pubmed-article:1829675 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0079183 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0441471 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0033713 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C1621812 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0851827 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C1701901 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
pubmed-article:1829675 | lifeskim:mentions | umls-concept:C0337094 | lld:lifeskim |
pubmed-article:1829675 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:1829675 | pubmed:dateCreated | 1991-8-14 | lld:pubmed |
pubmed-article:1829675 | pubmed:abstractText | Exit from M phase, which requires cyclin degradation, is prevented from occurring in unfertilized eggs of vertebrates arrested at second meiotic metaphase due to a cytostatic factor recently identified as p39mos, the product of the proto-oncogene c-mos. Calpain can destroy both p39mos and cyclin in vitro in extracts prepared from metaphase-arrested Xenopus eggs, but only when free Ca2+ concentration is raised to the millimolar range. When free Ca2+ concentration is raised for only 30 s to the micromolar range, as occurs in physiological conditions after fertilization, cyclin degradation is induced, byt p39mos is not degraded. Cyclin proteolysis at micromolar free Ca2+, is not inhibited by calpastatin, and therefore does not involve calpain. A cyclin mutant modified in the destruction box is found to be resistant at micromolar, but not millimolar free Ca2+, suggesting that the ubiquitin pathway mediates cyclin degradation at micromolar Ca2+ concentration whereas calpain is involved at the millimolar level. A synthetic peptide which binds Ca(2+)-calmodulin with high affinity suppresses cyclin degradation at micromolar but not millimolar free Ca2+, and this only when it is present in the extract during the first 30 s after raising free Ca2+ concentration. The inhibition of the cyclin degradation pathway by the Ca(2+)-calmodulin binding peptide can be overcome by adding calmodulin. These results strongly suggest that a Ca(2+)-calmodulin process is required as an early event following fertilization to release the cyclin degradation pathway from inhibition in metaphase-arrested eggs. In contrast, p39mos degradation is not required. | lld:pubmed |
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pubmed-article:1829675 | pubmed:language | eng | lld:pubmed |
pubmed-article:1829675 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1829675 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1829675 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1829675 | pubmed:month | Aug | lld:pubmed |
pubmed-article:1829675 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:GalboHH | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:DoréeMM | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:CavadoreJ CJC | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:DevaultAA | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:LorcaTT | lld:pubmed |
pubmed-article:1829675 | pubmed:author | pubmed-author:FesquetDD | lld:pubmed |
pubmed-article:1829675 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1829675 | pubmed:volume | 10 | lld:pubmed |
pubmed-article:1829675 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1829675 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1829675 | pubmed:pagination | 2087-93 | lld:pubmed |
pubmed-article:1829675 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:1829675 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1829675 | pubmed:articleTitle | Degradation of the proto-oncogene product p39mos is not necessary for cyclin proteolysis and exit from meiotic metaphase: requirement for a Ca(2+)-calmodulin dependent event. | lld:pubmed |
pubmed-article:1829675 | pubmed:affiliation | CNRS and INSERM, BP 505, Montpellier, France. | lld:pubmed |
pubmed-article:1829675 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1829675 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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