Phosphorylation of MAP kinase and p90rsk and its regulation during in vitro maturation of cumulus-enclosed rabbit oocytes.
Numerous studies have demonstrated that activation of the mitogen-activated protein (MAP) kinase is involved in the maturation of oocytes. In this study, the expression and phosphorylation of MAP kinase and p90rsk, one of the substrates of MAP kinase, during rabbit oocyte maturation were studied. The results showed that MAP kinase phosphorylation began to occur after germinal vesicle breakdown (GVBD) and the active form was maintained until metaphase II. p90rsk was also activated after GVBD following MAP kinase activation. Immunofluorescent analysis showed that p90rsk was enriched in the nuclear area after GVBD and was gradually localised to the spindle. When GVBD was inhibited by increased cAMP or decreased protein kinase C activity, the phosphorylation of both MAP kinase and p9rsk was blocked. Our data suggest that (1) MAP kinase/p90rsk activation is not necessary for GVBD, but plays an important role in the post-GVBD events including spindle assembly in rabbit oocytes; and (2) MAP kinase/p9rsk activation is down-regulated by cAMP and up-regulated byprotein kinase C in cumulus-enclosed rabbit oocytes.
Yu
Hai-Quan
HQ
State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, PR China.
Bou
Shorgan
S
Chen
Da-Yuen
DY
Sun
Qing-Yuan
QY
D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D005260:Female; D005455:Fluorescent Antibody Technique; D066298:In Vitro Techniques; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism*; D009865:Oocytes / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D011817:Rabbits; D038744:Ribosomal Protein S6 Kinases, 90-kDa / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
D000242:Cyclic AMP; D038744:Ribosomal Protein S6 Kinases, 90-kDa; D011493:Protein Kinase C; D020928:Mitogen-Activated Protein Kinases