Inactivation of MAPK affects centrosome assembly, but not actin filament assembly, in mouse oocytes maturing in vitro

Lee, Seung‐Eun; Kim, Ji-Hoi; Kim, Nam‐Hyung

doi:10.1002/mrd.20695

Cited by 16 publications

(13 citation statements)

References 33 publications

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“…When MAPK3/MAPK1 activity was blocked by specific MEK1/2 inhibitor U0126 from the beginning of IVM, bovine oocytes progress through GVBD, but could not reach the correct MI stage (Tosca et al 2007); the same effect was reported in mice (Lee et al 2007). In contrast, when mouse oocytes were treated by U0126 after GVBD, although the phosphorylation of MAPK3/MAPK1 was drastically reduced, the polar body extrusion was normal, but the organisation of metaphase plate and chromosome segregation were affected (Lee et al 2007). Thus, in bovine oocytes, LiCl 2 led to the inhibition of MAPK3/MAPK1 activation prior to GVBD, which in turn contributed to the arrest at first meiotic division.…”

Section: Gsk3b Expression In Bovine Oocytes and Surrounding Folliculasupporting

confidence: 52%

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Uzbekova¹,

Salhab²,

Perreau³

et al. 2009

Reproduction

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Glycogen synthase kinase 3 (GSK3) regulates cellular metabolism and cell cycle via different signalling pathways. In response to insulin and growth factors GSK3 is serine-phosphorylated and inactivated. We analysed GSK3B expression and activation in bovine cumulus cells (CC) and oocytes at different meiotic stages in vitro in parallel with MAP kinases ERK (MAPK3/MAPK1) and p38 (MAPK14). GSK3B localised to cytoplasm in granulosa cells and in oocytes throughout folliculogenesis. In mature metaphase-II (MII) oocytes, GSK3B was concentrated to the region of midzone between the oocyte and the first polar body, as well as active phospho-Thr Aurora A kinase (AURKA). During in vitro maturation (IVM), in oocytes, phospho-Ser 9 -GSK3B level increased as well as phospho-MAPK3/MAPK1, while phospho-MAPK14 decreased. In CC, phospho-MAPK14 increased upon germinal vesicle breakdown (GVBD)/metaphase-I (MI) and then decreased during transition to MII. Administration of inhibitors of GSK3 activity (lithium chloride or 2 0 Z,3 0 E -6-bromoindirubin-3 0 -oxime) rapidly increased phospho-Ser 9 -GSK3B, and led to transient decrease of phospho-MAPK3/MAPK1 and to durable enhancing of phospho-MAPK14 in granulosa primary cell culture. GSK3 inhibitors during IVM diminished cumulus expansion and delayed meiotic progression. In cumulus, phospho-MAPK14 level was significantly higher in the presence of inhibitors, comparing with control, through the time of MI/MII transition. In oocytes, phospho-GSK3B was increased and phospho-MAPK3/MAPK1 was decreased before GVBD and oocytes were mainly arrested at MI. Therefore, GSK3B might regulate oocyte meiosis, notably MI/MII transition being the part of MAPK3/1 and MAPK14 pathways in oocytes and CC. GSK3B might be also involved in the local activation of AURKA that controls this transition.

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Section: Gsk3b Expression In Bovine Oocytes and Surrounding Folliculasupporting

confidence: 52%

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Uzbekova¹,

Salhab²,

Perreau³

et al. 2009

Reproduction

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“…Higher levels of U0126 (10 mM) were required to prevent PBE when treatment was done after GVBD (data not shown). This phenomenon suggests that the differences in the reports of Tong et al, Lee et al and Yu et al might be dependent on the timing and concentration of U0126 treatment (Tong et al, 2003;Lee et al, 2000;Lee et al, 2007;Yu et al, 2007).…”

Section: Resultsmentioning

confidence: 83%

“…In contrast, Mos knockout (Mos-KO) mouse oocytes extrude abnormally big polar bodies and enter parthenogenesis (Choi et al, 1996;Verlhac et al 2000), but injection of Mos antisense oligonucleotides (MosAS) (Paules et al, 1989) at GV stage prevents PBE in wild-type mouse oocytes. Despite these differences, inhibition of MEK activity by U0126 at GV stage prevents PBE consistently in cnidarian, mouse and pig oocytes (Lee et al, 2000;Lee et al, 2007;Amiel et al, 2009). However, variable results were obtained about MEK inhibition following GVBD in mouse oocytes: extrusion of normal polar bodies, large polar bodies, polar bodies without chromosomes or no polar bodies (Tong et al, 2003;Lee et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

“…Despite these differences, inhibition of MEK activity by U0126 at GV stage prevents PBE consistently in cnidarian, mouse and pig oocytes (Lee et al, 2000;Lee et al, 2007;Amiel et al, 2009). However, variable results were obtained about MEK inhibition following GVBD in mouse oocytes: extrusion of normal polar bodies, large polar bodies, polar bodies without chromosomes or no polar bodies (Tong et al, 2003;Lee et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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The Mos-MAPK pathway regulates Diaphanous-related formin activity to drive cleavage furrow closure during polar body emission in starfish oocytes

