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Updated: Jun 23, 2026

Whole Ovary Immunofluorescence, Clearing, and Multiphoton Microscopy for Quantitative 3D Analysis of the Developing Ovarian Reserve in Mouse
Published on: September 3, 2021
Ubiquitin carboxyl-terminal hydrolase L1 contributes to the oocyte selective elimination in prepubertal mouse ovaries
Yan-Qiong Gu1, Qiu-Ju Chen, Zheng Gu
1Shanghai Medical College of Fudan University, Shanghai, China.
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.
Insights
Abnormal oocyte elimination during mouse development involves Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1). Increased UCH-L1 expression correlates with the removal of defective oocytes, suggesting its crucial role in ovarian development.
Area of Science:
- Reproductive Biology
- Cellular Biology
- Developmental Biology
Background:
- The ubiquitin system regulates apoptosis through protein degradation.
- Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) is implicated in apoptosis, particularly in spermatogenesis.
- Selective elimination of abnormal oocytes is critical for proper ovarian development.
Purpose of the Study:
- To investigate the role of UCH-L1 in the elimination of abnormal oocytes during prepubertal mouse ovary development.
- To examine the changes in follicular pool and UCH-L1 expression during this critical period.
- To explore the association of UCH-L1 with other proteins like Jab1 and p27(Kipl) in oocyte apoptosis.
Main Methods:
- Immunohistochemical techniques were used to assess follicular numbers and UCH-L1 expression in prepubertal mouse ovaries.
- Immunofluorescent colocalization was employed to study the localization of UCH-L1 and Jab1 in oocytes.
- Affinity analysis was performed to confirm the interaction between UCH-L1 and Jab1.
Main Results:
- A significant decrease in the follicular pool was observed between postnatal days 21 and 28.
- UCH-L1 protein expression increased during this period, particularly in morphologically abnormal oocytes.
- UCH-L1 was found to concentrate in abnormal oocytes, with parallel changes observed in Jab1, and a confirmed interaction between UCH-L1 and Jab1.
Conclusions:
- UCH-L1 plays a significant role in the selective elimination of abnormal oocytes during prepubertal mouse development.
- The function of UCH-L1 in oocyte apoptosis may involve interactions with Jab1 and p27(Kipl).
- These findings contribute to understanding the molecular mechanisms governing oocyte quality control in early ovarian development.
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