Plasticity in mammalian skeletal muscle

While it has been recognized for many years that different limb muscles belonging to the same mammal may have markedly differing contractile characteristics, it is only comparatively recently that it has been demonstrated that these differences depend upon the motor innervation. By appropriately changing the peripheral nerve innervating a mammalian skeletal muscle, it is possible to change dramatically the contractile behaviour of the reinnervated muscle. The manner by which the motor innervation determines the nature of a muscle fibre’s contractile machinery is not completely understood, but it appears that the number and pattern of motor nerve impulses reaching the muscle play an important role. The biochemical changes occurring within muscle fibres whose contractile properties have been modified by altered motor innervation include the synthesis of different contractile proteins.

2012 ◽  
Vol 521 (1-2) ◽  
pp. 1-9 ◽  
Author(s):  
Stanislava V. Avrova ◽  
Nikita A. Rysev ◽  
Oleg S. Matusovsky ◽  
Nikolay S. Shelud’ko ◽  
Yurii S. Borovikov

1999 ◽  
Vol 515 (3) ◽  
pp. 843-857 ◽  
Author(s):  
László Csernoch ◽  
Péter Szentesi ◽  
Sándor Sárközi ◽  
Csaba Szegedi ◽  
István Jona ◽  
...  

1996 ◽  
Vol 316 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Antonio CONTI ◽  
L. GORZA ◽  
Vincenzo SORRENTINO

Activation of intracellular Ca2+-release channels/ryanodine receptors (RyRs) is a fundamental step in the regulation of muscle contraction. In mammalian skeletal muscle, Ca2+-release channels containing the type 1 isoform of RyR (RyR1) open to release Ca2+ from the sarcoplasmic reticulum (SR) upon stimulation by the voltage-activated dihydropyridine receptor on the T-tubule/plasma membrane. In addition to RyR1, low levels of the mRNA of the RyR3 isoform have been recently detected in mammalian skeletal muscles. Here we report data on the distribution of the RyR3 gene product in mammalian skeletal muscles. Western-blot analysis of SR of individual muscles indicated that, at variance with the even distribution of the RyR1 isoform, the RyR3 content varies among different muscles, with relatively higher amounts being detected in diaphragm and soleus, and lower levels in abdominal muscles and tibialis anterior. In these muscles RyR3 was localized in the terminal cisternae of the SR. No detectable levels of RyR3 were observed in the extensor digitorum longus. Preferential high content of RyR3 in the diaphragm muscle was observed in several mammalian species. In situ hybridization analysis demonstrated that RyR3 transcripts are not restricted to a specific subset of skeletal-muscle fibres. Differential utilization of the RyR3 isoform in skeletal muscle may be relevant to the modulation of Ca2+ release with respect to specific muscle-contraction properties.


2002 ◽  
Vol 31 (5) ◽  
pp. 331-340 ◽  
Author(s):  
Dietmar Uttenweiler ◽  
Wolfgang Kirsch ◽  
Erich Schulzke ◽  
Martin Both ◽  
Rainer Fink

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