Source:http://linkedlifedata.com/resource/pubmed/id/18664571
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
41
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pubmed:dateCreated |
2008-10-6
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pubmed:abstractText |
The Ca(2+)-binding protein DREAM regulates gene transcription and Kv potassium channels in neurons but has also been claimed to interact with presenilins, which are involved in the generation of beta-amyloid and in the regulation of the Ca(2+) content in the endoplasmic reticulum. The role of DREAM in Ca(2+) homeostasis was thus explored in SH-SY5Y cells stably or transiently overexpressing DREAM or a Ca(2+)-insensitive mutant of it. The overexpression of DREAM had transcriptional and post-transcriptional effects. Endoplasmic reticulum Ca(2+) and capacitative Ca(2+) influx were reduced in stably expressing cells. The previously shown down-regulation of Na(+)/Ca(2+) exchanger 3 expression was confirmed; it could cause a local increase of subplasma membrane Ca(2+) and thus inhibit capacitative Ca(2+) influx. DREAM up-regulated the expression of the inositol 1,4,5-trisphosphate receptor and could thus increase the unstimulated release of Ca(2+) through it. The transient coexpression of DREAM and presenilin potentiated the decrease of endoplasmic reticulum Ca(2+) observed in presenilin-overexpressing cells. This could be due to a direct effect of DREAM on presenilin as the two proteins interacted in a Ca(2+)-independent fashion.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/KCNIP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Kv Channel-Interacting Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium Channels, Voltage-Gated,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27494-503
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18664571-Amyloid beta-Peptides,
pubmed-meshheading:18664571-Calcium,
pubmed-meshheading:18664571-Calcium Signaling,
pubmed-meshheading:18664571-Cell Line, Tumor,
pubmed-meshheading:18664571-Endoplasmic Reticulum,
pubmed-meshheading:18664571-Humans,
pubmed-meshheading:18664571-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:18664571-Kv Channel-Interacting Proteins,
pubmed-meshheading:18664571-Mutation,
pubmed-meshheading:18664571-Neurons,
pubmed-meshheading:18664571-Potassium Channels, Voltage-Gated,
pubmed-meshheading:18664571-Presenilins,
pubmed-meshheading:18664571-Repressor Proteins,
pubmed-meshheading:18664571-Transcription, Genetic
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pubmed:year |
2008
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pubmed:articleTitle |
Interplay of the Ca2+-binding protein DREAM with presenilin in neuronal Ca2+ signaling.
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pubmed:affiliation |
Department of Biochemistry, University of Padova, Padova 35131, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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