Ubiquitin carboxyl-terminal hydrolase L1 contributes to the oocyte selective elimination in prepubertal mouse ovaries.
Apoptosis of abnormal oocytes is essential for defective oocyte elimination during prepubertal ovary development, and the ubiquitin system regulates the cell apoptosis via the degradation of specific proteins. Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) is a component of the ubiquitin system, and the UCH-L1-dependent apoptosis is important for spermatogenesis. In the present study, the change in the number of follicles and the expression of UCH-L1 in oocytes were determined in prepubertal mouse ovaries by immunohistochemical techniques. A significant decrease in the follicular pool was found in prepubertal mouse ovaries during the period of day 21 to day 28 after birth, and accordingly, the UCH-L1 protein expression was increased, to some degree in association with Jun activation domain-binding protein 1 (Jab1) and cyclin-dependent kinase inhibitor p27(Kipl). The increased UCH-L1 protein, together with the corresponding changes of Jab1 was detected in morphologically abnormal oocytes of prepubertal ovaries. Through the immunofluorescent colocalization, UCH-L1 was shown concentrating in abnormal oocytes, and a parallel change in Jab1 was also seen. The affinity analysis confirmed the interaction between UCH-L1 and Jab1 in ovaries. These results suggest that UCH-L1 plays an important role, possibly in association with Jab1 and p27(Kipl), in selective elimination of abnormal oocytes during mouse prepubertal development.
Gu
Yan-Qiong
YQ
Shanghai Medical College of Fudan University, Shanghai, China.
Chen
Qiu-Ju
QJ
Gu
Zheng
Z
Shi
Yan
Y
Yao
Yu-Wei
YW
Wang
Jian
J
Sun
Zhao-Gui
ZG
Tso
Jia-Ke
JK
D000818:Animals; D017209:Apoptosis; D005260:Female; D051379:Mice; D009865:Oocytes / Q000166:cytology*; D010053:Ovary / Q000201:enzymology*; D043222:Ubiquitin Thiolesterase / Q000378:metabolism*
D043222:Ubiquitin Thiolesterase