USP7 reduction leads to developmental failure of mouse early embryos

Exp Cell Res. 2023 Jun 15;427(2):113605. doi: 10.1016/j.yexcr.2023.113605. Epub 2023 Apr 18.

Abstract

As a member of Ubiquitin-specific protease subfamily, ubiquitin specific protease 7 (USP7) has been reported to participate in a variety of cellular processes, including cell cycle, apoptosis, DNA damage response, and epigenetic modification. However, its function in preimplantation embryos is still obscure. To investigate the functions of USP7 during preimplantation embryo development, we used siRNA to degrade endogenous USP7 messenger RNA. We found that USP7 knockdown significantly decreased the development rate of mouse early embryos. Moreover, depletion of USP7 induced the accumulation of the DNA lesions and apoptotic blastomeres in early embryos. In addition, USP7 knockdown caused an abnormal H3K27me3 modification in 2-cell embryos. Overall, our results indicate that USP7 maintains genome stability perhaps via regulating H3K27me3 and DNA damage, consequently controlling the embryo quality.

Keywords: Apoptosis; DNA damage; Embryo; USP7.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • DNA Damage / genetics
  • Histones* / genetics
  • Mice
  • Ubiquitin Thiolesterase* / genetics
  • Ubiquitin Thiolesterase* / metabolism
  • Ubiquitin-Specific Peptidase 7 / genetics
  • Ubiquitin-Specific Peptidase 7 / metabolism
  • Ubiquitin-Specific Proteases / genetics

Substances

  • Ubiquitin-Specific Peptidase 7
  • Histones
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Proteases