| http://purl.uniprot.org/citations/15184369 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15184369 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15184369 | http://www.w3.org/2000/01/rdf-schema#comment | "Microfluorimetry and patch-clamp experiments were performed on TRPV6-expressing HEK cells to determine whether this Ca(2+)-sensing Ca(2+) channel is constitutively active. Intact cells loaded with fura-2 had an elevated intracellular free Ca(2+) concentration ([Ca(2+)](i)), which decreased to the same level such as in non-transfected cells if external Ca(2+) was chelated by EGTA. Whole cell recordings from non-transfected HEK cells and cells expressing human TRPV6 revealed the presence of a basal inward current in both types of cells when the internal solution contained 0.1 mm EGTA and 100 nm [Ca(2+)](i) or if the cytosolic Ca(2+) buffering remained undisturbed in perforated patch-clamp experiments. If recombinantly expressed TRPV6 forms open channels, one would expect Ca(2+)-induced current inhibition, because TRPV6 is negatively regulated by internal Ca(2+). However, dialyzing solutions with high [Ca(2+)] such as 1 microm into TRPV6-expressing cells did not block the basal inward current, which was not different from the recordings from non-transfected cells. In contrast, dialyzing 0.5 mm EGTA into TRPV6-expressing cells readily activated Ca(2+) inward currents, which were undetectable in non-transfected cells. Interestingly, monovalent cations permeated the TRPV6 channels under conditions where no Ca(2+) permeation was detectable, indicating that divalent cations block TRPV6 channels from the extracellular side. Like human TRPV6, the truncated human TRPV6(Delta695-725), which lacks the C-terminal domain required for Ca(2+)-calmodulin binding, does not form constitutive active channels, whereas the human TRPV6(D542A), carrying a point mutation in the presumed pore region, does not function as a channel. In summary, no constitutive open TRPV6 channels were detected in patch-clamp experiments from transfected HEK cells. However, channel activity is highly regulated by intracellular and extracellular divalent cations."xsd:string |
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| http://purl.uniprot.org/citations/15184369 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m404679200"xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/author | "Flockerzi V."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/author | "Flockerzi V."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/author | "Bodding M."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/author | "Bodding M."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/pages | "36546-36552"xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/pages | "36546-36552"xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/title | "Ca2+ dependence of the Ca2+-selective TRPV6 channel."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/title | "Ca2+ dependence of the Ca2+-selective TRPV6 channel."xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15184369 | http://purl.uniprot.org/core/volume | "279"xsd:string |
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| http://purl.uniprot.org/citations/15184369 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15184369 |
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| http://purl.uniprot.org/citations/15184369 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15184369 |
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