Involvement of ER-calreticulin-Ca2+ signaling in the regulation of porcine oocyte meiotic maturation and maternal gene expression

2010 ◽  
Vol 77 (5) ◽  
pp. 462-471 ◽  
Author(s):  
Ding-Xiao Zhang ◽  
Xiao-Ping Li ◽  
Shao-Chen Sun ◽  
Xing-Hui Shen ◽  
Xiang-Shun Cui ◽  
...  
Keyword(s):  
Gene Expression ◽  
Meiotic Maturation ◽  
Porcine Oocyte ◽  
Oocyte Meiotic Maturation ◽  
Maternal Gene

Cumulus cell-derived and maternal SIRT6 differentially regulates porcine oocyte meiotic maturation

2020 ◽  
Vol 142 ◽  
pp. 158-168
Author(s):  
Zubing Cao ◽  
Dandan Zhang ◽  
Xu Tong ◽  
Yiqing Wang ◽  
Xin Qi ◽  
...  
Keyword(s):  
Cumulus Cell ◽  
Meiotic Maturation ◽  
Porcine Oocyte ◽  
Oocyte Meiotic Maturation

Gonadotropins Improve Porcine Oocyte Maturation and Embryo Development through Regulation of Maternal Gene Expression

2013 ◽  
Vol 28 (4) ◽  
pp. 361-371 ◽  
Author(s):  
Qing-Ling Wang ◽  
◽  
Ming-Hui Zhao ◽  
Yong-Xun Jin ◽  
Nam-Hyung Kim ◽  
...  
Keyword(s):  
Gene Expression ◽  
Embryo Development ◽  
Oocyte Maturation ◽  
Porcine Oocyte ◽  
Maternal Gene

Characterization of Aurora-A in porcine oocytes and early embryos implies its functional roles in the regulation of meiotic maturation, fertilization and cleavage

Zygote ◽  
2005 ◽  
Vol 13 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Li-Juan Yao ◽  
Qing-Yuan Sun
Keyword(s):  
Confocal Microscopy ◽  
Germinal Vesicle ◽  
Mitotic Cell ◽  
Microtubule Assembly ◽  
Meiotic Maturation ◽  
Aurora A ◽  
Microtubule Organization ◽  
Germinal Vesicle Breakdown ◽  
Porcine Oocyte ◽  
Oocyte Meiotic Maturation

Aurora-A is a serine/threonine protein kinase that plays important regulatory roles during mitotic cell cycle progression. In this study, Aurora-A expression, subcellular localization, and possible functions during porcine oocyte meiotic maturation, fertilization and early embryonic cleavage were studied by using Western blot, confocal microscopy and drug treatments. The quantity of Aurora-A protein remained stable during porcine oocyte meiotic maturation. Confocal microscopy revealed that Aurora-A distributed abundantly in the nucleus at the germinal vesicle stage. After germinal vesicle breakdown, Aurora-A concentrated around the condensed chromosomes and the metaphase I spindle, and finally, Aurora-A was associated with spindle poles during the formation of the metaphase II spindle. Aurora-A concentrated in the pronuclei in fertilized eggs. Aurora-A was not found in the spindle region when colchicine or staurosporine was used to inhibit microtubule organization, while it accumulated as several dots in the cytoplasm after taxol treatment. In conclusion, Aurora-A may be a multifunctional kinase that plays pivotal regulatory roles in microtubule assembly during porcine oocyte meiotic maturation, fertilization and early embryonic mitosis.

scholarly journals Regulation of Maternal Gene Expression by MEK/MAPK and MPF Signaling in Porcine Oocytes During In Vitro Meiotic Maturation

2011 ◽  
Vol 57 (1) ◽  
pp. 49-56 ◽  
Author(s):  
Ding-Xiao ZHANG ◽  
Won-Jun PARK ◽  
Shao-Chen SUN ◽  
Yong-Nan XU ◽  
Ying-Hua LI ◽  
...  
Keyword(s):  
Gene Expression ◽  
Meiotic Maturation ◽  
Maternal Gene

scholarly journals HASPIN kinase mediates histone deacetylation to regulate oocyte meiotic maturation in pigs

Reproduction ◽  
2019 ◽  
Vol 157 (6) ◽  
pp. 501-510 ◽  
Author(s):  
Zubing Cao ◽  
Tengteng Xu ◽  
Xu Tong ◽  
Dandan Zhang ◽  
Chengxue Liu ◽  
...  
Keyword(s):  
Spindle Assembly Checkpoint ◽  
Histone H3 ◽  
Germinal Vesicle ◽  
Early Embryo ◽  
Histone Deacetylation ◽  
Meiotic Maturation ◽  
Metaphase Chromosomes ◽  
Germinal Vesicle Breakdown ◽  
Porcine Oocyte ◽  
Oocyte Meiotic Maturation

