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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1999-11-19
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin B,
http://linkedlifedata.com/resource/pubmed/chemical/Dual Specificity Phosphatase 6,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Maturation-Promoting Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Progesterone,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/geldanamycin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0950-1991
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
126
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4537-46
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10498688-Animals,
pubmed-meshheading:10498688-Benzoquinones,
pubmed-meshheading:10498688-CDC2 Protein Kinase,
pubmed-meshheading:10498688-Cyclin B,
pubmed-meshheading:10498688-Dual Specificity Phosphatase 6,
pubmed-meshheading:10498688-Enzyme Activation,
pubmed-meshheading:10498688-Female,
pubmed-meshheading:10498688-Insulin,
pubmed-meshheading:10498688-Lactams, Macrocyclic,
pubmed-meshheading:10498688-Maturation-Promoting Factor,
pubmed-meshheading:10498688-Meiosis,
pubmed-meshheading:10498688-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10498688-Oocytes,
pubmed-meshheading:10498688-Progesterone,
pubmed-meshheading:10498688-Protein Tyrosine Phosphatases,
pubmed-meshheading:10498688-Quinones,
pubmed-meshheading:10498688-Xenopus
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pubmed:year |
1999
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pubmed:articleTitle |
Dissociation of MAP kinase activation and MPF activation in hormone-stimulated maturation of Xenopus oocytes.
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pubmed:affiliation |
CNRS-CRBM, 34293 Montpellier Cedex 5, France. fisher@crbm.cnrs-mop. fr.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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