| First Author | Sekiguchi S | Year | 2006 |
| Journal | Am J Pathol | Volume | 169 |
| Issue | 5 | Pages | 1722-9 |
| PubMed ID | 17071595 | Mgi Jnum | J:114649 |
| Mgi Id | MGI:3689663 | Doi | 10.2353/ajpath.2006.060301 |
| Citation | Sekiguchi S, et al. (2006) Localization of ubiquitin C-terminal hydrolase l1 in mouse ova and its function in the plasma membrane to block polyspermy. Am J Pathol 169(5):1722-9 |
| abstractText | 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. |