HASPIN kinase-catalyzed phosphorylation of histone H3 on threonine 3 (H3T3p) directs the activity and localization of chromosomal passenger complex (CPC) and spindle assembly checkpoint (SAC) to regulate chromosome condensation and segregation in both mitosis and meiosis. However, the function of HASPIN kinase in the meiotic maturation of porcine oocytes is not yet known. Here, we found that HASPIN mRNA is constantly expressed in porcine oocyte maturation and subsequent early embryo development. H3T3p is highly enriched on chromosomes at germinal vesicle breakdown (GVBD) stage and thereafter maintains a low level in progression through metaphase I (MI) to metaphase II (MII). Correspondingly, H3T3p was completely abolished in oocytes treated with an inhibitor of HASPIN kinase. Functionally, inhibition of HASPIN activity led to a significant reduction in the rate of oocyte meiotic maturation and the limited cumulus expansion. Additionally, HASPIN inhibition caused both spindle disorganization and chromosome misalignment in oocytes at MI and MII stage. Importantly, HASPIN inhibition severely prevented deacetylation of several highly conserved lysine (K) residues of histone H3 and H4 including H3K9, H3K14, H4K5, H4K8, H4K12 and H4K16 on the metaphase chromosomes during oocyte meiotic maturation. Taken together, these results demonstrate that HASPIN kinase regulates porcine oocyte meiotic maturation via modulating histone deacetylation.

EZH2 is essential for spindle assembly regulation and chromosomal integrity during porcine oocyte meiotic maturation†

2020 ◽  
Author(s):  
Qingqing Cai ◽  
Keying Wen ◽  
Miao Ma ◽  
Wei Chen ◽  
Delin Mo ◽  
...  
Keyword(s):  
Embryonic Development ◽  
Polar Body ◽  
Spindle Assembly ◽  
Meiotic Maturation ◽  
Meiotic Progression ◽  
First Polar Body ◽  
Porcine Oocyte ◽  
Polar Body Extrusion ◽  
Oocyte Meiotic Maturation ◽  
Early Occurrence

Abstract Enhancer of zeste homolog 2 (EZH2) has been extensively investigated to participate in diverse biological processes, including carcinogenesis, the cell cycle, X-chromosome inactivation, and early embryonic development. However, the functions of this protein during mammalian oocyte meiotic maturation remain largely unexplored. Here, combined with RNA-Seq, we provided evidence that EZH2 is essential for oocyte meiotic maturation in pigs. First, EZH2 protein expression increased with oocyte progression from GV to MII stage. Second, the siRNA-mediated depletion of EZH2 led to accelerated GVBD and early occurrence of the first polar body extrusion. Third, EZH2 knockdown resulted in defective spindle assembly, abnormal SAC activity, and unstable K-MT attachment, which was concomitant with the increased rate of aneuploidy. Finally, EZH2 silencing exacerbated oxidative stress by increasing ROS levels and disrupting the distribution of active mitochondria in porcine oocytes. Furthermore, parthenogenetic embryonic development was impaired following the depletion of EZH2 at GV stage. Taken together, we concluded that EZH2 is necessary for porcine oocyte meiotic progression through regulating spindle organization, maintaining chromosomal integrity, and mitochondrial function.

scholarly journals LIMK1/2 inhibitor LIMKi 3 suppresses porcine oocyte maturation

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e2553 ◽  
Author(s):  
Ru-Xia Jia ◽  
Xing Duan ◽  
Si-Jing Song ◽  
Shao-Chen Sun
Keyword(s):  
Oocyte Maturation ◽  
Polar Body ◽  
Meiotic Spindle ◽  
Actin Dynamics ◽  
Immunofluorescent Staining ◽  
Meiotic Maturation ◽  
Spindle Positioning ◽  
Oocyte Meiosis ◽  
Porcine Oocyte ◽  
Oocyte Meiotic Maturation

LIMKi 3 is a specific selective LIMK inhibitor against LIMK1 and LIMK2, while LIMK1 and LIMK2 are the main regulators of actin cytoskeleton to participate in many cell activities. However, the effect of LIMKi 3 in porcine oocyte meiosis is still unclear. The present study was designed to investigate the effects of LIMKi 3 and potential regulatory role of LIMK1/2 on porcine oocyte meiotic maturation. Immunofluorescent staining of p-LIMK1/2 antibody showed that LIMK1/2 was localized mainly to the cortex of porcine oocyte, which co-localized with actin. After LIMKi 3 treatment, the diffusion of COCs became weak and the rate of polar body extrusion was decreased. This could be rescued by moving oocytes to fresh medium. After prolonging the culture time of oocytes, the maturation rate of porcine oocyte increased in LIMKi 3 groups, indicating that LIMKi 3 may suppress the cell cycle during porcine oocyte maturation. We also found that after LIMKi 3 treatment actin distribution was significantly disturbed at porcine oocyte membranes and cytoplasm, indicating the conserved roles of LIMK1/2 on actin dynamics. Next we examined the meiotic spindle positioning in porcine oocyte, and the results showed that a majority of spindles were not attached to the cortex of porcine oocyte, indicating that LIMKi 3 may affect actin-mediated spindle positioning. Taken together, these results showed that LIMK1/2 inhibitor LIMKi 3 had a repressive role on porcine oocyte meiotic maturation.

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