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G-Protein-Coupled Receptor Kinase 2 Inhibition Induces Meiotic Arrest by Disturbing Ca 2+ Release in Porcine Oocytes.

Ji-Dam KimSong-Hee LeeXiao-Han LiQin-Yue LuCheng-Lin ZhanGyu-Hyun LeeJae-Min SimHyeon-Ji SongDongjie ZhouXiang-Shun Cui
Published in: Reproduction in domestic animals = Zuchthygiene (2024)
G-protein-coupled receptor kinase 2 (GRK2) interacts with Gβγ and Gαq, subunits of G-protein alpha, to regulate cell signalling. The second messenger inositol trisphosphate, produced by activated Gαq, promotes calcium release from the endoplasmic reticulum (ER) and regulates maturation-promoting factor (MPF) activity. This study aimed to investigate the role of GRK2 in MPF activity during the meiotic maturation of porcine oocytes. A specific inhibitor of GRK2 (βi) was used in this study. The present study showed that GRK2 inhibition increased the percentage of oocyte arrest at the metaphase I (MI) stage (control: 13.84 ± 0.95%; βi: 31.30 ± 4.18%), which resulted in the reduction of the maturation rate (control: 80.36 ± 1.94%; βi: 65.40 ± 1.14%). The level of phospho-GRK2 decreased in the treated group, suggesting that GRK2 activity was reduced upon GRK2 inhibition. Furthermore, the addition of βi decreased Ca 2+ release from the ER. The protein levels of cyclin B and cyclin-dependent kinase 1 were higher in the treatment group than those in the control group, indicating that GRK2 inhibition prevented a decrease in MPF activity. Collectively, GRK2 inhibition induced meiotic arrest at the MI stage in porcine oocytes by preventing a decrease in MPF activity, suggesting that GRK2 is essential for oocyte meiotic maturation in pigs.
Keyphrases
  • endoplasmic reticulum
  • cell cycle
  • protein kinase
  • tyrosine kinase
  • stem cells
  • small molecule
  • signaling pathway
  • drug induced
  • diabetic rats
  • amino acid
  • stress induced
  • replacement therapy
  • newly diagnosed