction of the filamentary resting tension.7. The experiments with the latency relaxation were facilitated by the use of strongly hypertonic solutions. The positive twitch tension is then greatly reduced, or may be practically abolished, while the latency relaxation remains at about its normal size and is extended in duration.

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Section: Discussionmentioning

confidence: 99%

Tension due to interaction between the sliding filaments in resting striated muscle. the effect of stimulation

Hill¹

1968

The Journal of Physiology

391

296

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“…Alterations in interfilament lattice spacing, such as increases in the lattice spacing as a result of shortening, leads to sarcomere thickening and intracellular volume redistribution (Elliott et al 1963(Elliott et al , 1967Brandt et al 1967). In turn, the developed active tension decreases via decreased approximation of myosin and actin filaments, and thus less strong binding cross-bridges are formed (Rome 1972;Matsubara and Millman 1974b).…”

Section: Interfilament Lattice Spacing Versus Myocyte Lengtheningmentioning

confidence: 99%

Historical perspective on heart function: the Frank–Starling Law

Sequeira

Velden

2015

Biophys Rev

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More than a century of research on the FrankStarling Law has significantly advanced our knowledge about the working heart. The Frank-Starling Law mandates that the heart is able to match cardiac ejection to the dynamic changes occurring in ventricular filling and thereby regulates ventricular contraction and ejection. Significant efforts have been attempted to identify a common fundamental basis for the Frank-Starling heart and, although a unifying idea has still to come forth, there is mounting evidence of a direct relationship between length changes in individual constituents (cardiomyocytes) and their sensitivity to Ca 2+ ions. As the Frank-Starling Law is a vital event for the healthy heart, it is of utmost importance to understand its mechanical basis in order to optimize and organize therapeutic strategies to rescue the failing human heart. The present review is a historic perspective on cardiac muscle function. We Brevive^a century of scientific research on the heart's fundamental protein constituents (contractile proteins), to their assemblies in the muscle (the sarcomeres), culminating in a thorough overview of the several synergistically events that compose the Frank-Starling mechanism. It is the authors' personal beliefs that much can be gained by understanding the Frank-Starling relationship at the cellular and whole organ level, so that we can finally, in this century, tackle the pathophysiologic mechanisms underlying heart failure.

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“…However, since xray diffraction only reveals average values for the predominantly repetitive structures, and cross-bridge orientation is quite varied in vivo (13,24), the precise surface lattice of the cross-bridges has remained a point of dispute until recently (25,26,28).…”

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confidence: 99%

Axial arrangement of the myosin rod in vertebrate thick filaments: immunoelectron microscopy with a monoclonal antibody to light meromyosin.

Shimizu¹,

Dennis²,

Masaki³

et al. 1985

The Journal of Cell Biology

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A monoclonal antibody, MF20, which has been shown previously to bind the myosin heavy chain of vertebrate striated muscle, has been proven to bind the light meromyosin (LMM) fragment by solid phase radioimmune assay with alpha-chymotryptic digests of purified myosin. Epitope mapping by electron microscopy of rotary-shadowed, myosinantibody complexes has localized the antibody binding site to LMM at a point ~92 nm from the C-terminus of the myosin heavy chain. Since this epitope in native thick filaments is accessible to monoclonal antibodies, we used this antibody as a high affinity ligand to analyze the packing of LMM along the backbone of the thick filament. By immunofluorescence microscopy, MF20 was shown to bind along the entire A-band of chicken pectoralis myofibrils, although the epitope accessibility was greater near the ends than at the center of the A-bands. Thin-section, transmission electron microscopy of myofibrils decorated with MF20 revealed 50 regularly spaced, cross-striations in each half A-band, with a repeat distance of ~13 nm. These were numbered consecutively, 1-50, from the A-band to the last stripe, ~68 nm from the filament tips. These same striations could be visualized by negative staining of native thick filaments labeled with MF20. All 50 striations were of a consecutive, uninterrupted repeat which approximated the 14-15-nm axial translation of cross-bridges. Each half M-region contained five MF20 striations (~13 nm apart) with a distance between stripes 1 and 1', on each half of the bare zone, of ~18 nm. This is compatible with a packing model with full, antiparallel overlap of the myosin rods in the bare zone region. Differences in the spacings measured with negatively stained myofilaments and thin-sectioned myofibrils have been shown to arise from specimen shrinkage in the fixed and embedded preparations.These observations provide strong support for Huxley's original proposal for myosin packing in thick filaments of vertebrate muscle (Huxley, H. E., 1963, J. Mol. Biol., 7:281-308) and, for the first time, directly demonstrate that the 14-15-nm axial translation of LMM in the thick filament backbone corresponds to the cross-bridge repeat detected with x-ray diffraction of living muscle.The thick myofilaments of vertebrate skeletal muscle are complex polymeric structures composed predominantly of myosin but also contain a set of minor proteins including Mprotein (32, 50), C-protein (34, 40), myomesin (16), M-creatine kinase (51), H-protein (6), AMP deaminase (1), endprotein (49), and titin or connectin (31,54).A basic model for the structure of thick filaments was first described by H. E. Huxley (22). Based on electron microscopy

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Low-angle X-ray diffraction studies of living striated muscle during contraction

Cited by 164 publications

References 23 publications

Tension due to interaction between the sliding filaments in resting striated muscle. the effect of stimulation

Tension due to interaction between the sliding filaments in resting striated muscle. the effect of stimulation

Historical perspective on heart function: the Frank–Starling Law

Axial arrangement of the myosin rod in vertebrate thick filaments: immunoelectron microscopy with a monoclonal antibody to light meromyosin.

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