Source:http://linkedlifedata.com/resource/pubmed/id/16912081
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
Pt 17
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| pubmed:dateCreated |
2006-8-25
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| pubmed:abstractText |
In the ciliate Paramecium, a variety of well characterized processes are regulated by Ca2+, e.g. exocytosis, endocytosis and ciliary beat. Therefore, among protozoa, Paramecium is considered a model organism for Ca2+ signaling, although the molecular identity of the channels responsible for the Ca2+ signals remains largely unknown. We have cloned - for the first time in a protozoan - the full sequence of the gene encoding a putative inositol (1,4,5)-trisphosphate (Ins(1,4,5)P3) receptor from Paramecium tetraurelia cells showing molecular characteristics of higher eukaryotic cells. The homologously expressed Ins(1,4,5)P3-binding domain binds [3H]Ins(1,4,5)P3, whereas antibodies unexpectedly localize this protein to the osmoregulatory system. The level of Ins(1,4,5)P3-receptor expression was reduced, as shown on a transcriptional level and by immuno-staining, by decreasing the concentration of extracellular Ca2+ (Paramecium cells rapidly adjust their Ca2+ level to that in the outside medium). Fluorochromes reveal spontaneous fluctuations in cytosolic Ca2+ levels along the osmoregulatory system and these signals change upon activation of caged Ins(1,4,5)P3. Considering the ongoing expulsion of substantial amounts of Ca2+ by the osmoregulatory system, we propose here that Ins(1,4,5)P3 receptors serve a new function, i.e. a latent, graded reflux of Ca2+ to fine-tune [Ca2+] homeostasis.
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Inositol 1,4,5-Trisphosphate...,
http://linkedlifedata.com/resource/pubmed/chemical/Lithium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
119
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3705-17
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| pubmed:meshHeading |
pubmed-meshheading:16912081-Amino Acid Sequence,
pubmed-meshheading:16912081-Animals,
pubmed-meshheading:16912081-Calcium,
pubmed-meshheading:16912081-Calcium Signaling,
pubmed-meshheading:16912081-Gene Expression Regulation,
pubmed-meshheading:16912081-Homeostasis,
pubmed-meshheading:16912081-Inositol 1,4,5-Trisphosphate,
pubmed-meshheading:16912081-Inositol 1,4,5-Trisphosphate Receptors,
pubmed-meshheading:16912081-Lithium Chloride,
pubmed-meshheading:16912081-Models, Molecular,
pubmed-meshheading:16912081-Molecular Sequence Data,
pubmed-meshheading:16912081-Paramecium tetraurelia,
pubmed-meshheading:16912081-Phylogeny,
pubmed-meshheading:16912081-Protein Structure, Tertiary,
pubmed-meshheading:16912081-Protozoan Proteins,
pubmed-meshheading:16912081-Rats,
pubmed-meshheading:16912081-Recombinant Fusion Proteins,
pubmed-meshheading:16912081-Sequence Alignment,
pubmed-meshheading:16912081-Water-Electrolyte Balance
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| pubmed:year |
2006
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| pubmed:articleTitle |
An Ins(1,4,5)P3 receptor in Paramecium is associated with the osmoregulatory system.
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| pubmed:affiliation |
Department of Biology, University of Konstanz, 78457 Konstanz, Germany. Eva.Landenburger@uni-konstanz.de
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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