Ucar

Tachibana

Kishimoto

2013

Journal of Cell Science

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SummaryMaintenance of spindle attachment to the cortex and formation of the cleavage furrow around the protruded spindle are essential for polar body extrusion (PBE) during meiotic maturation of oocytes. Although spindle movement to the cortex has been well-studied, how the spindle is maintained at the cortex during PBE is unknown. Here, we show that activation of Diaphanous-related formin mediated by mitogen-activated protein kinase (MAPK) is required for tight spindle attachment to the cortex and cleavage furrow closure during PBE in starfish (Asterina pectinifera) oocytes. A. pectinifera Diaphanous-related formin (ApDia) had a distinct localization in immature oocytes and was localized to the cleavage furrow during PBE. Inhibition of the Mos-MAPK pathway or the actin nucleating activity of formin homology 2 domain prevented cleavage furrow closure and resulted in PBE failure. In MEK/MAPK-inhibited oocytes, activation of ApDia by relief of its intramolecular inhibition restored PBE. In summary, this study elucidates a link between the Mos-MAPK pathway and Diaphanous-related formins, that is responsible for maintaining tight spindle attachment to the cortex and cleavage furrow closure during PBE.

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“…Following germinal vesicle breakdown (GVBD), the chromatin is condensed, the metaphase I (MI) spindle is organized and oocytes extrude the first polar body upon completion of meiosis I. Subsequently, oocytes develop to metaphase of meiosis II (MII) and maintain the second meiotic arrest until fertilization [1][2][3]. Protein phosphorylation and dephosphorylation play pivotal roles in the oocyte meiotic cell cycle.…”

mentioning

confidence: 99%

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

et al. 2011

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Abstract. Mitogen-activated protein kinase (MAPK) and maturation/M phase promoting factor (MPF) play crucial roles in oocyte meiotic maturation in mammals. However, the underlying molecular mechanisms have not been addressed. In this study, the effects of the MEK/MAPK pathway inhibitor U0126 and the MPF inhibitor roscovitine on meiotic maturation and maternal gene expression in pig cumulus-oocyte complexes (COCs) and denuded oocytes (DOs) were investigated. Both inhibitors can reversibly block the resumption of meiosis in pig oocytes. COCs or DOs initially cultured in drug-free medium for 24 h and then transferred to medium containing U0126 showed normal progress to the Metaphase II stage (MII); (90.38 vs. 92.16% control group). In contrast, roscovitine treatment from 24 to 44 h significantly inhibited maturation of COCs and DOs. To explore the underlying molecular mechanisms, expression patterns and polyadenylation states of five representative maternal transcripts, cyclin B1, Cdc2, C-mos, GDF9 and BMP15, were examined by real-time PCR and poly(A)-test PCR (PAT assay). U0126 treatment resulted in aberrant expression of Cdc2 and GDF9, while roscovitine significantly maintained all five maternal transcripts at very high levels in treated COCs compared with the control group. The polyadenylation of these mRNAs increased as well. Furthermore, the experiments were repeated in DOs, and the results also indicated that both Cdc2 and GDF9 showed significantly higher expression in both mRNA and polyadenylation levels in the drug treatment groups. Together, these results provide the first demonstration in a mammalian system that MAPK and MPF play important roles in regulation of maternal gene expression during oocyte maturation. Key words: Cytoplasmic polyadenylation, Maternal gene, Mitogen-activated protein kinase (MAPK), M phase promoting factor (MPF) (J. Reprod. Dev. 57: [49][50][51][52][53][54][55][56] 2011) n mammals, fully grown follicular oocytes are arrested at the G2 stage, which is called the germinal vesicle (GV) stage of development. The oocytes resume meiosis in response to specific signals, usually hormones, or after being released from their follicular environment. Following germinal vesicle breakdown (GVBD), the chromatin is condensed, the metaphase I (MI) spindle is organized and oocytes extrude the first polar body upon completion of meiosis I. Subsequently, oocytes develop to metaphase of meiosis II (MII) and maintain the second meiotic arrest until fertilization [1][2][3]. Protein phosphorylation and dephosphorylation play pivotal roles in the oocyte meiotic cell cycle. Maturation/M-phase promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are the principal regulatory systems that drive meiotic progression of oocytes. MAPK p42 and p44, also known as extracellular signal-regulated kinase 1 and 2 (ERK1 and ERK2), are serine/threonine kinases that can be phosphorylated and activated by MAPK kinase (MEK) [1,4]. MPF is a complex composed of a catalytic subunit, p34/cdc2, with serine/threon...

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Inactivation of MAPK affects centrosome assembly, but not actin filament assembly, in mouse oocytes maturing in vitro

Cited by 16 publications

References 33 publications

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

The Mos-MAPK pathway regulates Diaphanous-related formin activity to drive cleavage furrow closure during polar body emission in starfish oocytes

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

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