Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes

Endo, Toshihiko; Naito, Kunihiko; Kume, Sachi; Nishimura, Yukio; Kashima, Koji; Tojo, Hideaki

doi:10.1530/rep.1.00924

Cited by 16 publications

(15 citation statements)

References 39 publications

(59 reference statements)

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“…MPF is responsible for many aspects of oocyte maturation, including GVBD [32]. In the current study, the levels of phosphorylated MAPK and MPF activity corresponded to the proportion of oocytes at GVBD stage.…”

Section: Discussionsupporting

confidence: 49%

Zinc Regulates Meiotic Resumption in Porcine Oocytes via a Protein Kinase C-Related Pathway

et al. 2014

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Zinc is an extremely important trace element that plays important roles in several biological processes. However, the function of zinc in meiotic division of porcine oocytes is unknown. In this study, we investigated the role of zinc during meiotic resumption in in vitro matured porcine oocytes. During meiotic division, a massive release of zinc was observed. The level of free zinc in the cytoplasm significantly increased during maturation. Depletion of zinc using N, N, N′, N′-tetrakis (2-pyridylmethyl) ethylenediamine (TPEN), a Zn2+ chelator, blocked meiotic resumption in a dose dependent manner. The level of phosphorylated mitogen activated protein kinase (MAPK) and p34cdc2 kinase activity were reduced when zinc was depleted. Moreover, zinc depletion reduced the levels of phosphorylated protein kinase C (PKC) substrates in a dose dependent manner. Real-time PCR analysis showed that expression of the MAPK- and maturation promoting factor related genes C-mos, CyclinB1, and Cdc2 was downregulated following zinc depletion. Treatment with the PKC agonist phorbol 12-myristate 13-acetate (PMA) increased phosphorylation of PKC substrates and MAPK and increased p34cdc2 kinase activity. This rescued the meiotic arrest, even in the presence of TPEN. Activation of PKC by PMA increased the level of zinc in the cytoplasm. These data demonstrate that zinc is required for meiotic resumption in porcine oocytes, and this appears to be regulated via a PKC related pathway.

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Section: Discussionsupporting

confidence: 49%

Zinc Regulates Meiotic Resumption in Porcine Oocytes via a Protein Kinase C-Related Pathway

et al. 2014

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“…Based on our results, H4/K5 deacetylation may not be required for progression through these stages, since TSAtreated oocytes were able to undergo GVBD with acetylated H4/K5. In pig [6,15,23] and mouse [13] oocytes, acetylation of H4/K5 is obvious from the GV to L-GV stage. This discrepancy may be associated with a species difference.…”

Section: Discussionmentioning

confidence: 96%

Dynamic Changes in Histone Acetylation During Sheep Oocyte Maturation

Tang

Wang

Xiong

et al. 2007

Journal of Reproduction and Development

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Abstract. The changes in histone acetylation are not always consistent in various cell types and at different developmental stages. We immunostained specific antibodies against acetylated lysine 9 of histone H3 and acetylated lysines 5 and 12 of histone H4 in an effort to understand the detailed changes in histone acetylation during sheep oocyte meiosis. We found that the acetylation fluorescence signals of H3/K9 and H4/K12 on chromatin appeared intensively in the germinal vesicle (GV), late-GV (L-GV), and germinal vesicle breakdown (GVBD) stages and became weak in metaphase I (MI); however staining reappeared in anaphase I-telophase-I (AI-TI) and metaphase II (MII). Furthermore, staining was detected in the first polar bodies. The fluorescence signals of H4/K5 first appeared in the MI stage and became intensive in the AI-TI stage; however they were barely detectable in MII stage chromosomes and first polar bodies. We conclude that the acetylation patterns of H3/K9 and H4/K12 during oocyte meiotic maturation are similar and that the pattern of H4/K5 is unique. Key words: Histone acetylation, Meiotic maturation, Sheep oocyte, Trichostain A (J. Reprod. Dev. 53: [555][556][557][558][559][560][561] 2007) h e b a s i c s t r u c t u r a l u n i t o f e u k a r y o t i c chromosomes is a DNA protein complex called the nucleosome that consists of 147 base pairs of DNA wrapped around an octamer of the H2A, H2B, H3, and H4 histone proteins. The nucleosome histones are thought to play important roles in various cellular functions. It is well known that post-translational acetylation, methylation, phosphorylation, and ubiquitination of histones play an intrinsic role in transcription regulation [1,2]. In these post-translational modifications, h i s t o n e a c e t y l a t i o n a f f e c t s c h r o m a t i o n conformation [3], correlates with gene activity [4,5], and is required for orderly meiosis [6]. The Nterminal tails of histone H3 and H4 have a critical role in the folding of higher order chromatin structure [7][8][9]. The different effects of histone acetylaion on chromatin organization have been analyzed both in vitro and in vivo [10,11] and in mitosis and in meiosis [12]. Recent results show that the acetylation of different lysines of histone is associated with a diversity of chromatin-related processes in mitosis [13] and is necessary for orderly meiosis [6]. The lysine residue-specific changes in histone acetylation during pig oocyte meiosis have distinctive characteristics [6,15] compared with those of mouse oocytes [14].In the present study, we investigated the changes in acetylation of lysine K9 of histone H3, and lysine K5, K12 of histone H4 in sheep oocytes at different stages of maturation.

