Morphological dynamics of cumulus-oocyte complex during oocyte maturation.
The recent advances on the cytoplasmic regulators of the induction of germinal vesicle break down, maturation and degeneration of oocytes, and glycosaminoglycan composition during cumulus expansion of cumulus-oocyte complexes are discussed. A) Inactive mitogen-activated protein kinases (MAPKs) are present in the oocytes at germinal vesicle (GV) stage, and are activated with germinal vesicle breakdown (GVBD), and remain highly active throughout maturation in porcine oocytes. Inactive MAPKs are localized in the cytoplasm of GV-arrested oocytes and active MAPKs were detected in the GV just before GVBD. B) Cumulus expansion of porcine cumulus-oocyte complexes (COCs) was reduced by oocy tectomy. The profile of total glycosaminoglycan synthesis was attributed to hyaluronic acid rather than chondroitin sulfate in intact COCs and oocytectomy reduced hyaluronic acid synthesis. C) The abnormalities of chromosomes and alpha-tubulin morphology were observed in the oocytes of c-mos deficient mice. MAPK activity of c-mos deficient oocytes did not significantly fluctuate throughout maturation and was clearly lower than that of wild-type oocytes. One of the most drastic abnormalities in c-mos knockout mouse oocytes was their entrance into the interphase instead of second meiosis after first polar body emission. D) Reverse transcriptase/polymerase chain reaction-Southern blot hybridization demonstrated positive expression of Fas in intraovarian mouse oocytes. In contrast, expression of Fas ligand was detected in granulosa cells. These findings were histologically confirmed by in situ hybridization with Fas- and FasL-specific probes. Co-culture of intact and zona-free eggs and granulosa cells demonstrated positive TUNEL staining only zona-free eggs.
Sato
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Animal Reproduction Unit, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan. eimei@bios.tohoku.ac.jp
D000818:Animals; D017209:Apoptosis / Q000502:physiology; D002467:Cell Nucleus / Q000201:enzymology / Q000502:physiology*; D002478:Cells, Cultured; D003593:Cytoplasm / Q000201:enzymology / Q000502:physiology; D053222:Fas Ligand Protein; D005260:Female; D006025:Glycosaminoglycans / Q000378:metabolism; D008540:Meiosis; D008562:Membrane Glycoproteins / Q000378:metabolism; D051379:Mice; D018345:Mice, Knockout; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D009865:Oocytes / Q000166:cytology / Q000201:enzymology / Q000254:growth & development*; D013552:Swine / Q000502:physiology; D015044:Zona Pellucida / Q000201:enzymology / Q000502:physiology*
D053222:Fas Ligand Protein; C505658:Fasl protein, mouse; D006025:Glycosaminoglycans; D008562:Membrane Glycoproteins; D020928:Mitogen-Activated Protein Kinases