Source:http://linkedlifedata.com/resource/pubmed/id/15550678
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-2-18
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pubmed:abstractText |
TRPM3, a member of the melastatin-like transient receptor potential channel subfamily (TRPM), is predominantly expressed in human kidney and brain. TRPM3 mediates spontaneous Ca2+ entry and nonselective cation currents in transiently transfected human embryonic kidney 293 cells. Using measurements with the Ca2+-sensitive fluorescent dye fura-2 and the whole-cell patch-clamp technique, we found that D-erythro-sphingosine, a metabolite arising during the de novo synthesis of cellular sphingolipids, activated TRPM3. Other transient receptor potential (TRP) channels tested [classic or canonical TRP (TRPC3, TRPC4, TRPC5), vanilloid-like TRP (TRPV4, TRPV5, TRPV6), and melastatin-like TRP (TRPM2)] did not significantly respond to application of sphingosine. Sphingosine-induced TRPM3 activation was not mediated by inhibition of protein kinase C, depletion of intracellular Ca2+ stores, and intracellular conversion of sphingosine to sphingosine-1-phosphate. Although sphingosine-1-phosphate and ceramides had no effect, two structural analogs of sphingosine, dihydro-D-erythro-sphingosine and N,N-dimethyl-D-erythro-sphingosine, also activated TRPM3. Sphingolipids, including sphingosine, are known to have inhibitory effects on a variety of ion channels. Thus, TRPM3 is the first ion channel activated by sphingolipids.
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pubmed:commentsCorrections | |
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/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Sphingosine,
http://linkedlifedata.com/resource/pubmed/chemical/TRPM Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/TRPM3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/erythro-(2R,3S)-sphingosine
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0026-895X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
798-805
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pubmed:dateRevised |
2007-10-30
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pubmed:meshHeading |
pubmed-meshheading:15550678-Calcium,
pubmed-meshheading:15550678-Cell Line,
pubmed-meshheading:15550678-Humans,
pubmed-meshheading:15550678-Ion Channels,
pubmed-meshheading:15550678-Kidney,
pubmed-meshheading:15550678-Kinetics,
pubmed-meshheading:15550678-Membrane Potentials,
pubmed-meshheading:15550678-Patch-Clamp Techniques,
pubmed-meshheading:15550678-Recombinant Proteins,
pubmed-meshheading:15550678-Sphingolipids,
pubmed-meshheading:15550678-Sphingosine,
pubmed-meshheading:15550678-TRPM Cation Channels,
pubmed-meshheading:15550678-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Activation of the melastatin-related cation channel TRPM3 by D-erythro-sphingosine [corrected].
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pubmed:affiliation |
Institut für Pharmakologie, Charité Campus Benjamin Franklin, Thielallee 69-73, 14195 Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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