2006 Volume 52 Issue 2 Pages 287-291
Protein phosphorylation on certain serine or threonine residues preceding proline (Ser/Thr-Pro) is a pivotal signaling mechanism in diverse cellular processes. Pin1 is a highly conserved enzyme that isomerizes only the phosphorylated Ser/Thr-Pro bonds in certain proteins, thereby inducing conformational changes. Although much protein is phosphorylated in the ovary, the role of Pin1 in the ovary is still unknown. The purpose of this study is to investigate the effects of gonadotropins on protein and mRNA expression of Pin1 in mice ovaries. Quantitative PCR analysis showed that the expression of Pin1 mRNA significantly increased in the ovaries of equine chorionic gonadotropin (eCG)-treated mice compared with those of untreated mice (P<0.05). However, human chorionic gonadotropin (hCG) attenuated the expression of Pin1 mRNA increased by eCG. The protein level of Pin1 showed the same tendency as the expression of mRNA. The mRNA expression of E2F transcription factor, which controlled the expression of Pin1, was significantly decreased in the eCG-treated ovaries compared with the controls (P<0.05). These observations suggest that gonadotropins may regulate the expression of Pin1 without E2F transcription factor, indicating that Pin1 might be an important factor for protein signal transduction during follicular development.
