De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

Dana Chuderland, Zeev Dvashi, Ruth Kaplan-Kraicer, Daniella Ben-Meir, Ruth Shalgi*, Sara Lavi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Oocyte maturation in mammals is a multiple-stage process that generates fertilizable oocytes. Ovarian oocytes are arrested at prophase of the first meiotic division characterized by the presence of a germinal vesicle. Towards ovulation, the oocytes resume meiosis and proceed to the second metaphase in a process known as maturation; they undergo nuclear and cytoplasmic changes that are accompanied by translation and degradation of mRNA. Protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A), which belongs to the metal-dependent serine/threonine protein phosphatase family, is highly conserved during evolution. PPM1A plays a significant role in many cellular functions such as cell cycle progression, apoptosis and cellular differentiation. It works through diverse signaling pathways, including p38 MAP kinase JNK and transforming growth factor beta (TGF-β). Herein we report that PPM1A is expressed in mouse oocytes and that its mRNA level rises during oocyte maturation. Using quantitative real-time polymerase chain reaction (qPCR) and western blot analysis, we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A protein. Since PPM1A function is mainly affected by its level, we propose that it might have an important role in oocyte maturation.

Original languageEnglish
Pages (from-to)433-445
Number of pages13
JournalCellular and Molecular Biology Letters
Issue number3
StatePublished - Sep 2012


  • GV
  • MII
  • Maturation
  • Oocyte
  • Ovary
  • P38-MAPK
  • PPM1A
  • Phosphatase
  • Signal transduction
  • Transcription


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