Ubiquitin carboxyl-terminal hydrolase L1 contributes to the oocyte selective elimination in prepubertal mouse ovaries.
- Author:
Yan-Qiong GU
1
;
Qiu-Ju CHEN
;
Zheng GU
;
Yan SHI
;
Yu-Wei YAO
;
Jian WANG
;
Zhao-Gui SUN
;
Jia-Ke TSO
Author Information
1. Shanghai Medical College of Fudan University, Shanghai, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Apoptosis;
Female;
Mice;
Oocytes;
cytology;
Ovary;
enzymology;
Ubiquitin Thiolesterase;
metabolism
- From:
Acta Physiologica Sinica
2009;61(2):175-184
- CountryChina
- Language:English
-
Abstract:
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.
