EVALUATION OF OOCYTES QUALITY THOROUGH ANALYSIS OF APOPTOTIC SIGNAL TRANSDUCTION IN FOLLICLES.

本实验用凋亡信号转导系统Fas-Fas配体（Fas-Fas ligand）研究了排卵前雌性小鼠（B6 C3系）卵巢中的凋亡信号转导系统。Fas抗原位于颗粒细胞膜表面。Fas配体与Fas抗原结合后，细胞内信号转导开始。小鼠闭锁卵泡中的卵母细胞表面未见Fas抗原。Fas抗原和Fas配体表达于颗粒细胞表面。原位杂交显示凋亡颗粒细胞产生Fas抗原而不产生Fas配体。Fas配体在卵母细胞中产生。因此，卵母细胞是卵泡发育或闭锁卵泡的关键。蛋白C激酶介导颗粒细胞的细胞内信号转导。提示有其他信号转导途径，但阻断蛋白C激酶的细胞内信号转导途径对卵泡发育无作用。p38蛋白有α、β、γ和δ 4种亚型。在这些组中，p38α刺激卵泡凋亡，而p38β不刺激。进一步研究闭锁卵泡凋亡的细胞内信号转导机制是必要的。

Fas-Fas ligand which is a major system of signal transduction of apoptosis was used for elucidation of apoptotic system in ovaries from preovulatory female mice (B6C3 strain). Fas antigen is on the surface of granulosa cell membrane. Intracellular signal transduction starts after Fas ligand combines to Fas antigen. Fas antigen was not found on the surface of oocyte even in the atretic follicle of mouse. Otherwhile Fas antigen and Fas ligand was found on the surface of granulosa cells. In situ hybridization showed that apoptotic granulosa cells producted Fas antigen and not Fas ligand. Fas ligands was producted in oocyte. Therefore oocytes hold the key to follicle development or atretic follicles. Protein C kinase mediates intracellular signal transduction of granulosa cells. Other signal transduction was suggested while blockage of intracellular transduction via protein C kinase was no use in follicle development. There was p38 protein which contains 4 kinds of isoforms (α,β,γ and δ). In those groups, p38α stimulates follicular apoptosis but p38β does not. Further investigation is necessary for detection of all of intracellular signal transduction for apoptosis in atretic follicles.