Laurila A L, Jeffery S, Savolainen J, Takala T E, Carter N D, Väänänen H K
Department of Pathology, University of Oulu, Finland.
J Histochem Cytochem. 1991 May;39(5):617-24. doi: 10.1177/39.5.1901877.
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.
在大鼠后肢踝关节处于跖屈或背屈状态下进行石膏固定期间,对I型肌纤维中的主要可溶性蛋白碳酸酐酶III(CA III)的含量及纤维分布进行了研究。在为期3周的固定期内,缩短的和拉长的胫前肌中CA III的浓度分别增加了两倍(p<0.05)和三倍(p<0.01)。固定6周后,增加幅度更大(p<0.001)。同时,拉长肌肉中CA III阳性纤维的数量增加,以至于几乎所有纤维均呈阳性。比目鱼肌中CA III浓度未见显著变化。基于肌动球蛋白ATP酶染色,胫前肌中IIb型纤维向IIa型转变,而比目鱼肌中I型纤维向IIa型纤维转变。因此,肌肉中CA III浓度的增加似乎与肌肉向更具氧化型的细胞转变有关。