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Journal of Biochemistry 2006 139(1):71-80; doi:10.1093/jb/mvj007
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© 2006 The Japanese Biochemical Society.

Regular Paper

A Proteomic Assessment of Muscle Contractile Alterations during Unloading and Reloading

Younguk Seo1, Kisoo Lee1, Kyoungsook Park2, Kiho Bae1 and Inho Choi1,*

1 Department of Life Science, College of Liberal Arts and Science, Yonsei University, Wonju, 220-710, Republic of Korea,; and 2 Molecular Therapy Research Center, Sungkyunkwan University, Seoul, 135-710, Republic of Korea

* To whom correspondence should be addressed. Tel: +82-33-760-2244, Fax: +82-33-760-2183, E-mail: ichoi{at}dragon.yonsei.ac.kr

Unloading of skeletal muscle causes atrophy and altered contractility. To identify major muscle proteins responding significantly to the altered loading and to elucidate how the contractile alterations reflect potential proteomic modifications, we examined protein expression in the rat soleus muscle during 3-week hindlimb suspension and 2-week reloading. Compared with unsuspended controls, experimental animals had a 0.5- to 0.6-fold decrease in tension during unloading and early reloading, comparable to 0.2- to 0.6-fold decreases in the protein levels of myosin light chain 1 (MLC1), {alpha}-actin, tropomyosin ß-chain, and troponins T1 and T2. The observed 1.4- to 1.6-fold increase in shortening velocity appears to reflect 1.2- to 9.0-fold increases in the protein levels of fast-type MLC2, glycolytic enzymes, and creatine kinase, and 0.2- to 0.3-fold decreases in slow-type troponins T1 and T2. The levels of three heat shock proteins (p20, alpha crystallin B chain, and HSP90) decreased during unloading but returned to control levels during reloading. These results imply that proteomic responses to unloading change overall myofibrillar integrity and metabolic regulation, resulting in altered contractility.


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