scholarly journals Inhibitory Effect of Different Durations of Intermittent Stretching on Muscle Disuse Atrophy in Different Regions of the Rat Soleus Muscle

2017 ◽  
Vol 32 (2) ◽  
pp. 291-296
Author(s):  
Shigefumi KIMURA ◽  
Takuma ISHIKAWA ◽  
Toshiaki YAMAZAKI
2017 ◽  
Vol 32 (2) ◽  
pp. 165-170
Author(s):  
Azusa KUBO ◽  
Katsuya UENO ◽  
Ryo MIYACHI ◽  
Toshiaki YAMAZAKI

2009 ◽  
Vol 12 (1) ◽  
pp. 13-19
Author(s):  
Toshiaki Yamazaki ◽  
Masami Yokogawa ◽  
Katsuhiko Tachino

2019 ◽  
Vol 34 (1) ◽  
pp. 13-16
Author(s):  
Hirotaka TANIGUCHI ◽  
Kazumi ZUSHI ◽  
Toshiaki YAMAZAKI

2007 ◽  
Vol 292 (5) ◽  
pp. C1723-C1731 ◽  
Author(s):  
Marianne Vermaelen ◽  
Pascal Sirvent ◽  
Fabrice Raynaud ◽  
Catherine Astier ◽  
Jacques Mercier ◽  
...  

Calpains have been proposed to be involved in the cytoskeletal remodeling and wasting of skeletal muscle. However, limited data are available about the specific involvement of each calpain in the early stages of muscle atrophy. The aims of this study were to determine whether calpains 1 and 2 are autolyzed after a short period of muscle disuse, and, if so, where in the myofibers the autolyzed products are localized. In the rat soleus muscle, 5 days of immobilization increased autolyzed calpain 1 in the particulate and not the soluble fraction. Conversely, autolyzed calpain 2 was not found in the particulate fraction, whereas it was increased in the soluble fraction after immobilization. In the less atrophied plantaris muscle, no difference was noted between the control and immobilized groups whatever the fraction or calpain. Other proteolytic pathways were also investigated. The ubiquitin-proteasome pathway was activated in both skeletal muscles, and caspase 3 was activated only in the soleus muscle. Taken together, our data suggest that calpains 1 and 2 are involved in atrophy development in slow type muscle exclusively and that they have different regulation and protein targets. Moreover, the activation of proteolytic pathways appears to differ in slow and fast muscles, and the proteolytic mechanisms involved in fast-type muscle atrophy remain unclear.


1994 ◽  
Vol 302 (3) ◽  
pp. 745-751 ◽  
Author(s):  
I Dørup ◽  
T Clausen

For technical reasons, 86Rb is frequently preferred to 42K as a tracer for K+. Systematic comparisons of the two isotopes, however, are rarely done. In this paper we compare the transport of 42K and 86Rb in rat and mouse soleus muscle and in rat erythrocytes. Ouabain-suppressible K+ uptake in rat soleus was the same whether measured with 42K or 86Rb, both when stimulated by insulin, salbutamol and calcitonin-gene-related peptide (CGRP), and when inhibited by graded concentrations of ouabain. Control experiments with rat erythrocytes, where Na(+)-K(+)-Cl- co-transport has earlier been demonstrated, showed closely similar inhibitory effects of bumetanide on 42K and 86Rb uptake. In contrast, bumetanide produced no significant change in 42K uptake of rat and mouse soleus muscle, but clearly inhibited 86Rb uptake at concentrations down to 10(-7) M (P < 0.001). Whereas the addition of 150 mM NaCl had no effect on 42K uptake in rat soleus, 86Rb uptake, and in particular the bumetanide-suppressible component, was markedly increased by this addition. The inhibitory effect of bumetanide on 86Rb uptake gives rise to the false impression that skeletal muscle contains a NaKCl2 co-transport system. Efflux studies showed that the fractional loss of 42K from rat soleus muscle is 2.3 times larger than that of 86Rb. Salbutamol and CGRP increased 86Rb efflux, but inhibited 42K efflux. This implies that for studies of K+ efflux and bumetanide-sensitive K+ transport, 86Rb is not even an acceptable tracer for the detection of qualitative changes. Control experiments with 42K are essential in any characterization of unknown K+ transport processes.


1998 ◽  
Vol 1 (1) ◽  
pp. 19-24 ◽  
Author(s):  
Toshiaki Yamazaki ◽  
Nobuhide Haida ◽  
Katsuhiko Tachino

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