Journal of Applied Physiology AJP: Renal Physiology
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J Appl Physiol 92: 1465-1472, 2002; doi:10.1152/japplphysiol.00621.2001
8750-7587/02 $5.00
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Vol. 92, Issue 4, 1465-1472, April 2002

Passive tension of rat skeletal soleus muscle fibers: effects of unloading conditions

Thierry Toursel1, Laurence Stevens1, Henk Granzier2, and Yvonne Mounier1

1 Laboratoire de Plasticité Neuromusculaire, Université des Sciences et Technologies de Lille I, Bat SN4, F-59655 Villeneuve d'Ascq Cedex, France; and 2 Department of Veterinary and Comparative Anatomy, Pharmacology and Physiology, Washington State University, Pullman, Washington 99164

In this work we studied changes in passive elastic properties of rat soleus muscle fibers subjected to 14 days of hindlimb unloading (HU). For this purpose, we investigated the titin isoform expression in soleus muscles, passive tension-fiber strain relationships of single fibers, and the effects of the thick filament depolymerization on passive tension development. The myosin heavy chain composition was also measured for all fibers studied. Despite a slow-to-fast transformation of the soleus muscles on the basis of their myosin heavy chain content, no modification in the titin isoform expression was detected after 14 days of HU. However, the passive tension-fiber strain relationships revealed that passive tension of both slow and fast HU soleus fibers increased less steeply with sarcomere length than that of control fibers. Gel analysis suggested that this result could be explained by a decrease in the amount of titin in soleus muscle after HU. Furthermore, the thick filament depolymerization was found to similarly decrease passive tension in control and HU soleus fibers. Taken together, these results suggested that HU did not change titin isoform expression in the soleus muscle, but rather modified muscle stiffness by decreasing the amount of titin.

depolymerization; hindlimb unloading, myosin heavy chain; titin


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