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Molecular human reproduction1998; 4(6); 563-570; doi: 10.1093/molehr/4.6.563

Maturation-promoting factor (MPF) and mitogen activated protein kinase (MAPK) expression in relation to oocyte competence for in-vitro maturation in the mare.

Abstract: In the equine species, a large proportion of oocytes fail to complete meiosis during in-vitro culture. The biochemical and molecular basis of this failure is unknown. The meiotic cell cycle is controlled in part by the maturation-promoting factor (MPF) and the mitogen-activated protein kinase (MAPK). In this study, we evaluated the oocyte competence for in-vitro maturation and the expression of MPF components (p34cdc2 and cyclin B) and MAPK after in-vitro culture. The maturation rate was influenced by the culture medium and the physiological stage of the mare at the time of oocyte recovery. We showed that MAPK and the two subunits of MPF were present in equine oocytes whatever the nuclear stage they reached after in-vitro culture and whatever the culture medium used. In incompetent oocytes, MAPK remained in its non-phosphorylated form, supposed to be inactive. In conclusion, the incompetence of equine oocytes to resume and complete meiosis is not due to the absence of p34cdc2, cyclin B or MAPK. Our results suggest that it is more probably due to a deficiency of regulators of MPF and/or to an inability to phosphorylate MAPK.
Publication Date: 1998-07-17 PubMed ID: 9665339DOI: 10.1093/molehr/4.6.563Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article investigates the expression of Maturation-Promoting Factor (MPF) and Mitogen Activated Protein Kinase (MAPK) in relation to the ability of horse oocytes (eggs) to mature in laboratory conditions. The study found that these proteins are present in equine oocytes, but their regulation or activation may be responsible for the high rate of failed meiosis in these cells during in-vitro maturation.

Research Objectives

  • The most important objective of this paper is determining the role of two proteins in equine oocyte in-vitro maturation: Maturation-Promoting Factor (MPF) and Mitogen Activated Protein Kinase (MAPK).
  • The researchers aimed to establish if the inability of many horse oocytes to complete meiosis during in-vitro culture is due to the absence of these proteins.

Methodology

  • The study evaluates both the competency of the oocytes for in-vitro maturation. To do this, several variables are considered including the physiological stage of the mare from which the oocytes were recovered, and the type of culture medium that was used during the in-vitro maturation process.
  • It goes on to analyze the expression of the MPF and MAPK proteins in the oocytes after they have undergone in-vitro culture. This included distinguishing between the phosphorylated and non-phosphorylated forms of MAPK, as the non-phosphorylated form is assumed to be inactive.

Findings

  • The study revealed that whether or not horse oocytes matured successfully in the lab was influenced by the culture medium used, and the physiological stage of the mare when the oocytes were taken.
  • This study further established that MPF and MAPK proteins are universally present in horse oocytes, regardless of the in-vitro culture method used or the nuclear stage reached by the oocytes post-in-vitro culture.
  • In oocytes that were not competent to mature, the MAPK protein remained non-phosphorylated and thus, inactive.

Conclusion

  • Based on the findings, this study concluded that the failure to complete meiosis in horse oocytes during in-vitro incubation is not due to the lack of MPF or MAPK proteins. Instead, it is more likely due to defective regulators of MPF or the inability to activate MAPK through phosphorylation.

Cite This Article

APA
Goudet G, Belin F, Bézard J, Gérard N. (1998). Maturation-promoting factor (MPF) and mitogen activated protein kinase (MAPK) expression in relation to oocyte competence for in-vitro maturation in the mare. Mol Hum Reprod, 4(6), 563-570. https://doi.org/10.1093/molehr/4.6.563

Publication

ISSN: 1360-9947
NlmUniqueID: 9513710
Country: England
Language: English
Volume: 4
Issue: 6
Pages: 563-570

Researcher Affiliations

Goudet, G
  • I.N.R.A.-Haras Nationaux, Equipe de Reproduction Equine, Station P.R.M.D., Nouzilly, France.
Belin, F
    Bézard, J
      Gérard, N

        MeSH Terms

        • Animals
        • CDC2 Protein Kinase / analysis
        • Calcium-Calmodulin-Dependent Protein Kinases / biosynthesis
        • Calcium-Calmodulin-Dependent Protein Kinases / genetics
        • Cell Cycle
        • Cells, Cultured
        • Culture Media
        • Cyclin B / analysis
        • Cyclin B1
        • Estrus
        • Female
        • Gene Expression Regulation
        • Horses / physiology
        • Maturation-Promoting Factor / biosynthesis
        • Maturation-Promoting Factor / genetics
        • Meiosis
        • Mitogen-Activated Protein Kinase Kinases
        • Oogenesis / physiology
        • Ovarian Follicle / growth & development
        • Phosphorylation
        • Protein Kinases / deficiency
        • Protein Kinases / physiology
        • Protein Processing, Post-Translational

        Citations

        This article has been cited 6 times.
        1. Bai X, Wang S. Signaling pathway intervention in premature ovarian failure.. Front Med (Lausanne) 2022;9:999440.
          doi: 10.3389/fmed.2022.999440pubmed: 36507521google scholar: lookup
        2. Li S, Kang JD, Jin JX, Hong Y, Zhu HY, Jin L, Gao QS, Yan CG, Cui CD, Li WX, Yin XJ. Effect of demecolcine-assisted enucleation on the MPF level and cyclin B1 distribution in porcine oocytes.. PLoS One 2014;9(3):e91483.
          doi: 10.1371/journal.pone.0091483pubmed: 24626152google scholar: lookup
        3. Lee SK, Zhao MH, Kwon JW, Li YH, Lin ZL, Jin YX, Kim NH, Cui XS. The association of mitochondrial potential and copy number with pig oocyte maturation and developmental potential.. J Reprod Dev 2014 Apr 24;60(2):128-35.
          doi: 10.1262/jrd.2013-098pubmed: 24492657google scholar: lookup
        4. Kim KH, Kim EY, Kim Y, Kim E, Lee HS, Yoon SY, Lee KA. Gas6 downregulation impaired cytoplasmic maturation and pronuclear formation independent to the MPF activity.. PLoS One 2011;6(8):e23304.
          doi: 10.1371/journal.pone.0023304pubmed: 21850267google scholar: lookup
        5. Downs SM. Regulation of the G2/M transition in rodent oocytes.. Mol Reprod Dev 2010 Jul;77(7):566-85.
          doi: 10.1002/mrd.21175pubmed: 20578061google scholar: lookup
        6. Martoriati A, Gérard N. Interleukin-1 (IL-1) system gene expression in granulosa cells: kinetics during terminal preovulatory follicle maturation in the mare.. Reprod Biol Endocrinol 2003 May 16;1:42.
          doi: 10.1186/1477-7827-1-42pubmed: 12803652google scholar: lookup