The signaling pathways linking to lysophosphatidic acid-promoted meiotic maturation in mice

Komatsu, J; Yamano, Shuji; Kuwahara, Akira; Tokumura, Akira; Irahara, Minoru

doi:10.1016/j.lfs.2006.01.028

Cited by 30 publications

(26 citation statements)

References 41 publications

(46 reference statements)

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“…Moreover, we cannot exclude that LPA supplementation of maturation medium can impact the maturation process itself and/or early pronuclear stages of embryo development. In rodents, LPA promoted nuclear and cytoplasmic oocyte maturation via cumulus cells and through the closure or loosening of gap junctions between cumulus cells and the oocyte [35, 36], as well as stimulated blastocyst development [38, 78, 79]. Differences in early embryonic development between the mouse and bovine models may account for the discrepancy in the rate of blastocyst development observed in our study and in the studies with rodents.…”

Section: Discussionmentioning

confidence: 56%

“…This indicates that bovine COCs are a potential source and target of LPA action and that LPA may be involved in cellular signaling between the oocyte and cumulus cells during maturation. Up to now, the presence of LPAR1 and LPAR2 was proposed only in the murine cumulus cells [35]. In mice it was also demonstrated that during blastocyst differentiation in vitro , embryos expressed LPAR1 mRNA constitutively, LPAR2 only in the late stage blastocysts, and there was no expression of LPAR3 [38].…”

Section: Discussionmentioning

confidence: 99%

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The Effect of Lysophosphatidic Acid duringIn VitroMaturation of Bovine Oocytes: Embryonic Development and mRNA Abundances of Genes Involved in Apoptosis and Oocyte Competence

Boruszewska

Torres

Kowalczyk-Zięba

et al. 2014

Mediators of Inflammation

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In the present study we examined whether LPA can be synthesized and act during in vitro maturation of bovine cumulus oocyte complexes (COCs). We found transcription of genes coding for enzymes of LPA synthesis pathway (ATX and PLA2) and of LPA receptors (LPAR 1–4) in bovine oocytes and cumulus cells, following in vitro maturation. COCs were matured in vitro in presence or absence of LPA (10−5 M) for 24 h. Supplementation of maturation medium with LPA increased mRNA abundance of FST and GDF9 in oocytes and decreased mRNA abundance of CTSs in cumulus cells. Additionally, oocytes stimulated with LPA had higher transcription levels of BCL2 and lower transcription levels of BAX resulting in the significantly lower BAX/BCL2 ratio. Blastocyst rates on day 7 were similar in the control and the LPA-stimulated COCs. Our study demonstrates for the first time that bovine COCs are a potential source and target of LPA action. We postulate that LPA exerts an autocrine and/or paracrine signaling, through several LPARs, between the oocyte and cumulus cells. LPA supplementation of maturation medium improves COC quality, and although this was not translated into an enhanced in vitro development until the blastocyst stage, improved oocyte competence may be relevant for subsequent in vivo survival.

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Section: Discussionmentioning

confidence: 56%

Section: Discussionmentioning

confidence: 99%

The Effect of Lysophosphatidic Acid duringIn VitroMaturation of Bovine Oocytes: Embryonic Development and mRNA Abundances of Genes Involved in Apoptosis and Oocyte Competence

Boruszewska

Torres

Kowalczyk-Zięba

et al. 2014

Mediators of Inflammation

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“…For example, TGF-β signaling, which plays a crucial role in oocyte maturation and fertilization [33], may be governed by its negative regulator PPM1A. Similarly, P38-MAPK, which is known for its important role in uncoupling the communication between cumulus cells and the oocyte after LH stimulation, might be affected by this phosphatase [34,35]. The important role of phosphatases in oocyte maturation was demonstrated by regulation of the dual specific phosphatase Cdc25, which promotes oocyte maturation by reversing the inhibitory phosphorylation that keeps the oocytes at the GV stage, and by activation of MPF to promote progression of the cell cycle [6].…”

