title: Histone H1 kinase activity, germinal vesicle breakdown and M phase entry in mouse oocytes.
abstract: Meiotic reinitiation of the mouse oocyte is characterized by a slow entry into metaphase I, beginning with germinal vesicle breakdown and ending with spindle formation. It is accompanied by a cascade of protein kinases and phosphatases increasing protein phosphorylation. The activation of histone H1 kinase and that of the mitogen-activated protein kinase p42 have been compared during spontaneous or okadaic acid-induced meiotic reinitiation. In spontaneously maturing oocytes, histone H1 kinase activity increases before germinal vesicle breakdown (2-fold), in a protein synthesis-independent manner. It is associated with the disappearance of the upper migrating form of p34cdc2, which, in our system, seems to represent the tyrosine phosphorylated form. Following germinal vesicle breakdown, histone H1 kinase activity culminates (8-fold) in metaphase I and requires protein synthesis. Activation by phosphorylation of p42MAPK is observed as a permanent shift upward-migrating form and by its myelin basic protein kinase activity. It occurs after germinal vesicle breakdown and depends on protein synthesis. In contrast, no increase of histone H1 kinase is detectable in oocytes induced to reinitiate meiosis by a transient inhibition of okadaic acid-sensitive phosphatase(s), either before germinal vesicle breakdown or during the following 7 hours of culture. A slight increase is nevertheless evident after 17 hours, when oocytes are arrested with an abnormal metaphase I spindle. The upper migrating form of p34cdc2 is present for 8 hours. The activation of p42MAPK begins before germinal vesicle breakdown.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: Department of Obstetrics and Gynaecology, Hôpital Cantonal Universitaire, Geneva, Switzerland.
authors.forename: A C
authors.initials: AC
authors.lastname: Gavin
authors.forename: J C
authors.initials: JC
authors.lastname: Cavadore
authors.forename: S
authors.initials: S
authors.lastname: Schorderet-Slatkine
mesh_terms: D000818:Animals; D016203:CDC2 Protein Kinase / Q000378:metabolism; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D002453:Cell Cycle / Q000502:physiology*; D003513:Cycloheximide / Q000494:pharmacology; D004789:Enzyme Activation; D004988:Ethers, Cyclic / Q000494:pharmacology; D005260:Female; D038362:Glycogen Synthase Kinase 3; D066298:In Vitro Techniques; D008540:Meiosis; D051379:Mice; D008938:Mitosis / Q000502:physiology; D019319:Okadaic Acid; D009865:Oocytes / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology; D006656:Protamine Kinase / Q000378:metabolism*; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors
chemical_list: D004988:Ethers, Cyclic; D019319:Okadaic Acid; D003513:Cycloheximide; D006656:Protamine Kinase; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D016203:CDC2 Protein Kinase; D038362:Glycogen Synthase Kinase 3; D017027:Protein Tyrosine Phosphatases