Dynamic acetylation profile during mammalian neurulation

Birth Defects Res. 2020 Jan 15;112(2):205-211. doi: 10.1002/bdr2.1618. Epub 2019 Nov 23.

Abstract

Background: Neural tube defects (NTDs) result from failure of neural tube closure during embryogenesis. These severe birth defects of the central nervous system include anencephaly and spina bifida, and affect 0.5-2 per 1,000 pregnancies worldwide in humans. It has been demonstrated that acetylation plays a pivotal role during neural tube closure, as animal models for defective histone acetyltransferase proteins display NTDs. Acetylation represents an important component of the complex network of posttranslational regulatory interactions, suggesting a possible fundamental role during primary neurulation events. This study aimed to assess protein acetylation contribution to early patterning of the central nervous system both in human and murine specimens.

Methods: We used both human and mouse (Cited2 -/- ) samples to analyze the dynamic acetylation of proteins during embryo development through immunohistochemistry, western blot analysis and quantitative polymerase chain reaction.

Results: We report the dynamic profile of histone and protein acetylation status during neural tube closure. We also report a rescue effect in an animal model by chemical p53 inhibition.

Conclusions: Our data suggest that the p53-acetylation equilibrium may play a role in primary neurulation in mammals.

Keywords: Cited2; acetylation profile; neural tube defects; neurodevelopment; p53.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Anencephaly / etiology
  • Anencephaly / physiopathology
  • Animals
  • Disease Models, Animal
  • Embryonic Development / genetics
  • Embryonic Development / physiology
  • Histone Acetyltransferases / metabolism
  • Humans
  • Mammals
  • Mice / embryology
  • Neural Tube Defects / embryology*
  • Neurulation / genetics*
  • Neurulation / physiology
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism
  • Spinal Dysraphism / etiology
  • Spinal Dysraphism / physiopathology
  • Trans-Activators / genetics
  • Trans-Activators / metabolism
  • Transcription Factors
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Cited2 protein, mouse
  • Repressor Proteins
  • Trans-Activators
  • Transcription Factors
  • Tumor Suppressor Protein p53
  • Histone Acetyltransferases