期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 634, 期 -, 页码 40-47出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2022.09.113
关键词
Proteasome; Proteolysis; Aminopeptidase; Myoblast; Amino acid
资金
- Japan Society for the Promotion of Science (JSPS) KAKENHI [JP20K19478, JP21H04857]
- Nakatomi Foundation, Japan
- Sumitomo Foundation, Japan
- [22J00078]
The proteasome and aminopeptidases are thought to be involved in protein synthesis through intracellular energy production by recycled-amino acid metabolism, thereby maintaining myoblast integrity.
Myoblast integrity is essential for skeletal muscle regeneration. Many intracellular proteins are degraded by the proteasome and converted to amino acids by aminopeptidases through the protein degradation pathway. Although we previously reported its importance for myoblast integrity, the involved mecha-nism remains unclear. In this study, we focused on the reusability of proteolytic products to elucidate the regulatory mechanism of protein synthesis mediated by the proteasome and aminopeptidases. Protea-some inhibition decreased protein synthesis, but recycled-amino acids derived from proteasomal pro-teolysis were not reused for de novo protein synthesis in C2C12 myoblasts. On the other hand, proteasome and aminopeptidase inhibition decreased intracellular ATP levels in C2C12 myoblasts. Therefore, it was indicated that amino acids produced by these proteolytic systems may be reutilized for ATP production through its metabolism, not for de novo protein synthesis. These findings suggested the proteasome and aminopeptidases are thought to be involved in protein synthesis through intracellular energy production by recycled-amino acid metabolism, thereby maintaining myoblast integrity.(c) 2022 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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