Dissociation of MAP kinase activation and MPF activation in hormone-stimulated maturation of Xenopus oocytes

Development ◽  
1999 ◽  
Vol 126 (20) ◽  
pp. 4537-4546 ◽  
Author(s):  
D.L. Fisher ◽  
T. Brassac ◽  
S. Galas ◽  
M. Doree
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Kinase Activity ◽  
Early Response ◽  
Meiotic Maturation ◽  
Cdc2 Kinase ◽  
Kinase Activation ◽  
Cell Cycle Activation ◽  
Map Kinase Phosphatase ◽  
Universal Mechanism

MAP kinase activation occurs during meiotic maturation of oocytes from all animals, but the requirement for MAP kinase activation in reinitiation of meiosis appears to vary between different classes. In particular, it has become accepted that MAP kinase activation is necessary for progesterone-stimulated meiotic maturation of Xenopus oocytes, while this is clearly not the case in other systems. In this paper, we demonstrate that MAP kinase activation in Xenopus oocytes is an early response to progesterone and can be temporally dissociated from MPF activation. We show that MAP kinase activation can be suppressed by treatment with geldanamycin or by overexpression of the MAP kinase phosphatase Pyst1. A transient and low-level early activation of MAP kinase increases the efficiency of cell cycle activation later on, when MAP kinase activity is no longer essential. Many oocytes can still undergo reinitiation of meiosis in the absence of active MAP kinase. Suppression of MAP kinase activation does not affect the formation or activation of Cdc2-cyclin B complexes, but reduces the level of active Cdc2 kinase. We discuss these findings in the context of a universal mechanism for meiotic maturation in oocytes throughout the animal kingdom.

scholarly journals Mitogen-activated protein kinase activation down-regulates a mechanism that inactivates cyclin B-cdc2 kinase in G2-arrested oocytes.

1997 ◽  
Vol 8 (2) ◽  
pp. 249-261 ◽  
Author(s):  
A Abrieu ◽  
M Dorée ◽  
A Picard
Keyword(s):  
Map Kinase ◽  
Xenopus Oocytes ◽  
Cyclin B ◽  
Mitogen Activated Protein Kinase ◽  
Cdc2 Kinase ◽  
Hormonal Stimulation ◽  
Germinal Vesicle Breakdown ◽  
Kinase Activation ◽  
Map Kinase Phosphatase ◽  
Mitogen Activated Protein

The G2 arrest of oocytes from frogs, clams, and starfish requires that preformed cyclin B-cdc2 complexes [prematuration-promoting factor (MPF)] be kept in an inactive form that is largely due to inhibitory phosphorylation of this pre-MPF. We have investigated the role of mitogen-activated protein (MAP) kinase in the activation of this pre-MPF. The cytoplasm of both frog and starfish oocytes contains an activity that can rapidly inactivate injected MPF. When the MAP kinase of G2-arrested starfish or Xenopus oocytes was prematurely activated by microinjection of c-mos or Ste-11 delta N fusion proteins, the rate and extent of MPF inactivation was much reduced. Both effects were suppressed by expression of the specific MAP kinase phosphatase Pyst 1. These results show that MAP kinase down-regulates a mechanism that inactivates cyclin B-cdc2 kinase in Xenopus oocytes. In starfish oocytes, however, MAP kinase activation occurs only after germinal vesicle breakdown, much after MPF activation. In this case, down-regulation of the cyclin B-cdc2 inhibiting pathway is a sensitive response to hormonal stimulation that does not require MAP kinase activation.

