1. Academic Validation
  2. The acetylome of adult mouse sciatic nerve

The acetylome of adult mouse sciatic nerve

  • J Neurochem. 2022 Aug;162(3):262-275. doi: 10.1111/jnc.15648.
Mi Shen 1 Zixin Chen 2 Mengru Ming 1 Zhenghui Cheng 1 Junjie Sun 1 Qingyun Liang 1 Tongxin Shang 1 Qi Zhang 1 Songlin Zhou 1 Yuhua Ji 1 2 Fei Ding 1
Affiliations

Affiliations

  • 1 Key Laboratory of Neuroregeneration of Jiangsu and Ministry of Education, Co-innovation Center of Neuroregeneration, NMPA Key Laboratory for Research and Evaluation of Tissue Engineering Technology Products, Jiangsu Clinical Medicine Center of Tissue Engineering and Nerve Injury Repair, Nantong University, Nantong, China.
  • 2 Department of Immunology, College of Life science and Technology, Jinan University, Guangzhou, China.
Abstract

Lysine acetylation is a reversible post-translational modification (PTM) involved in multiple physiological functions. Recent studies have demonstrated the involvement of protein acetylation in modulating the biology of Schwann cells (SCs) and regeneration of the peripheral nervous system (PNS). However, the mechanisms underlying these processes remain partially understood. Here, we characterized the acetylome of the mouse sciatic nerve (SN) and investigated the cellular distribution of acetylated proteins. We identified 483 acetylated proteins containing 1442 acetylation modification sites in the SN of adult C57BL/6 mice. Bioinformatics suggested that these acetylated SN proteins were mainly located in the myelin sheath, mitochondrial inner membrane, and Cytoskeleton, and highlighted the significant differences between the mouse SN and brain acetylome. Manual annotation further indicated that most acetylated proteins (> 45%) were associated with mitochondria, energy metabolism, and Cytoskeleton and cell adhesion. We verified three newly discovered acetylation-modified proteins, including neurofilament LIGHT polypeptide (NEFL), neurofilament medium/high polypeptide (NFM/H), and periaxin (PRX). Immunofluorescence illustrated that the acetylated proteins, including acetylated alpha-tubulin, were mainly co-localized with S100-positive SCs. Herein, we provided a comprehensive acetylome for the mouse SN and demonstrated that acetylated proteins in the SN were predominantly located in SCs. These results will extend our understanding and promote further study of the role and mechanism of protein acetylation in SC development and PNS regeneration.

Keywords

PNS regeneration; Schwann cells; acetylome; mouse; peripheral nervous system; sciatic nerve.

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