Reconstruction of 3D Muscle Fiber Structure Using High Resolution Cryosectioned Volume

2018 ◽  
pp. 85-94 ◽  
Author(s):  
Yoshito Otake ◽  
Kohei Miyamoto ◽  
Axel Ollivier ◽  
Futoshi Yokota ◽  
Norio Fukuda ◽  
...  
Keyword(s):  
High Resolution ◽  
Muscle Fiber ◽  
Fiber Structure

How to sample the entire length of a single muscle fiber quick-frozen after electrical point stimulation for high resolution EM

1992 ◽  
Vol 50 (1) ◽  
pp. 776-777
Author(s):  
Joachim R. Sommer ◽  
Teresa High ◽  
Betty Scherer ◽  
Isaiah Taylor ◽  
Rashid Nassar
Keyword(s):  
Skeletal Muscle ◽  
High Resolution ◽  
Action Potential ◽  
Muscle Fiber ◽  
Freeze Fracture ◽  
Freeze Substitution ◽  
Electrical Field Stimulation ◽  
Skeletal Muscle Fiber ◽  
Freeze Dried ◽  
Quick Freezing

We have developed a model that allows the quick-freezing at known time intervals following electrical field stimulation of a single, intact frog skeletal muscle fiber isolated by sharp dissection. The preparation is used for studying high resolution morphology by freeze-substitution and freeze-fracture and for electron probe x-ray microanlysis of sudden calcium displacement from intracellular stores in freeze-dried cryosections, all in the same fiber. We now show the feasibility and instrumentation of new methodology for stimulating a single, intact skeletal muscle fiber at a point resulting in the propagation of an action potential, followed by quick-freezing with sub-millisecond temporal resolution after electrical stimulation, followed by multiple sampling of the frozen muscle fiber for freeze-substitution, freeze-fracture (not shown) and cryosectionmg. This model, at once serving as its own control and obviating consideration of variances between different fibers, frogs etc., is useful to investigate structural and topochemical alterations occurring in the wake of an action potential.

scholarly journals High-resolution TEM Studies on Fiber Structure

1990 ◽  
Vol 46 (9) ◽  
pp. P388-P394
Author(s):  
MASAKI TSUJI ◽  
KEN-ICHI KATAYAMA
Keyword(s):  
High Resolution ◽  
Fiber Structure ◽  
High Resolution Tem

Diffusion Tensor Imaging for Spatially-Resolved Characterization of Muscle Fiber Structure in Seafood

2022 ◽  
pp. 132099
Author(s):  
Kathryn E. Anderssen ◽  
Mathias Kranz ◽  
Shaheen Syed ◽  
Svein Kristian Stormo
Keyword(s):  
Diffusion Tensor Imaging ◽  
Muscle Fiber ◽  
Diffusion Tensor ◽  
Fiber Structure ◽  
Spatially Resolved

Mimicking muscle fiber structure and function through electromechanical actuation of electrospun silk fiber bundles

2017 ◽  
Vol 5 (40) ◽  
pp. 8105-8114 ◽  
Author(s):  
S. Y. Severt ◽  
S. L. Maxwell ◽  
J. S. Bontrager ◽  
J. M. Leger ◽  
A. R. Murphy
Keyword(s):  
Conducting Polymers ◽  
Muscle Fiber ◽  
Contractile Function ◽  
Structure And Function ◽  
Silk Fiber ◽  
Fiber Bundles ◽  
Fiber Structure ◽  
And Function ◽  
Electromechanical Actuation

Fiber bundles composed of silk and conducting polymers undergo linear actuation, thus mimicking the structure and contractile function of muscles.

Muscle fiber structure in an aging long‐lived seabird, the black‐legged kittiwake ( Rissa tridactyla )

2019 ◽  
Vol 280 (7) ◽  
pp. 1061-1070 ◽  
Author(s):  
Karl Brown ◽  
Ana Gabriela Jimenez ◽  
Shannon Whelan ◽  
Kristen Lalla ◽  
Scott A. Hatch ◽  
...  
Keyword(s):  
Muscle Fiber ◽  
Fiber Structure ◽  
Rissa Tridactyla

scholarly journals 493 The Influence of Muscle Fiber Structure on Meat Palatability.

