Role of O-GlcNAcylation in Central Nervous System Development and Injuries: A Systematic Review

Li Zhang1, Wanshan Bai1, Yaonan Peng1

  • 1Department of Neurosurgery, Jinling Hospital, School of Medicine, Nanjing University, Jiangsu Province, Nanjing, People's Republic of China.

Molecular Neurobiology
|February 17, 2024
PubMed

Insights

O-GlcNAcylation is crucial for central nervous system (CNS) development and injury recovery. Modulating O-GlcNAcylation offers therapeutic potential for CNS diseases and brain damage.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Central nervous system (CNS) development is vital for cognitive functions.
  • CNS injuries cause severe neurological dysfunction.
  • O-GlcNAcylation, a post-translational modification, regulates protein activity and stability.
  • O-GlcNAcylation interacts with other modifications like phosphorylation and ubiquitination.

Purpose of the Study:

  • To review the significant role of O-GlcNAcylation in CNS development.
  • To highlight O-GlcNAcylation's involvement in CNS injuries.
  • To explore O-GlcNAcylation as a therapeutic target for CNS diseases.

Main Methods:

  • Literature review of studies on O-GlcNAcylation in the CNS.
  • Analysis of O-GlcNAcylation's role in neurogenesis and neuronal function.
  • Examination of O-GlcNAcylation's impact on CNS injury outcomes.

Main Results:

  • O-GlcNAcylation is essential for neurogenesis, neuronal development, and function.
  • O-GlcNAcylation is implicated in CNS injuries like stroke and hemorrhage.
  • O-GlcNAcylation aids in mitigating brain damage by reducing inflammation and ER stress.

Conclusions:

  • O-GlcNAcylation plays a critical role in both CNS development and injury.
  • Interventions targeting O-GlcNAcylation show promise for treating CNS disorders.
  • Further research into O-GlcNAcylation could lead to novel therapeutic strategies for neurological conditions.

Related Concept Videos

Glial Cells01:04

Glial Cells

Overview
87.2K
Neurogenesis and Regeneration of Nervous Tissue01:15

Neurogenesis and Regeneration of Nervous Tissue

In the CNS, neurogenesis, the birth of new neurons from stem cells, is limited to the hippocampus in adults. In other regions of the brain and spinal cord, neurogenesis is almost non-existent due to inhibitory influences from neuroglia, especially oligodendrocytes, and the absence of growth-stimulating cues. The myelin produced by oligodendrocytes in the CNS inhibits neuronal regeneration. Furthermore, astrocytes proliferate rapidly after neuronal damage, forming scar tissue that physically...
784
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K
Nervous Tissue: Glial Cells01:31

Nervous Tissue: Glial Cells

Glia, or neuroglia, are vital support cells that assist neurons in their functions. The term "glia" originates from the Greek word for "glue," reflecting their role in holding the nervous system together. These cells can be categorized into six types: four in the central nervous system (CNS) and two in the peripheral nervous system (PNS).
The CNS glial cell includes the astrocytes, the oligodendrocytes, the microglia, and the ependymal cells.
Astrocytes are star-shaped glial...
3.0K
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
6.9K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
2.8K