siRNA knockdown of alanine aminopeptidase impairs myoblast proliferation and differentiation

A large number of intracellular proteins are degraded by the ubiquitin-proteasome system, one of the major protein degradation pathways. It produces peptides of several different sizes through protein degradation, and these peptides are rapidly degraded into free amino acids by various intracellular...

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Bibliographic Details
Published in:Experimental cell research 2020-12, Vol.397 (1), p.112337-112337, Article 112337
Main Authors: Osana, Shion, Kitajima, Yasuo, Suzuki, Naoki, Xu, Yidan, Murayama, Kazutaka, Nagatomi, Ryoichi
Format: Article
Language:English
Subjects:
Alanine-aminopeptidase
Animals
Apoptosis
CD13 Antigens - antagonists & inhibitors
CD13 Antigens - genetics
CD13 Antigens - metabolism
Cell Differentiation
Cell Proliferation
Cell-cycle
Mice
Myoblasts - enzymology
Myoblasts - pathology
Myogenesis
Myogenic-differentiation
RNA, Small Interfering - genetics
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Summary:A large number of intracellular proteins are degraded by the ubiquitin-proteasome system, one of the major protein degradation pathways. It produces peptides of several different sizes through protein degradation, and these peptides are rapidly degraded into free amino acids by various intracellular aminopeptidases. Previously, we reported that the activity of proteasomes and aminopeptidases in the proteolysis pathway are necessary for myoblast proliferation and differentiation. However, the detailed function of intracellular aminopeptidases in myoblast proliferation and differentiation has not yet been elucidated. In this study, we focused on alanine aminopeptidase (APN) and investigated the function of APN in C2C12 myoblast proliferation and differentiation. In myoblasts and myotubes, APN was mainly localized in the cell membrane as well as expressed at low levels in the cytoplasm and nucleus. The reduction of the APN enzymatic activity impaired the cell cycle progression in C2C12 myoblasts. In addition, apoptosis was induced after APN-knockdown. Finally, myogenic differentiation was also delayed in the APN-suppressed myoblasts. These findings indicate that APN is required for myoblast proliferation and differentiation.
ISSN:0014-4827
1090-2422
DOI:10.1016/j.yexcr.2020.112337