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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6716
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pubmed:dateCreated |
1999-2-18
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pubmed:databankReference |
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pubmed:abstractText |
Eukaryotic cells respond to many hormones and neurotransmitters with increased activity of the enzyme phospholipase C and a subsequent rise in the concentration of intracellular free calcium ([Ca2+]i). The increase in [Ca2+]i occurs as a result of the release of Ca2+ from intracellular stores and an influx of Ca2+ through the plasma membrane; this influx of Ca2+ may or may not be store-dependent. Drosophila transient receptor potential (TRP) proteins and some mammalian homologues (TRPC proteins) are thought to mediate capacitative Ca2+ entry. Here we describe the molecular mechanism of store-depletion-independent activation of a subfamily of mammalian TRPC channels. We find that hTRPC6 is a non-selective cation channel that is activated by diacylglycerol in a membrane-delimited fashion, independently of protein kinases C activated by diacylglycerol. Although hTRPC3, the closest structural relative of hTRPC6, is activated in the same way, TRPCs 1, 4 and 5 and the vanilloid receptor subtype 1 are unresponsive to the lipid mediator. Thus, hTRPC3 and hTRPC6 represent the first members of a new functional family of second-messenger-operated cation channels, which are activated by diacylglycerol.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-(6-((3-methoxyestra-1,3,5(10)-trie...,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Estrenes,
http://linkedlifedata.com/resource/pubmed/chemical/Histamine,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrrolidinones,
http://linkedlifedata.com/resource/pubmed/chemical/TRPC Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/TRPC3 cation channel,
http://linkedlifedata.com/resource/pubmed/chemical/TRPC6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
397
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-63
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9930701-Animals,
pubmed-meshheading:9930701-CHO Cells,
pubmed-meshheading:9930701-Calcium,
pubmed-meshheading:9930701-Calcium Channels,
pubmed-meshheading:9930701-Cell Membrane Permeability,
pubmed-meshheading:9930701-Cloning, Molecular,
pubmed-meshheading:9930701-Cricetinae,
pubmed-meshheading:9930701-Diglycerides,
pubmed-meshheading:9930701-Enzyme Inhibitors,
pubmed-meshheading:9930701-Estrenes,
pubmed-meshheading:9930701-Histamine,
pubmed-meshheading:9930701-Humans,
pubmed-meshheading:9930701-Ion Channel Gating,
pubmed-meshheading:9930701-Ion Channels,
pubmed-meshheading:9930701-Manganese,
pubmed-meshheading:9930701-Molecular Sequence Data,
pubmed-meshheading:9930701-Patch-Clamp Techniques,
pubmed-meshheading:9930701-Protein Kinase C,
pubmed-meshheading:9930701-Pyrrolidinones,
pubmed-meshheading:9930701-Second Messenger Systems,
pubmed-meshheading:9930701-TRPC Cation Channels,
pubmed-meshheading:9930701-Thapsigargin,
pubmed-meshheading:9930701-Type C Phospholipases
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pubmed:year |
1999
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pubmed:articleTitle |
Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol.
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pubmed:affiliation |
Institut für Pharmakologie, Universitätsklinikum Benjamin Franklin, Freie Universität Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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