scholarly journals Architectural properties of the neuromuscular compartments in selected forearm skeletal muscles

2014 ◽  
Vol 225 (1) ◽  
pp. 12-18 ◽  
Author(s):  
An-Tang Liu ◽  
Ben-Li Liu ◽  
Li-Xuan Lu ◽  
Gang Chen ◽  
Da-Zhi Yu ◽  
...  
1986 ◽  
Vol 64 (4) ◽  
pp. 495-498 ◽  
Author(s):  
Marc D. Binder

Results from a wide variety of recent studies on the architecture and innervation of skeletal muscles, the neuromechanical characteristics of motor units, and the properties and spinal reflex actions of muscle proprioceptors present a number of challenges to conventional views of the functional organization of the segmental motor system. To illustrate the nature of these challenges, studies directed toward several specific issues are reviewed. These include the functional subdivision of single muscles into two or more neuromuscular compartments; the patterns of synaptic input from peripheral afferent fibers to motoneurons innervating muscle units of different "type;" and the convergence in the segmental reflex pathways from muscle spindles and tendon organs to motoneurons.


Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.


Author(s):  
F.T. Llados ◽  
V. Krlho ◽  
G.D. Pappas

It Is known that Ca++ enters the muscle fiber at the junctional area during the action of the neurotransmitter, acetylcholine (ACh). Pappas and Rose demonstrated that following Intense stimulation, calcium deposits are found In the postsynaptic muscle membrane, Indicating the existence of calcium uptake In the postsynaptic area following ACh release. In addition to this calcium uptake, when mammal Ian skeletal muscles are exposed to a sustained action of the neurotransmitter, muscle damage develops. These same effects, l.e., Increased transmitter release, calcium uptake and finally muscle damage, can be obtained by Incubating the muscle with lonophore A23178.


1993 ◽  
Vol 5 (2) ◽  
pp. 137-146
Author(s):  
Seiichiro INOKUCHI ◽  
Tadanao KIMURA ◽  
Masataka SUZUKI ◽  
Junji ITO ◽  
Hiroo KUMAKURA

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 2482-PUB
Author(s):  
JIDONG LIU ◽  
ZHENG SUN

Diabetes ◽  
1987 ◽  
Vol 36 (7) ◽  
pp. 842-848 ◽  
Author(s):  
K. Kjeldsen ◽  
H. Braendgaard ◽  
P. Sidenius ◽  
J. S. Larsen ◽  
A. Norgaard

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