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“…In agreement with this proposal, a previous study using porcine oocytes showed that global histone deacetylation induced by HDACs is correlated with mixing of nuclear contents and cytoplasmic factors following GVBD. 72,73 Thus, HDAC2 activity during oocyte maturation may be regulated by cytoplasmic factors or factors only expressed/degraded after GVBD, which activate HDAC2 or form a complex with HDAC2 and mediate HDAC2's ability to bind chromatin; HDACs lack a DNA-binding domain and execute their function by being a component of repressor complexes. 74,75 A recent study provided strong evidence to support this notion.…”

Section: Hdac2 Regulates Chromosome Segregation and Kinetochore Functmentioning

confidence: 99%

HDAC1 and HDAC2 in mouse oocytes and preimplantation embryos: Specificity versus compensation

Schultz

2016

Cell Death Differ

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Oocyte and preimplantation embryo development entail dynamic changes in chromatin structure and gene expression, which are regulated by a number of maternal and zygotic epigenetic factors. Histone deacetylases (HDACs), which tighten chromatin structure, repress transcription and gene expression by removing acetyl groups from histone or non-histone proteins. HDAC1 and HDAC2 are two highly homologous Class I HDACs and display compensatory or specific roles in different cell types or in response to different stimuli and signaling pathways. We summarize here the current knowledge about the functions of HDAC1 and HDAC2 in regulating histone modifications, transcription, DNA methylation, chromosome segregation, and cell cycle during oocyte and preimplantation embryo development. What emerges from these studies is that although HDAC1 and HDAC2 are highly homologous, HDAC2 is more critical than HDAC1 for oocyte development and reciprocally, HDAC1 is more critical than HDAC2 for preimplantation development. In eukaryotes, DNA is organized into a highly ordered nucleoprotein assembly called chromatin, whose fundamental unit is the nucleosome. The nucleosome consists of 146 bp of DNA wrapped around a histone core comprised of two molecules each of histones H2A, H2B, H3 and H4. Histone H1 is bound to linker DNA between nucleosomes. 1,2 Histones are subject to multiple post-translational modifications (PTMs), including acetylation, methylation, ubiquitylation, phosphorylation, and sumoylation. These PTMs determine open and closed chromatin conformations, which, in turn, regulate the differential access and recruitment of transcription factors and other regulatory chromatin-binding proteins to DNA. 3-5 Among these histone modifications, histone acetylation is the most well-studied modification, which occurs at the ε-amino groups of evolutionarily conserved lysine residues located at the N termini. Although all core histones are acetylated in vivo, modifications of histones H3 and H4 are more extensively characterized than those of H2A and H2B. Abbreviations: HDAC, histone deacetylase; HAT, histone acetyl transferase; PTM, post-translational modification; KDAC, lysine deacetylase; TSA, trichostatin A; NAD + , nicotinamide adenine dinucleotide; HAD, HDAC association domain ; GVBD, germinal vesicle breakdown; ChIP-seq, chromatin immunoprecipitation sequencing; TFIID, transcription factor II D; YY1, yin yang 1; Pol II CTD S2, serine 2 within the RNApolymerase II C-terminal domain; H3K4, lysine 4 of histone 3; H3K9, lysine 9 of histone 3; H4K16, lysine 16 of histone 4; SIRT, NAD-dependent deacetylase sirtuin; TBP2, TATA-binding protein 2; DNMT, DNA methyltransferases; RBAP46, retinoblastoma binding protein P46; RNAi, RNA interference; aa, amino acidic; BrUTP, 5-Bromouridine 5′-triphosphate; qRT-PCR, quantitative reverse transcription polymerase chain reaction;

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Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes

Cited by 16 publications

References 39 publications

Zinc Regulates Meiotic Resumption in Porcine Oocytes via a Protein Kinase C-Related Pathway

Zinc Regulates Meiotic Resumption in Porcine Oocytes via a Protein Kinase C-Related Pathway

Dynamic Changes in Histone Acetylation During Sheep Oocyte Maturation

HDAC1 and HDAC2 in mouse oocytes and preimplantation embryos: Specificity versus compensation

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