Three-Dimensional Structure of Muscle Membranes Involved in the Regulation of Contraction in Skeletal-Muscle Fibers

1982 ◽  
pp. 221-230 ◽  
Author(s):  
Lee D. Peachey
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Skeletal Muscle Fibers ◽  
Regulation Of Contraction

scholarly journals Development of a human neuromuscular tissue-on-a-chip model on a 24-well-plate-format compartmentalized microfluidic device

Lab on a Chip ◽  
2021 ◽  
Author(s):  
Kazuki Yamamoto ◽  
Nao Yamaoka ◽  
Yu Imaizumi ◽  
Takunori Nagashima ◽  
Taiki Furutani ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Microfluidic Device ◽  
Motor Neurons ◽  
Muscle Fibers ◽  
Three Dimensional ◽  
Tissue Model ◽  
Skeletal Muscle Fibers

A three-dimensional human neuromuscular tissue model that mimics the physically separated structures of motor neurons and skeletal muscle fibers is presented.

scholarly journals Circuit Models of the Passive Electrical Properties of Frog Skeletal Muscle Fibers

1974 ◽  
Vol 63 (4) ◽  
pp. 432-459 ◽  
Author(s):  
R. Valdiosera ◽  
C. Clausen ◽  
R. S. Eisenberg
Keyword(s):  
Skeletal Muscle ◽  
Phase Angle ◽  
Muscle Fibers ◽  
Three Dimensional ◽  
Objective Measure ◽  
Electric Circuit ◽  
Field Equations ◽  
Low Frequencies ◽  
Cable Theory ◽  
Skeletal Muscle Fibers

The relation between the fine structure, electric field equations, and electric circuit models of skeletal muscle fibers is discussed. Experimental evidence illustrates the profound variation of potential with circumferential position, even at low frequencies (100 Hz). Since one-dimensional cable theory cannot account for such variation, three-dimensional cable theory must be used. Several circuit models of a sarcomere are presented and plots are made of the predicted phase angle between sinusoidal applied current and potential. The circuit models are described by equations involving normalized variables, since they affect the phase plot in a relatively simple way. A method is presented for estimating the values of the circuit elements and the standard deviation of the estimates. The reliability of the estimates is discussed. An objective measure of fit, Hamilton's R test, is used to test the significance of different fits to data. Finally, it is concluded that none of the proposed circuit models provides an adequate description of the observed variation of phase angle with circumferential location. It is not clear whether the source of disagreement is inadequate measurements or inadequate theory.

scholarly journals Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.

1996 ◽  
Vol 133 (3) ◽  
pp. 571-583 ◽  
Author(s):  
J P Schroeter ◽  
J P Bretaudiere ◽  
R L Sass ◽  
M A Goldstein
Keyword(s):  
Skeletal Muscle ◽  
Cross Sections ◽  
Three Dimensional ◽  
Square Lattice ◽  
Actin Binding ◽  
Dimensional Structure ◽  
Mammalian Skeletal Muscle ◽  
Axial Filament ◽  
Three Dimensional Structure ◽  
Dimensional Reconstruction

The three-dimensional structure of the vertebrate skeletal muscle Z band reflects its function as the muscle component essential for tension transmission between successive sarcomeres. We have investigated this structure as well as that of the nearby I band in a normal, unstimulated mammalian skeletal muscle by tomographic three-dimensional reconstruction from electron micrograph tilt series of sectioned tissue. The three-dimensional Z band structure consists of interdigitating axial filaments from opposite sarcomeres connected every 18 +/- 12 nm (mean +/- SD) to one to four cross-connecting Z-filaments are observed to meet the axial filaments in a fourfold symmetric arrangement. The substantial variation in the spacing between cross-connecting Z-filament to axial filament connection points suggests that the structure of the Z band is not determined solely by the arrangement of alpha-actinin to actin-binding sites along the axial filament. The cross-connecting filaments bind to or form a "relaxed interconnecting body" halfway between the axial filaments. This filamentous body is parallel to the Z band axial filaments and is observed to play an essential role in generating the small square lattice pattern seen in electron micrographs of unstimulated muscle cross sections. This structure is absent in cross section of the Z band from muscles fixed in rigor or in tetanus, suggesting that the Z band lattice must undergo dynamic rearrangement concomitant with crossbridge binding in the A band.

Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase

2017 ◽  
Vol 39 (3) ◽  
pp. 309-319
Author(s):  
Vu Van Dung ◽  
Yoshitaka Umetsu ◽  
Shinya Ohki
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Skeletal Muscle Myosin ◽  
Three Dimensional Structure ◽  
Calmodulin Binding ◽  
Muscle Myosin

In our previous study, functional ability and conformational stability had been examined for C-terminal deletion mutants of a 148-residue Ca2+-binding protein, chicken calmodulin (CaM). In that study, we had reported that a mutant named CCMΔ5, missing five residues at the C-terminus, activates CaM-target as much as full-length CaM does. This finding is intriguing because CCMΔ5 lacks the key residues, Met144 and Met145, for the target activation. To uncover why CCMΔ5 displays proper function, here we report the three-dimensional structure of CCMΔ5 bound to the peptide derived from skeletal muscle myosin light-chain kinase (skMLCK). The structure determination was achieved using multidimensional nuclear magnetic resonance (NMR) spectroscopy. The complex structure of CCM∆5-skMLCK was compared to that of wild CaM-skMLCK. The results showed that the orientation of helix-1 and helix-5 in CCM∆5 differs from those in wild CaM. Moreover, distinctive hydrophobic interaction manner was found in the binding between CCM∆5 and peptide; Phe141, Ala128, Met109, Leu105 and Phe92 of CCM∆5 contribute to the interaction with Trp4 of the skMLCK peptide.   Abbreviations: CaM, calmodulin; CCMΔX, a deletion mutant of CaM that lacks X C-terminal residues; NMR, Nuclear magnetic resonance; PDB, Protein date bank; skMLCK, skeletal muscle myosin light-chain kinase; TOF-MS, Time-of-flight mass spectrometry; RMSD, root mean square deviation; SDS-PAGE, Sodium dodecyl sulfate polyacrylamide gel electrophoresis Citation: Vu Van Dung, Umetsu Y., Ohki S., 2017. Three-dimensional structure of the complex between calmodulin mutant lacking the c-terminal five residues and the calmodulin-binding peptide derived from skeletal muscle myosin light-chain kinase. Tap chi Sinh hoc, 39(3): 309-319. DOI: 10.15625/0866-7160/v39n3.10111. *Corresponding author: [email protected] Received 19 June 2017, accepted 20 August 2017 

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