Female infertility in PDE3A(-/-) mice: polo-like kinase 1 (Plk1) may be a target of protein kinase A (PKA) and involved in meiotic arrest of oocytes from PDE3A(-/-) mice.

Publisher: Taylor & Francis Country of Publication: United States NLM ID: 101137841 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1551-4005 (Electronic) Linking ISSN: 15514005 NLM ISO Abbreviation: Cell Cycle Subsets: MEDLINE

Publication: 2015- : Philadelphia, PA : Taylor & Francis
Original Publication: Georgetown, TX : Landes Bioscience, c2002-

Cell Cycle Proteins/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 3/*metabolism ; Infertility, Female/*enzymology ; Oocytes/*enzymology ; Protein Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism; Animals ; CDC2 Protein Kinase/analysis ; CDC2 Protein Kinase/metabolism ; Cell Division ; Cells, Cultured ; Cyclic Nucleotide Phosphodiesterases, Type 3/analysis ; Cyclic Nucleotide Phosphodiesterases, Type 3/genetics ; Cyclin B1/metabolism ; Female ; G2 Phase ; Genotype ; HeLa Cells ; Histones/metabolism ; Humans ; Infertility, Female/metabolism ; Meiosis ; Mice ; Mice, Knockout ; Oocytes/growth & development ; Oocytes/metabolism ; Phosphorylation ; Signal Transduction ; cdc25 Phosphatases/metabolism ; Polo-Like Kinase 1

Mechanisms of cAMP/PKA-induced meiotic arrest in oocytes are not completely identified. In cultured, G2/M-arrested PDE3A(-/-) murine oocytes, elevated PKA activity was associated with inactivation of Cdc2 and Plk1, and inhibition of phosphorylation of histone H3 (S10) and of dephosphorylation of Cdc25B (S323) and Cdc2 (Thr14/Tyr15). In cultured WT oocytes, PKA activity was transiently reduced and then increased to that observed in PDE3A(-/-) oocytes; Cdc2 and Plk1 were activated, phosphorylation of histone H3 (S10) and dephosphorylation of Cdc25B (S323) and Cdc2 (Thr14/Tyr15) were observed. In WT oocytes, PKAc were rapidly translocated into nucleus, and then to the spindle apparatus, but in PDE3A(-/-) oocytes, PKAc remained in the cytosol. Plk1 was reactivated by incubation of PDE3A(-/-) oocytes with PKA inhibitor, Rp-cAMPS. PDE3A was co-localized with Plk1 in WT oocytes, and co-immunoprecipitated with Plk1 in WT ovary and Hela cells. PKAc phosphorylated rPlk1 and Hela cell Plk1 and inhibited Plk1 activity in vitro. Our results suggest that PKA-induced inhibition of Plk1 may be critical in oocyte meiotic arrest and female infertility in PDE3A(-/-) mice.

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United States Intramural NIH HHS

0 (Cell Cycle Proteins)
0 (Cyclin B1)
0 (Histones)
0 (Proto-Oncogene Proteins)
EC 2.7.11.1 (Protein Serine-Threonine Kinases)
EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
EC 2.7.11.22 (CDC2 Protein Kinase)
EC 3.1.3.48 (Cdc25b protein, mouse)
EC 3.1.3.48 (cdc25 Phosphatases)
EC 3.1.4.17 (Cyclic Nucleotide Phosphodiesterases, Type 3)
EC 3.1.4.17 (Pde3a protein, mouse)

Date Created: 20101125 Date Completed: 20110412 Latest Revision: 20231213

20231215

PMC3048038

10.4161/cc.9.23.14090

21099356