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Neurochem.<\/jats:italic> (2012) <jats:bold>121<\/jats:bold>, 806\u2013817.<\/jats:p><\/jats:sec><jats:sec><jats:title>Abstract<\/jats:title><jats:p>Our previous studies have indicated that <jats:italic>de novo<\/jats:italic> ceramide synthesis plays a critical role in ethanol\u2010induced apoptotic neurodegeneration in the 7\u2010day\u2010old mouse brain. In this study, we examined whether the formation of sphingosine 1\u2010phosphate (S1P), a ceramide metabolite, is associated with this apoptotic pathway. Analyses of basal levels of S1P\u2010related compounds indicated that S1P, sphingosine, sphingosine kinase 2, and S1P receptor 1 increased significantly during postnatal brain development. In the 7\u2010day\u2010old mouse brain, sphingosine kinase 2 was localized mainly in neurons. Subcellular fractionation studies of the brain homogenates showed that sphingosine kinase 2 was enriched in the plasma membrane and the synaptic membrane\/synaptic vesicle fractions, but not in the nuclear and mitochondrial\/lysosomal fractions. Ethanol exposure in 7\u2010day\u2010old mice induced sphingosine kinase 2 activation and increased the brain level of S1P transiently 2\u20134\u2003h after exposure, followed by caspase 3 activation that peaked around 8\u2003h after exposure. Treatment with dimethylsphingosine, an inhibitor of sphingosine kinases, attenuated the ethanol\u2010induced caspase 3 activation and the subsequent neurodegeneration. These results indicate that ethanol activates sphingosine kinase 2, leading to a transient increase in S1P, which may be involved in neuroapoptotic action of ethanol in the developing brain.<\/jats:p><\/jats:sec>","DOI":"10.1111\/j.1471-4159.2012.07723.x","type":"journal-article","created":{"date-parts":[[2012,3,6]],"date-time":"2012-03-06T20:21:55Z","timestamp":1331065315000},"page":"806-817","source":"Crossref","is-referenced-by-count":13,"title":["Ethanol triggers sphingosine 1\u2010phosphate elevation along with neuroapoptosis in the developing mouse brain"],"prefix":"10.1111","volume":"121","author":[{"given":"Goutam","family":"Chakraborty","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mitsuo","family":"Saito","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Relish","family":"Shah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rui\u2010Fen","family":"Mao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Csaba","family":"Vadasz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariko","family":"Saito","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2012,4,12]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neulet.2009.12.070"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M306024200"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.ab.2003.11.018"},{"key":"e_1_2_7_5_1","doi-asserted-by":"crossref","first-page":"19824","DOI":"10.1016\/S0021-9258(19)88628-3","article-title":"Role of cadmium in activating nuclear protein kinase C and the enzyme binding to nuclear protein","volume":"267","author":"Block C.","year":"1992","journal-title":"J. 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