ASGSB 2003 Annual Meeting Abstracts


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PROTEIN EXPRESSION PROFILING OF THE RAT ANTIGRAVITY MUSCLE DURING HINDLIMB UNLOADING. Y. Seo, J. Park, K. Park and I. Choi. Department of Life Science, College of Liberal Arts and Science, Yonsei University, Republic of Korea.

   To analyze protein expression profiling in an antigravity muscle during unloading, we conducted 2D electrophoresis using the rat soleus muscle after 1-wk and 3-wk hindlimb suspension. Sample proteins were resolved on a 24 cm dry strip (pH 3 - 10) using IPGphor Isoelectric Focusing system. Compared to the age-matched controls, the relative level of beta-enolase (a glycolytic enzyme) increased 3.45- and 2.84-fold in 1-wk and 3-wk unloading, respectively, whereas the level of cytochrome c oxidase (an oxidative enzyme) decreased 0.18- and 0.13-fold in each respective period. The relative expression level of myosin light chain did not change significantly. In contrast, the actin level decreased 0.81- to 0.82-fold during unloading. In addition, the level of alpha B crystalline (probably associated with actin filaments) decreased 0.78- and 0.36-fold, but that of tropomyosin increased 1.3- and 1.6-fold during the two unloading periods, respectively. Our results suggest that antigravity muscle expresses relatively more anaerobic proteins, and that actin contractile filaments are more susceptible to loss during unloading.

(Supported by KOSEF R05-2003-000-10589-0 to I. Choi.)

 

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