Microtubule and chromatin behavior follow MAP kinase activity but not MPF activity during meiosis in mouse oocytes

Development ◽  
1994 ◽  
Vol 120 (4) ◽  
pp. 1017-1025 ◽  
Author(s):  
M.H. Verlhac ◽  
J.Z. Kubiak ◽  
H.J. Clarke ◽  
B. Maro
Keyword(s):  
Cell Cycle ◽  
Myelin Basic Protein ◽  
Map Kinase ◽  
Kinase Activity ◽  
Basic Protein ◽  
Chromatin Condensation ◽  
Meiotic Maturation ◽  
Protein Kinase Activity ◽  
Microtubule Organization ◽  
Kinase Activation

Oocyte meiotic maturation is triggered by different stimuli (hormones, unknown signals through cell interactions) in different species. These stimuli indirectly lead to the activation of a major cell cycle regulating activity, the maturation promoting factor (MPF). Other factors, such as the product of the proto-oncogene c-mos or enzymes of the MAP kinase family, are also involved in the process of maturation. MAP kinase activation occurs during meiotic maturation in oocytes from different species with different kinetics. The relationships between MPF activation and MAP kinase activation have been well studied in species such as clam and Xenopus. In this paper, we study the precise timing of MAP kinase activation (as measured by phosphorylation of exogenous myelin basic protein and shifts in mobility of ERK 1 and ERK 2) versus MPF activation (as measured by phosphorylation of exogenous histone H1) during mouse oocyte maturation and, in parallel, morphological events such as changes in microtubule organization and chromatin condensation. We observed that MAP kinase activation was delayed after MPF activation and that this activity persisted throughout maturation whereas MPF activity dropped between the two meiotic metaphases. After parthenogenetic activation of ovulated eggs, MAP kinase inactivation was very slow compared to MPF inactivation. During the first mitotic cell cycle, a rise in myelin basic protein kinase activity at M-phase was observed but it was not related to MAP kinase activation. Furthermore, microtubules and chromatin remained in a metaphase-like state during the complete period of maturation (including the period between the two meiotic metaphases) and a few hours after activation.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals Effect of caffeine on meiotic maturation of porcine oocytes

Zygote ◽  
2004 ◽  
Vol 12 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Radomir Kren ◽  
Sugako Ogushi ◽  
Takashi Miyano
Keyword(s):  
Map Kinase ◽  
Calf Serum ◽  
Germinal Vesicle ◽  
Inhibitory Effect ◽  
Meiotic Maturation ◽  
Cdc2 Kinase ◽  
Kinase Activation ◽  
Prolonged Culture ◽  
Artificial Activation ◽  
Camp Levels

This study was conducted to evaluate the effect of caffeine on the meiotic maturation of porcine oocytes. Oocyte–cumulus complexes were collected from slaughterhouse-derived ovaries and cultured for 24, 32 or 48 h in medium 199 supplemented with 10% fetal calf serum, 10 μg/ml FSH, 50 μg/ml sodium pyruvate and 50 μg/ml gentamicin in the presence or absence of 2.5 mM caffeine. Caffeine inhibited the meiotic resumption of pig oocytes effectively after 24 h of culture, and 95.5% of oocytes were arrested at the germinal vesicle (GV) stage (control 17.8%, p<0.05). Prolonged culture with caffeine up to 32 h or 48 h, however, resulted in a significant decrease in the inhibitory effect (GV: 13.8% and 8.2%). The number of oocytes at metaphase II after 48 h of culture in the presence of caffeine was significantly lower than that in the control medium (65.3% vs 94.7%, p<0.05). The withdrawal of caffeine after 24 h of culture resulted in the resumption of meiotic maturation, and the oocytes reached metaphase II after 48 h. However, the ability of caffeine-treated oocytes to develop to blastocysts after artificial activation was lower than that of the control (5.5% vs 9.1%, p<0.05). Caffeine treatment significantly increased cAMP levels in the oocytes after 24 h of culture, while both Cdc2 kinase and MAP kinase activation were inhibited in the oocytes. These results suggest that caffeine, similarly to other purine derivatives, prolongs the meiotic arrest of porcine oocytes at the GV stage, perhaps by its action of increasing the cAMP level and by the suppression of Cdc2 kinase and MAP kinase activities in the oocytes.

scholarly journals Role of receptor desensitization, phosphatase induction and intracellular cyclic AMP in the termination of mitogen-activated protein kinase activity in UTP-stimulated EAhy 926 endothelial cells

