The Protein Acetylation after Traumatic Spinal Cord Injury: Mechanisms and Therapeutic Opportunities

Spinal cord injury (SCI) results in loss of normal functions with limited recovery. Protein acetylation following SCI is important and influences spinal cord plasticity, axon growth, and sensory nerve regeneration. This review explores the role of histone and non-histone protein acetylation in nerve growth and axon regeneration post-SCI. Acetylation is controlled by enzymes: lysine acetyltransferases (KATs) add acetyl groups, while lysine deacetylases (KDACs) remove them. These enzymes, including αTAT1, HDAC6, and SIRT2, are potential therapeutic targets to aid SCI recovery. A comprehensive understanding of protein acetylation and deacetylation after SCI could lead to new treatments. Therapies targeting these processes may help improve neuronal repair and reduce pain caused by SCI.

• 1
  Histone acetylation influences neural plasticity, synaptogenesis, and synaptic plasticity, impacting tissue remodeling post-SCI. Specifically, H4 acetylation levels are time-related and affect glial fibrillary acidic protein levels.
• 2
  Non-histone proteins, including α-tubulin, HSP90, and p53, are acetylated, playing crucial roles in axon regeneration and neuron differentiation. These modifications influence protein interactions, distribution, stability, and activity.
• 3
  HDAC inhibitors show promise in neuroprotection and anti-inflammation in the CNS, potentially promoting functional recovery after SCI by targeting HDAC1, HDAC3, and HDAC6.