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Post-translational modifications and bronchopulmonary dysplasia

Kun Yang1, Ting He1, Xue Sun1

  • 1Department of Neonatology, Children's Medical Center, The Affiliated Hospital of Southwest Medical University, Luzhou, China.

Frontiers in Pediatrics
|January 20, 2025
PubMed

Insights

Protein post-translational modifications influence bronchopulmonary dysplasia (BPD) development. Understanding these modifications offers new therapeutic targets for this infant respiratory disorder.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neonatology

Background:

  • Bronchopulmonary dysplasia (BPD) is a major respiratory complication in premature infants.
  • Limited therapeutic options exist for BPD, necessitating a deeper understanding of its pathogenesis.
  • Protein post-translational modifications (PTMs) are crucial regulators of cellular functions and protein diversity.

Purpose of the Study:

  • To review the role of various PTMs in the molecular mechanisms of BPD.
  • To explore the connection between specific PTMs and BPD pathogenesis.
  • To identify potential therapeutic targets for BPD based on PTMs.

Main Methods:

  • Literature review focusing on PTMs and BPD.
  • Analysis of signaling pathways affected by PTMs in BPD.
  • Synthesis of current evidence linking PTMs to BPD progression.

Main Results:

  • PTMs like phosphorylation, acetylation, ubiquitination, SUMOylation, methylation, glycosylation, glycation, S-glutathionylation, and S-nitrosylation are linked to BPD.
  • These modifications contribute to BPD pathogenesis via complex signal transduction cascades.
  • Evidence suggests PTMs significantly impact cellular processes relevant to BPD.

Conclusions:

  • PTMs are integral to the molecular pathogenesis of bronchopulmonary dysplasia.
  • Targeting specific protein PTMs presents a promising avenue for novel BPD therapies.
  • Further research into PTMs could revolutionize the clinical management of BPD.

Keywords:
bronchopulmonary dysplasiahyperoxialung injurypost-translational modificationsubstrate protein

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