1996 ◽  
Vol 315 (2) ◽  
pp. 563-569 ◽  
Author(s):  
Anne GRAHAM ◽  
Angela McLEES ◽  
Kevin MALARKEY ◽  
Gwyn W. GOULD ◽  
Robin PLEVIN
Keyword(s):  
Endothelial Cells ◽  
Protein Synthesis ◽  
Map Kinase ◽  
Kinase Activity ◽  
Mitogen Activated Protein Kinase ◽  
Receptor Desensitization ◽  
Kinase Activation ◽  
Map Kinase Phosphatase ◽  
Mitogen Activated Protein ◽  
Map Kinase Kinase

We have investigated the mechanisms that bring about the termination of mitogen-activated protein kinase (MAP kinase) activation in response to UTP in EAhy 926 endothelial cells. UTP-stimulated MAP kinase activity was transient, returning to basal values by 60 min. At this time MAP kinase activation was desensitized; re-application of UTP did not further activate MAP kinase, full re-activation of MAP kinase being only apparent after a 1–2 h wash period. However, activation of MAP kinase by UTP could be sustained beyond 60 min by preincubation of the cells with the protein synthesis inhibitor cycloheximide. UTP also stimulated expression of MAP kinase phosphatase-1 and this was abolished after pretreatment with cycloheximide. Pretreatment of cells with forskolin abolished the initial activation of MAP kinase kinase or c-Raf-1 by UTP, but only affected MAP kinase activity during prolonged stimulation. The effect of forskolin on prolonged MAP kinase activation was also prevented by cycloheximide. These results suggest that the termination of MAP kinase activity in response to UTP involves a number of interacting mechanisms including receptor desensitization and the induction of a phosphatase. However, several pieces of evidence do not support a major role for MAP kinase phosphatase-1 in termination of the MAP kinase signal. Raising intracellular cyclic AMP may also be involved but only after an initial protein-synthesis step and by a mechanism that does not involve the inactivation of c-Raf-1 or MAP kinase kinase.

scholarly journals MAP kinase does not inactivate, but rather prevents the cyclin degradation pathway from being turned on in Xenopus egg extracts

1996 ◽  
Vol 109 (1) ◽  
pp. 239-246 ◽  
Author(s):  
A. Abrieu ◽  
T. Lorca ◽  
J.C. Labbe ◽  
N. Morin ◽  
S. Keyse ◽  
...  
Keyword(s):  
Map Kinase ◽  
Degradation Pathway ◽  
Cdc2 Kinase ◽  
Vitro Assay ◽  
Kinase Activation ◽  
Egg Extracts ◽  
Dependent Protein ◽  
Xenopus Egg ◽  
Xenopus Egg Extracts

Unfertilized frog eggs arrest at the second meiotic metaphase, due to cytostatic activity of the c-mos proto-oncogene (CSF). MAP kinase has been proposed to mediate CSF activity in suppressing cyclin degradation. Using an in vitro assay to generate CSF activity, and recombinant CL 100 phosphatase to inactivate MAP kinase, we confirm that the c-mos proto-oncogene blocks cyclin degradation through MAP kinase activation. We further show that for MAP kinase to suppress cyclin degradation, it must be activated before cyclin B-cdc2 kinase has effectively promoted cyclin degradation. Thus MAP kinase does not inactivate, but rather prevents the cyclin degradation pathway from being turned on. Using a constitutively active mutant of Ca2+/calmodulin dependent protein kinase II, which mediates the effects of Ca2+ at fertilization, we further show that the kinase can activate cyclin degradation in the presence of both MPF and the c-mos proto-oncogene without inactivating MAP kinase.

scholarly journals Mice lacking MAP kinase phosphatase-1 have enhanced MAP kinase activity and resistance to diet-induced obesity

2006 ◽  
Vol 4 (1) ◽  
pp. 61-73 ◽  
Author(s):  
J. Julie Wu ◽  
Rachel J. Roth ◽  
Ethan J. Anderson ◽  
Eun-Gyoung Hong ◽  
Mi-Kyung Lee ◽  
...  
Keyword(s):  
Map Kinase ◽  
Kinase Activity ◽  
Diet Induced Obesity ◽  
Map Kinase Phosphatase

scholarly journals Tyrosine phosphorylation and activation of homologous protein kinases during oocyte maturation and mitogenic activation of fibroblasts.

