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(American Journal of Pathology. 2006;169:1722-1729.)
© 2006 American Society for Investigative Pathology
DOI: 10.2353/ajpath.2006.060301

Localization of Ubiquitin C-Terminal Hydrolase L1 in Mouse Ova and Its Function in the Plasma Membrane to Block Polyspermy

Satoshi Sekiguchi*, Jungkee Kwon{dagger}{ddagger}, Etsuko Yoshida§, Hiroko Hamasaki*, Shizuko Ichinose, Makoto Hideshima*, Mutsuki Kuraoka*, Akio Takahashi{dagger}, Yoshiyuki Ishii*, Shigeru Kyuwa*, Keiji Wada{dagger} and Yasuhiro Yoshikawa*

From the Department of Biomedical Science,* Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan; the Department of Degenerative Neurological Disease{dagger} and the Section of Laboratory Animal Resources,§ National Institute of Neuroscience, National Center of Neurology and Psychiatry, Tokyo, Japan; the Instrumental Analysis Research Center for Life Science, Tokyo Medical and Dental University, Tokyo, Japan; and the Laboratory of Animal Medicine,{ddagger} College of Veterinary Medicine, Chonbuk National University, Jeonju, Korea

Protein degradation is essential for oogenesis and embryogenesis. The ubiquitin-proteasome system regulates many cellular processes via the rapid degradation of specific proteins. Ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) is exclusively expressed in neurons, testis, ovary, and placenta, each of which has unique biological activities. However, the functional role of UCH-L1 in mouse oocytes remains unknown. Here, we report the expression pattern of UCH-L1 and its isozyme UCH-L3 in mouse ovaries and embryos. Using immunocytochemistry, UCH-L1 was selectively detected on the plasma membrane, whereas UCH-L3 was mainly detected in the cytoplasm, suggesting that these isozymes have distinct functions in mouse eggs. To further investigate the functional role of UCH-L1 in mouse eggs, we analyzed the fertilization rate of UCH-L1-deficient ova of gad female mice. Female gad mice had a significantly increased rate of polyspermy in in vitro fertilization assays, although the rate of fertilization did not differ significantly from wild-type mice. In addition, the litter size of gad female mice was significantly reduced compared with wild-type mice. These results may identify UCH-L1 as a candidate for a sperm-oocyte interactive binding or fusion protein on the plasma membrane that functions during the block to polyspermy in mouse oocytes.




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