Section: Discussionmentioning

confidence: 99%

De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

Chuderland

Dvashi

Kaplan-Kraicer

et al. 2012

Cellular and Molecular Biology Letters

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Oocyte maturation in mammals is a multiple-stage process that generates fertilizable oocytes. Ovarian oocytes are arrested at prophase of the first meiotic division characterized by the presence of a germinal vesicle. Towards ovulation, the oocytes resume meiosis and proceed to the second metaphase in a process known as maturation; they undergo nuclear and cytoplasmic changes that are accompanied by translation and degradation of mRNA. Protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A), which belongs to the metal-dependent serine/threonine protein phosphatase family, is highly conserved during evolution. PPM1A plays a significant role in many cellular functions such as cell cycle progression, apoptosis and cellular differentiation. It works through diverse signaling pathways, including p38 MAP kinase JNK and transforming growth factor beta (TGF-β). Herein we report that PPM1A is expressed in mouse oocytes and that its mRNA level rises during oocyte maturation. Using quantitative real-time polymerase chain reaction (qPCR) and western blot analysis, we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A

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“…Whether or not gap junctions are phosphorylated, several compounds (i.e., growth factors, lindane, lysophosphatidic acid, 12- O -tetra-decanoylphorbol-13-acetate, and cannabinoids) are known to inhibit GJIC through a MEK-dependent pathway (Komatsu et al 2006; Mograbi et al 2003; Rivedal and Opsahl 2001; Upham et al 2003). Although many compounds activate MAPKs, such as p38 and ERK, the mechanism of inhibiting GJIC by many of these compounds is independent from these MAPKs (Machala et al 2003; Upham et al 2008).…”

Section: Discussionmentioning

confidence: 99%

Structure-Activity–Dependent Regulation of Cell Communication by Perfluorinated Fatty Acids using in Vivo and in Vitro Model Systems

Upham

Park

Babica

et al. 2009

Environ Health Perspect

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BackgroundPerfluoroalkanoates, [e.g., perfluorooctanoate (PFOA)], are known peroxisome proliferators that induce hepatomegaly and hepatocarcinogenesis in rodents, and are classic non-genotoxic carcinogens that inhibit in vitro gap-junctional intercellular communication (GJIC). This inhibition of GJIC is known to be a function of perfluorinated carbon lengths ranging from 7 to 10.ObjectivesThe aim of this study was to determine if the inhibition of GJIC by PFOA but not perfluoropentanoate (PFPeA) observed in F344 rat liver cells in vitro also occurs in F344 rats in vivo and to determine mechanisms of PFOA dysregulation of GJIC using in vitro assay systems.MethodsWe used an incision load/dye transfer technique to assess GJIC in livers of rats exposed to PFOA and PFPeA. We used in vitro assays with inhibitors of cell signaling enzymes and antioxidants known to regulate GJIC to identify which enzymes regulated PFOA-induced inhibition of GJIC.ResultsPFOA inhibited GJIC and induced hepatomegaly in rat livers, whereas PFPeA had no effect on either end point. Serum biochemistry of liver enzymes indicated no cytotoxic response to these compounds. In vitro analysis of mitogen-activated protein kinase (MAPK) indicated that PFOA, but not PFPeA, can activate the extracellular receptor kinase (ERK). Inhibition of GJIC, in vitro, by PFOA depended on the activation of both ERK and phosphatidylcholine-specific phospholipase C (PC-PLC) in the dysregulation of GJIC in an oxidative-dependent mechanism.ConclusionsThe in vitro analysis of GJIC, an epigenetic marker of tumor promoters, can also predict the in vivo activity of PFOA, which dysregulated GJIC via ERK and PC-PLC.

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The signaling pathways linking to lysophosphatidic acid-promoted meiotic maturation in mice

Cited by 30 publications

References 41 publications

The Effect of Lysophosphatidic Acid duringIn VitroMaturation of Bovine Oocytes: Embryonic Development and mRNA Abundances of Genes Involved in Apoptosis and Oocyte Competence

The Effect of Lysophosphatidic Acid duringIn VitroMaturation of Bovine Oocytes: Embryonic Development and mRNA Abundances of Genes Involved in Apoptosis and Oocyte Competence

De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

Structure-Activity–Dependent Regulation of Cell Communication by Perfluorinated Fatty Acids using in Vivo and in Vitro Model Systems

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