Abstract
Oocyte meiotic maturation and embryogenesis are some of the most important physiological processes that occur in organisms, playing crucial roles in the preservation of life in all species. The post-transcriptional regulation of maternal messenger ribonucleic acids (mRNAs) and the post-translational regulation of proteins are critical in the control of oocyte maturation and early embryogenesis. Translational control affects the basic mechanism of protein synthesis, thus, knowledge of the key components included in this machinery is required in order to understand its regulation. Cytoplasmic polyadenylation element binding proteins (CPEBs) bind to the 3′-end of mRNAs to regulate their localization and translation and are necessary for proper development. In this study we examined the expression pattern of cytoplasmic polyadenylation element binding protein 2 (CPEB2) both on the mRNA (by real-time quantitative reverse transcription polymerase chain reaction, qRT-PCR) and protein (by Western blotting, WB) level, as well as its localization during the meiotic maturation of porcine oocytes and early embryonic development by immunocytochemistry (ICC). For the elucidation of its functions, CPEB2 knockdown by double-strand RNA (dsRNA) was used. We discovered that CPEB2 is expressed during all stages of porcine meiotic maturation and embryonic development. Moreover, we found that it is necessary to enable a high percentage of oocytes to reach the metaphase II (MII) stage, as well as for the production of good-quality parthenogenetic blastocysts.
Highlights
The meiotic maturation of female germ cells, known as oocytes, is characterized by the virtual absence of transcription
To extend the knowledge of the roles that Cytoplasmic polyadenylation element binding proteins (CPEBs)-related proteins play in reproduction, we focused on the expression and function of cytoplasmic polyadenylation element binding protein 2 (CPEB2) during porcine meiotic maturation and early embryonic development
We have described the expression of CPEB2 at both messenger ribonucleic acids (mRNAs) and protein levels, as well as its localization during the meiotic maturation of porcine oocytes and during early embryogenesis
Summary
The meiotic maturation of female germ cells, known as oocytes, is characterized by the virtual absence of transcription. The accumulation of all the necessary RNAs during oocyte growth is crucial for proper meiotic maturation and early embryonic development. Translational regulation is partly controlled by changes in mRNA poly(A) tail length. Translational regulation through cytoplasmic polyadenylation and deadenylation is essential for the meiotic maturation of oocytes. The sequential waves of polyadenylation and deadenylation drive the meiotic progression forward, preventing the incorrect timing of specific protein translation during particular maturation phases in oocytes. Default deadenylation in maturing oocytes could be a means to liberate components of the translation apparatus for the synthesis of meiosis-specific proteins [1,2,3,4,5,6,7,8]
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