Involvement of MEK-Mitogen-Activated Protein Kinase Pathway in Follicle-Stimulating Hormone-Induced but Not Spontaneous Meiotic Resumption of Mouse Oocytes1

Su, You-Qiang; Rubinstein, Sara; Luria, A. R.; Lax, Yehudit; Breitbart, Haim

doi:10.1095/biolreprod65.2.358

Cited by 64 publications

(47 citation statements)

References 54 publications

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“…46 Protein samples were seperated in discontinuous Bis-Tris Gels (Invitrogen NP0316) followed by blotting onto PVDF membrane (Millipore IPVH00010). The following primary antibodies were used for western blot: a-tubulin (Sigma T5168), 1:10,000; b-actin (Sigma A5441), 1:10,000; PP2Ac (CST 2038), 1:1,000; securin (Abcam, ab3305).…”

Section: Protein Sample Preparation and Western Blottingmentioning

confidence: 99%

PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte

et al. 2016

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Section: Protein Sample Preparation and Western Blottingmentioning

confidence: 99%

PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte

et al. 2016

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“…In order to study the effects of MEK/ERK/p90 rsk cascade inhibition on meiotic maturation of mouse oocytes, cumulus-free and GV intact oocytes were incubated in M2 medium containing 1.5 M U0126 [19]. The culture medium containing U0126 was renewed every 12 h to prevent the possible degradation of U0126.…”

Section: Division Patterns and Activity Of Map Kinase And P90 Rsk In mentioning

confidence: 99%

“…When incubated in a medium with U0126, part of porcine oocytes completed the second meiotic division and entered into interphase [18]. In cumulus-enclosed mouse oocytes, U0126 produced a dose-dependent inhibitory effect on FSH-induced meiotic resumption [19].…”

Section: Introductionmentioning

confidence: 99%

Effects of MEK inhibitor U0126 on meiotic progression in mouse oocytes: microtuble organization, asymmetric division and metaphase II arrest

et al. 2003

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In this study we used U0126, a potent and specific inhibitor of MEK, to study the roles of MEK/ERK/p90 rsk signaling pathway in the meiotic cell cycle of mouse oocytes. The phosphorylation of MAP kinase and p90 rsk in the oocytes treated with 1.5 M U0126 was the same as that in oocytes cultured in drug-free medium. With 1.5 M U0126 treatment, the spindles appeared normal as they formed in oocytes, but failed to maintain its structure. Instead, the spindle lost one pole or elongated extraordinarily. After further culture, some oocytes extruded gigantic polar bodies (>30 m) that later divided into two small ones. Some oocytes underwent symmetric division and produced two equal-size daughter cells in which normal spindles formed. In oocytes with different division patterns, MAP kinase was normally phosphorylated. When the concentration of U0126 was increased to 15 M, the phosphorylation of both MAPK and p90 rsk were inhibited, while symmetric division was decreased. When incubating in medium containing 15 M U0126 for 14 h, oocytes were activated, but part of them failed to emit polar bodies. MII oocytes were also activated by 15 M U0126, at the same time the dephosphorylation of MAP kinase and p90 rsk was observed. Our results indicate that 1) MEK plays important but not indispensable roles in microtubule organization; 2) MEK keeps normal meiotic spindle morphology, targets peripheral spindle positioning and regulates asymmetric division by activating some unknown substrates other than MAP kinase /p90 rsk ; and 3) activation of MEK/ERK/p90 rsk cascade maintains MII arrest in mouse oocytes.

