Activities of maturation-promoting factor (MPF) and mitogen-activated protein kinase (MAPK) are not required for the global histone deacetylation observed after germinal vesicle breakdown (GVBD) in porcine oocytes.
The acetylation of nuclear core histone has been suggested to work as an epigenetic mark for transmitting gene expression patterns to daughter cells. Global histone deacetylations, presumably involved in the reprogramming of the gene expression, have been observed after germinal vesicle breakdown (GVBD) in a cell cycle-dependent manner during meiotic maturation of mouse and porcine oocytes, although the regulation mechanism of histone deacetylation has not been studied well. In the present study, we examined the involvement of a crucial cell-cycle-regulator, maturation-promoting factor (MPF), and a meiosis-related kinase, mitogen-activated protein kinase (MAPK), in the global histone deacetylation during porcine oocyte maturation. In order to know whether the activities of MPF and MAPK were required, or the breakdown of GV membrane was sufficient, for the global histone deacetylation observed after GVBD, we artificially destroyed the GV membrane of the porcine immature oocytes. The artificial GV destruction (AGVD) induced histone deacetylation without the activation of MPF and MAPK. This deacetylation after AGVD was not affected by an MPF inhibitor, roscovitine, or an inhibitor of protein synthesis, cycloheximide, but was completely prevented by an inhibitor of histone deactylases (HDACs), trichostatine A. HDAC1 was present in the GV of the immature oocytes and localized on chromosomes after GVBD and AGVD. These results suggest that the MPF and MAPK activities were dispensable and the breakdown of the GV membrane was sufficient for the global histone deacetylation, which was catalyzed by HDAC activity.
Endo
Tsutomu
T
Laboratory of Applied Genetics, Graduate School of Agriculture and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Naito
Kunihiko
K
Kume
Sachi
S
Nishimura
Yukio
Y
Kashima
Koji
K
Tojo
Hideaki
H
D000107:Acetylation; D000818:Animals; D002843:Chromatin / Q000648:ultrastructure; D003513:Cycloheximide / Q000494:pharmacology; D004789:Enzyme Activation; D005260:Female; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006877:Hydroxamic Acids / Q000494:pharmacology; D015151:Immunoblotting / Q000379:methods; D007150:Immunohistochemistry / Q000379:methods; D016200:Maturation-Promoting Factor / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008540:Meiosis; D000090204:Mesothelin; D051379:Mice; D019950:Mitogen-Activated Protein Kinase 1 / Q000378:metabolism*; D009865:Oocytes / Q000502:physiology*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D011687:Purines / Q000494:pharmacology; D000077546:Roscovitine
D002843:Chromatin; D056572:Histone Deacetylase Inhibitors; D006657:Histones; D006877:Hydroxamic Acids; C000715528:Msln protein, mouse; D011500:Protein Synthesis Inhibitors; D011687:Purines; D000077546:Roscovitine; C012589:trichostatin A; D003513:Cycloheximide; D016200:Maturation-Promoting Factor; D019950:Mitogen-Activated Protein Kinase 1; D006655:Histone Deacetylases; D000090204:Mesothelin