We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Heat shock protein 90a couples with the MAPK-signaling pathway to determine meiotic maturation of porcine oocytes.
- Authors
Liu, Yun-Hua; Liu, Xiao-Man; Wang, Pei-Chao; Yu, Xiao-Xia; Miao, Jia-Kun; Liu, Shuai; Wang, Yan-Kui; Du, Zhi-Qiang; Yang, Cai-Xia
- Abstract
Heat shock protein 90 (Hsp90) functions as a molecular chaperone in its interaction with clients to influence multiple cellular and physiological processes. However, our current understanding on Hsp90's relationship with mammalian oocyte maturation is still very limited. Here, we aimed to investigate Hsp90's effect on pig oocyte meiotic maturation. Endogenous Hsp90a was constantly expressed at both mRNA and protein levels in porcine maturing oocytes. Addition of 2 µM 17-allylamino-17-demethoxygeldanamycin (17-AAG), the Hsp90 inhibitor, to in vitro mature cumulus-oocyte complexes (COC) significantly decreased Hsp90a protein level (P < 0.05), delayed germinal vesicle breakdown (GVBD) (P < 0.05), and impeded the first polar body (PB1) extrusion (P < 0.01) of porcine oocytes. 2 µM 17-AAG treatment during in vitro maturation also decreased the subsequent development competence as indicated by the lower cleavage (P < 0.001) and higher fragmentation (P < 0.001) rates of parthenotes, whereas no effects on the percentage and average cell number of blastocysts were found. Immunodepletion of Hsp90a by antibody microinjection into porcine oocytes at germinal vesicle and metaphase II stages induced similar defects of meiotic maturation and parthenote development, to that resulted from 2 µM inhibitor 17-AAG. For oocytes treated by 2 µM 17-AAG, the cytoplasm and membrane actin levels were weakened (P < 0.01), and the spindle assembly was disturbed (P < 0.05), due to decreased p-ERK1/2 level (P < 0.05). However, the mitochondrial function and early apoptosis were not affected, as demonstrated by rhodamine 123 staining and Annexin V assays. Our findings indicate that Hsp90a can couple with mitogen-activated protein kinase to regulate cytoskeletal structure and orchestrate meiotic maturation of porcine oocytes.
- Subjects
MAMMAL heat shock proteins; OVUM physiology; MEIOSIS; SWINE embryology; MITOGEN-activated protein kinases; CELL physiology; SWINE genetics; SWINE physiology
- Publication
Journal of Animal Science, 2018, Vol 96, Issue 8, p3358
- ISSN
0021-8812
- Publication type
Article
- DOI
10.1093/jas/sky213