1991 ◽  
Vol 11 (5) ◽  
pp. 2517-2528 ◽  
Author(s):  
J Posada ◽  
J Sanghera ◽  
S Pelech ◽  
R Aebersold ◽  
J A Cooper
Keyword(s):  
Cell Cycle ◽  
Map Kinase ◽  
Tyrosine Phosphorylation ◽  
Oocyte Maturation ◽  
Mammalian Cells ◽  
Map Kinases ◽  
Kinase Activity ◽  
Mitotic Cell ◽  
Meiotic Maturation ◽  
Sea Star

Meiotic maturation of Xenopus and sea star oocytes involves the activation of a number of protein-serine/threonine kinase activities, including a myelin basic protein (MBP) kinase. A 44-kDa MBP kinase (p44mpk) purified from mature sea star oocytes is shown here to be phosphorylated at tyrosine. Antiserum to purified sea star p44mpk was used to identify antigenically related proteins in Xenopus oocytes. Two tyrosine-phosphorylated 42-kDa proteins (p42) were detected with this antiserum in Xenopus eggs. Xenopus p42 chromatographs with MBP kinase activity on a Mono Q ion-exchange column. Tyrosine phosphorylation of Xenopus p42 approximately parallels MBP kinase activity during meiotic maturation. These results suggest that related MBP kinases are activated during meiotic maturation of Xenopus and sea star oocytes. Previous studies have suggested that Xenopus p42 is related to the mitogen-activated protein (MAP) kinases of culture mammalian cells. We have cloned a MAP kinase relative from a Xenopus ovary cDNA library and demonstrate that this clone encodes the Xenopus p42 that is tyrosine phosphorylated during oocyte maturation. Comparison of the sequences of Xenopus p42 and a rat MAP kinase (ERK1) and peptide sequences from sea star p44mpk indicates that these proteins are close relatives. The family members appear to be tyrosine phosphorylated, and activated, in different contexts, with the murine MAP kinase active during the transition from quiescence to the G1 stage of the mitotic cell cycle and the sea star and Xenopus kinases being active during M phase of the meiotic cell cycle.

scholarly journals Phosphatidylinositol 3-kinase activity is important for progesterone-induced Xenopus oocyte maturation.

1993 ◽  
Vol 13 (11) ◽  
pp. 6661-6666 ◽  
Author(s):  
A J Muslin ◽  
A Klippel ◽  
L T Williams
Keyword(s):  
Oocyte Maturation ◽  
Kinase Activity ◽  
Sh2 Domain ◽  
Pi3 Kinase ◽  
Meiotic Maturation ◽  
Xenopus Laevis Oocytes ◽  
Phosphatidylinositol 3 Kinase ◽  
Kinase Activation ◽  
Phosphatidylinositol 3

In somatic cells, phosphatidylinositol 3-kinase (PI3 kinase) is a critical intermediary in growth factor-induced mitogenesis. We have examined the role of this enzyme in meiotic maturation of Xenopus laevis oocytes. PI3 kinase activity was present in immunoprecipitates of the p85 subunit of PI3 kinase from immature oocytes and markedly increased following progesterone stimulation. Injection of bacterially expressed protein corresponding to the C-terminal SH2 domain of p85 (SH2-C) inhibited progesterone-induced PI3 kinase activation and meiotic maturation. Injection of protein corresponding to the N-terminal SH2 domain or the SH3 domain of p85 did not inhibit PI3 kinase activation or maturation. SH2-C did not inhibit oocyte maturation induced by c-mos RNA injection. In addition, radiolabelled SH2-C was used to probe oocyte lysates, revealing that a novel 200-kDa protein bound to SH2-C. This protein may be an important mediator of progesterone-induced lipid metabolism in oocytes.

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