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Role of peptidylarginine deiminase 4 (PAD4) in pig parthenogenetic preimplantation embryonic development

Published online by Cambridge University Press:  13 July 2012

Manjula Brahmajosyula  and
Masashi Miyake
Manjula Brahmajosyula
Affiliation:
Department of Bioresource Science, Graduate School of Agricultural Science, Kobe University, 1–1 Rokkodai-cho, Nada-ku, Kobe 657–8501, Japan.
Masashi Miyake*
Affiliation:
Department of Bioresource Science, Graduate School of Agricultural Science, Kobe University, 1–1 Rokkodai-cho, Nada-ku, Kobe 657–8501, Japan. Organization of Advanced Science and Technology, Kobe University, 1–1 Rokkodai-cho, Nada-ku, Kobe 657–8501, Japan.
*
All correspondence to: Masashi Miyake. Department of Bioresource Science, Graduate School of Agricultural Science, Kobe University, 1–1 Rokkodai-cho, Nada-ku, Kobe 657–8501, Japan. Tel: +81 78 803 5807. Fax: +81 78 803 6581. e-mail: miyake@kobe-u.ac.jp
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Summary

Arginine modification to citrulline (citrullination) is catalyzed by peptidylarginine deiminases (PADs) and one of the isomers PAD4 is shown to be involved in the gene regulation. In our previous paper we studied the localization and expression of PAD4 and the target of PAD4 in mammalian gametes and preimplantation embryos. In this study the role of PAD4 was examined in the pig diploid parthenogenetic preimplantation embryonic development. Knockdown of PAD4 by RNAi resulted in delayed development. Inhibition of PAD4 by a potent PAD4 inhibitor Cl-amidine from the time of activation for 24 h resulted in developmental arrest at the first cleavage. Inhibition at the later stages of development resulted in delayed or arrested development. A shorter exposure to Cl-amidine for 6 h at any stage of growth resulted in slow development. Thus, this study suggests that PAD4 activity is essential for the normal development of the embryos.

Keywords

DevelopmentPAD4PreimplantationPig parthenotesRNAi
Type
Research Article
Information
Zygote , Volume 21 , Issue 4 , November 2013 , pp. 385 - 393
Copyright
Copyright © Cambridge University Press 2012 

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