Login / Signup

Inhibition of Hsp90 during in vitro maturation under thermoneutral or heat shock conditions compromises the developmental competence of bovine oocytes.

Eliza Diniz de SouzaJessica Fernanda da Silva E SouzaPedro Manoel de Oliveira NettoLuciano de Rezende CarvalheiraRibrio Ivan Tavares Pereira BatistaCarolina Capobiango Romano QuintãoIuri Drumond LouroLuiz Sérgio de Almeida Camargo
Published in: Zygote (Cambridge, England) (2022)
Heat shock protein 90 (Hsp90) is critical for cell homeostasis but its role on bovine oocyte maturation is not well known. We investigated the importance of Hsp90 for competence of bovine oocyte using 17-(allylamino)-17-demethoxygeldanamycin (17AAG), an inhibitor of Hsp90, during in vitro maturation (IVM). Three experiments evaluated the effect of 17AAG on developmental competence of oocytes matured in vitro under thermoneutral (38.5ºC) or heat shock (HS; 41.5ºC) temperatures. The first experiment found that the blastocyst rates were lower ( P < 0.05) with 2 µM 17AAG compared with the untreated control (0 µM). The abundance of HSF1 transcripts was higher in oocytes matured with 2 µM than with 0 and 1 µM 17AAG, whereas the abundance of HSP90AA1 and HSPA1A transcripts was lower ( P < 0.05) with 1 and 2 µM than with 0 µM. The second experiment found that 2 µM 17AAG for 12 or 24 h during IVM decreased ( P < 0.05) the blastocysts rates. In the third experiment, the association of 2 μM 17AAG with HS for 12 h during IVM resulted in lower ( P < 0.05) blastocysts rates than 17AAG, HS or untreated control. In conclusion, inhibition of Hsp90 during in vitro maturation compromises further embryo development; the association of Hsp90 inhibition with HS aggravates the deleterious effect of both on oocyte developmental competence.
Keyphrases
  • heat shock
  • heat shock protein
  • heat stress
  • oxidative stress
  • pregnant women
  • single cell
  • bone marrow
  • mass spectrometry
  • antibiotic resistance genes
  • high speed