Effects of ubiquitin C-terminal hydrolase L1 deficiency on mouse ova

被引:10
|
作者
Koyanagi, Sayaka [1 ]
Hamasaki, Hiroko [1 ]
Sekiguchi, Satoshi [1 ]
Hara, Kenshiro
Ishii, Yoshiyuki [1 ]
Kyuwa, Shigeru [1 ]
Yoshikawa, Yasuhiro [1 ,2 ]
机构
[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biomed Sci, Bunkyo Ku, Tokyo 1138657, Japan
[2] Kitasato Univ, Sch Vet Med, Lab Zoonoses, Towada, Aomori 0348628, Japan
基金
日本学术振兴会;
关键词
CORTICAL GRANULE EXOCYTOSIS; ACTIN DEPOLYMERIZING FACTOR; IN-VITRO MATURATION; PROTEIN-KINASE-C; ENDOPLASMIC-RETICULUM; MEIOTIC MATURATION; ZONA-PELLUCIDA; EMBRYO DEVELOPMENT; PROTEOMIC ANALYSIS; MATERNAL PROTEINS;
D O I
10.1530/REP-11-0128
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Maternal proteins are rapidly degraded by the ubiquitin proteasome system during oocyte maturation in mice. Ubiquitin C-terminal hydrolase L1 (UCHL1) is highly and specifically expressed in mouse ova and is involved in the polyspermy block. However, the role of UCHL1 in the underlying mechanism of polyspermy block is poorly understood. To address this issue, we performed a comprehensive proteomic analysis to identify maternal proteins that were relevant to the role of UCHL1 in mouse ova using UCHL1-deficient gad. Furthermore, we assessed morphological features in gad mouse ova using transmission electron microscopy. NACHT, LRR, and PYD domain-containing (NALP) family proteins and endoplasmic reticulum (ER) chaperones were identified by proteomic analysis. We also found that the 'maternal antigen that embryos require' (NLRP5 (MATER)) protein level increased significantly in gad mouse ova compared with that in wild-type mice. In an ultrastructural study, gad mouse ova contained less ER in the cortex than in wild-type mice. These results provide new insights into the role of UCHL1 in the mechanism of polyspermy block in mouse ova. Reproduction (2012) 143 271-279
引用
收藏
页码:271 / 279
页数:9
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