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“…4C ) ( P < 0.05). Previous reports showed that mice CEOs started to resume meiosis in 8 h if they were treated with FSH existing media ( 36 ). Therefore, we detected the protein expression of CYP51 at 8 h after FSH treatment and found that siRNAs decreased CYP51 protein levels within the 8 h culture period ( Fig.…”

Section: Rnai Silenced Cyp51 Gene Expression In In Vitro Cultured Feomentioning

confidence: 69%

Reducing CYP51 inhibits follicle-stimulating hormone induced resumption of mouse oocyte meiosis in vitro

Wang

Zhou

et al. 2009

Journal of Lipid Research

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This article is available online at http://www.jlr.orgMammalian oocytes arrested at the diplotene stage of the fi rst meiotic division are triggered to initiate meiosis by the preovulatory gonadotrophin surge in vivo, especially LH surge ( 1, 2 ). It has recently been suggested that certain intermediates of cholesterol biosynthesis, such as meiosis activating sterol (MAS), one of the upstream materials for synthesize of steroid hormones, instruct the oocyte to reinitiate meiosis ( 3-6 ). In invertebrate animals, such as xenopus, gonadotrophins induce progesterone secretion and initiate oocyte meiotic resumption. However, in mammals, whether gonadotrophins employ sterol to induce oocyte meiosis is still a pending question. In fact, sterol has the capacity to induce oocyte meiotic resumption. For example, Byskov et al. ( 7-10 ) fi rst discovered that fetal ovaries, which were cocultured with fetal testis, promoted sperm meiosis by secreting a meiosis activating substance. Later, Xia et al. ( 11 ) reported the substance may be a sterol because it is stable for heat. Byskov et al. ( 12 ) purifi ed and identifi ed the sterols from women's follicle fl uid and cattle's testis and nominated them as follicular fl uid derived-meiosis activating sterol and testis-meiosis activating sterol. Follicular fl uid derived-meiosis activating sterol, a direct product of lanosterol 14 ␣ -demethylase (CYP51) ( 13 ), had a dose-dependent effect on stimulating germinal vesicle breakdown (GVBD) in rodent, bovine, and human meiotically arrested oocytes ( 3,4,(14)(15)(16)(17)(18)(19)(20).To better understand the mechanism by which gonadotrophin employs CYP51-mediated sterol as the downstream signal to induce oocytes meiosis, many chemicals, such as Abstract Meiosis activating sterol, produced directly by lanosterol 14-␣ -demethylase (CYP51) during cholesterol biosynthesis, has been shown to promote the initiation of oocyte meiosis. However, the physiological signifi cance of CYP51 action on oocyte meiosis in response to gonadotrophins' induction remained to be further explored. Herein, we analyzed the role of CYP51 in gonadotrophin-induced in vitro oocyte maturation via RNA interference (RNAi). We showed that although both luteinizing hormone (LH) and follicle-stimulating hormone (FSH) signifi cantly induced meiotic resumption in follicle-enclosed oocytes (FEOs), the effect of LH on oocyte meiosis resumption in FEOs was weaker than FSH. Moreover, both FSH and LH were able to upregulate CYP51 expression in cultured follicular granulosa cells when examined at 8 h or 12 h posttreatments, respectively. Interestingly, whereas knockdown of CYP51 expression via small interference RNA (siRNA) moderately blocked (23% reduction at 24 h) FSH-induced oocyte maturation [43% germinal vesicle breakdown (GVBD) rate in RNAi vs. 66% in control, P < 0.05] in FEOs, similar treatments showed no apparent effects on LH-induced FEO meiotic maturation (58% GVBD rate in RNAi vs. 63% in control, P > 0.05). Moreover, the results in a cumulus-enclosed oocytes (CEOs)...

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Involvement of MEK-Mitogen-Activated Protein Kinase Pathway in Follicle-Stimulating Hormone-Induced but Not Spontaneous Meiotic Resumption of Mouse Oocytes1

Cited by 64 publications

References 54 publications

PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte

PP2A regulates kinetochore-microtubule attachment during meiosis I in oocyte

Effects of MEK inhibitor U0126 on meiotic progression in mouse oocytes: microtuble organization, asymmetric division and metaphase II arrest

Reducing CYP51 inhibits follicle-stimulating hormone induced resumption of mouse oocyte meiosis in vitro

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