Abstract
The amount and fiber distribution of carbonic anhydrase III (CA III), a major soluble protein in Type I muscle fibers, were studied during cast immobilization of rat hindlimb with the ankle in plantar or dorsiflexion. The concentration of CA III increased two- (p less than 0.05) and three- (p less than 0.01) fold in the shortened and lengthened tibialis anterior muscle during a 3-weeks immobilization period, respectively. After 6 weeks of immobilization the increase was even greater (p less than 0.001). Concomitantly, the number of CA III positive fibers in the lengthened muscle increased so that almost all fibers were positive. In the soleus muscle no significant change in the CA III concentration was seen. On the basis of actomyosin ATPase staining, the transition of Type IIb fibers towards Type IIa occurred in the tibialis anterior muscle, whereas in the soleus muscle a transformation of Type I fibers towards Type IIa fibers occurred. Therefore, the increase in the muscle CA III concentration seems to be associated with a cell transformation of the muscle towards a more oxidative type.