Expressions of ovarian function-related proteins in ovarian follicles in different development stages and their significances / 吉林大学学报(医学版)

Objective:To detect the expressions of ovarian function-related proteins in the ovarian follicles in different development stages,and to explore their roles and significances in the regulation of follicular development and ovarian function. Methods:The ovarian tissue containing primordial,primary,secondary follicles,mature follicles, atretic follicles and corpus albicans of the woman in the childbearing age was selected. Immunohisto chemical analysis was used to detect the expressions of Glyoxal enzyme I (glyoxalase I),ubiquitin carboxy-terminal hydrolase L1 (UCH-L1),heat shock protein 27 (HSP27),serum amyloid P (SAP)proteins in the ovarian follicles in different stages.The expression intensities of these proteins were compared.Results:The expression intensities of Glyoxalase I and UCH-L1 in the granulosa cells and theca cells of secondary follicles and marure follicles were strong,which were higher than those in the cytoplasm of primordial and primary follicles.The expression intensities of HSP27 in the cytoplasm of primordial and primary follicles were strong,which were higher than those in the granulosa cells and theca cells of secondary follicles and marure follicles.The expression intensities of Glyoxalase I and HSP27 in the atretic follicles were strong,which were higher than that in the growth follicles. The expressions of SAP were positive in the primordial,primary follicles,secondary and mature follicles and the expression intensities were not different.The expressions of four proteins in the corpus albicans did not express. Conclusion:The high expression of UCH-L1 and low expression of HSP27 are associated with the mature and development of follicles;the high expressions of Glyoxalase I and HSP27 are associated with the follicular atresia and ovarian failure.

Ubiquitin C-terminal Hydrolases L1:Physiological and Pathological Significance / 生物化学与生物物理进展

UCH-L1(ubiquitin carboxy-terminal hydrolases L1)is a member of the carboxyl-terminal ubiquitin hydrolase family,naturally,that there is hydrolase activity,however,and that there is ligase acitivity,which is different from the other members of UCHs.UCH-L1 hydrolase activity could keep the pool of free ubiquitin and compromise the ubiquitin-dependent degradation pathway,while UCH-L1 dimerizational-dependent,ubiquityl ligase activity could produce undegradable,K63-linked polyubiquitin chains that could inhibit proteasomal activity.Therefore,UCH-L1 is involved in the more diverse physiological activities,including neuron formation,gonadal development and fertilization.Mutation of UCH-L1 is linked to the neurodegenerative diseases,such as Parkinson's disease.Moreover,abnormal expression of UCH-L1 is response to carcinogenesis in many tissue such as thyroid lung.