Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8644398 | Gene | 2018 | 31 Pages |
Abstract
Skeletal muscle atrophy results from fasting, disuse and other systemic diseases. Muscle atrophy is associated with increased muscle protein degradation via the Ubiquitin proteasome system (UPS). The Ubiquitin Specific Proteases (USPs), also known as deubiquitinating enzymes, regulates a wide variety of cellular processes in skeletal muscle. In our study, among the 41 members of the USP family identified in the skeletal muscle transcriptome of Chinese perch, 24 USPs were differentially expressed between the fast and slow muscle fibers. The expressional profile of 4 muscle-related USPs (USP10, USP14, USP19, USP45) was investigated in the fast and slow muscle in response to fasting at 4 and 7â¯days. The results showed that the expression of USP10, USP14 and USP19 was significantly increased in the fast muscle after fasting for 4â¯days and 7â¯days. But only the USP10 and USP14 had significantly increased at 7â¯days of fasting in the slow muscle. The expression of MAFbx and MuRF1 up-regulated and major myofibrillar genes down-regulated, indicating that all of these four USPs are involved in the protein degradation of the fast and slow muscle.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Genetics
Authors
FangLiang Zhang, YuLong Li, Lin Chen, Jia Cheng, Ping Wu, WuYing Chu, JianShe Zhang,