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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6751
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pubmed:dateCreated |
1999-10-19
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pubmed:abstractText |
Polycystic kidney diseases are genetic disorders in which the renal parenchyma is progressively replaced by fluid-filled cysts. Two members of the polycystin family (polycystin-1 and -2) are mutated in autosomal dominant polycystic kidney disease (ADPKD), and polycystin-L is deleted in mice with renal and retinal defects. Polycystins are membrane proteins that share significant sequence homology, especially polycystin-2 and -L (50% identity and 71% similarity). The functions of the polycystins remain unknown. Here we show that polycystin-L is a calcium-modulated nonselective cation channel that is permeable to sodium, potassium and calcium ions. Patch-clamp experiments revealed single-channel activity with a unitary conductance of 137 pS. Channel activity was substantially increased when either the extracellular or intracellular calcium-ion concentration was raised, indicating that polycystin-L may act as a transducer of calcium-mediated signalling in vivo. Its large single-channel conductance and regulation by calcium ions distinguish it from other structurally related cation channels.
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pubmed:commentsCorrections |
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Chelating Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Egtazic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/PKD2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
23
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pubmed:volume |
401
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
383-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:10517637-Animals,
pubmed-meshheading:10517637-Calcium,
pubmed-meshheading:10517637-Calcium Channels,
pubmed-meshheading:10517637-Calcium Signaling,
pubmed-meshheading:10517637-Cations, Divalent,
pubmed-meshheading:10517637-Cell Membrane Permeability,
pubmed-meshheading:10517637-Chelating Agents,
pubmed-meshheading:10517637-Cloning, Molecular,
pubmed-meshheading:10517637-Egtazic Acid,
pubmed-meshheading:10517637-Electrophysiology,
pubmed-meshheading:10517637-Humans,
pubmed-meshheading:10517637-Membrane Glycoproteins,
pubmed-meshheading:10517637-Patch-Clamp Techniques,
pubmed-meshheading:10517637-Phosphoproteins,
pubmed-meshheading:10517637-Polycystic Kidney Diseases,
pubmed-meshheading:10517637-Receptors, Cell Surface,
pubmed-meshheading:10517637-Recombinant Proteins,
pubmed-meshheading:10517637-Thapsigargin,
pubmed-meshheading:10517637-Xenopus
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pubmed:year |
1999
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pubmed:articleTitle |
Polycystin-L is a calcium-regulated cation channel permeable to calcium ions.
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pubmed:affiliation |
Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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