2018 ◽  
Vol 96 (suppl_3) ◽  
pp. 273-274
Author(s):  
J Gonzalez ◽  
J Drouillard ◽  
T O’Quinn ◽  
K Phelps
Keyword(s):  
Muscle Fiber ◽  
Fiber Structure

scholarly journals Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels

2019 ◽  
Vol 151 (8) ◽  
pp. 1007-1016 ◽  
Author(s):  
Yahor Savich ◽  
Benjamin P. Binder ◽  
Andrew R. Thompson ◽  
David D. Thomas
Keyword(s):  
High Resolution ◽  
Muscle Fiber ◽  
Light Chain ◽  
Fluorescence Polarization ◽  
Myosin Light Chain ◽  
Angular Resolution ◽  
Muscle Fibers ◽  
Fiber Axis ◽  
X Ray ◽  
Lever Arm

Despite advances in x-ray crystallography, cryo-electron microscopy (cryo-EM), and fluorescence polarization, none of these techniques provide high-resolution structural information about the myosin light chain domain (LCD; lever arm) under ambient conditions in vertebrate muscle. Here, we measure the orientation of LCD elements in demembranated muscle fibers by electron paramagnetic resonance (EPR) using a bifunctional spin label (BSL) with an angular resolution of 4°. To achieve stereoselective site-directed labeling with BSL, we engineered a pair of cysteines in the myosin regulatory light chain (RLC), either on helix E or helix B, which are roughly parallel or perpendicular to the myosin lever arm, respectively. By exchanging BSL-labeled RLC onto oriented muscle fibers, we obtain EPR spectra from which the angular distributions of BSL, and thus the lever arm, can be determined with high resolution relative to the muscle fiber axis. In the absence of ATP (rigor), each of the two labeled helices exhibits both ordered (σ ∼9–11°) and disordered (σ > 38°) populations. Using these angles to determine the orientation of the lever arm (LCD combined with converter subdomain), we observe that the oriented population corresponds to a lever arm that is perpendicular to the muscle fiber axis and that the addition of ATP in the absence of Ca2+ (inducing relaxation) shifts the orientation to a much more disordered orientational distribution. Although the detected orientation of the myosin light chain lever arm is ∼33° different than predicted from a standard “lever arm down” model based on cryo-EM of actin decorated with isolated myosin heads, it is compatible with, and thus augments and clarifies, fluorescence polarization, x-ray interference, and EM data obtained from muscle fibers. These results establish feasibility for high-resolution detection of myosin LCD rotation during muscle contraction.

scholarly journals Effects of Oral Glutamine Supplementation on Early Postnatal Muscle Morphology in Low and Normal Birth Weight Piglets

Animals ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 1976
Author(s):  
Yaolu Zhao ◽  
Elke Albrecht ◽  
Quentin L. Sciascia ◽  
Zeyang Li ◽  
Solvig Görs ◽  
...  
Keyword(s):  
Birth Weight ◽  
Muscle Fiber ◽  
Lipid Droplets ◽  
Glutamine Supplementation ◽  
Lipid Deposition ◽  
Normal Birth Weight ◽  
Fiber Structure ◽  
Maternal Milk ◽  
Normal Birth ◽  
Adipocyte Development

Adapted nutrition can improve the growth of low birth weight (LBW) piglets. Since maternal milk is thought to provide insufficient glutamine (Gln) for LBW piglets, the current study investigated the influence of Gln supplementation during the early suckling period on development and lipid deposition in skeletal muscle. The weight differences between LBW and normal birth weight (NBW) littermates persisted from birth to slaughter (p < 0.001). However, intramuscular Gln and Ala concentrations were altered in piglets according to the supplementation (p < 0.01). There were larger muscle fibers (p = 0.048) in Gln-supplemented piglets. Capillarization or nuclei number per muscle fiber was not influenced by birth weight (BiW) or Gln supplementation. Abundance of myosin heavy chain (MYH) isoforms was slightly altered by Gln supplementation. LBW piglets had more lipid droplets than NBW piglets at day 5 of life in both muscles (p < 0.01). The differences decreased with age. Adipocyte development increased with age, but was not influenced by BiW or supplementation. The results indicate that BiW differences were accompanied by differences in lipid deposition and muscle fiber structure, suggesting a delayed development in LBW piglets. Supplementation with Gln may support piglets to overcome those disadvantages.

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