Source:http://linkedlifedata.com/resource/pubmed/id/21135099
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2011-2-14
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pubmed:abstractText |
Interaction of large conductance Ca(2+)- and voltage-activated K(+) (BK(Ca)) channels with Na(+)/K(+)-ATPase, caveolin-1, and cholesterol was studied in human melanoma IGR39 cells. Functional BK(Ca) channels were enriched in caveolin-rich and detergent-resistant membranes, i.e. rafts, and blocking of the channels by a specific BK(Ca) blocker paxilline reduced proliferation of the cells. Disruption of rafts by selective depletion of cholesterol released BK(Ca) channels from these domains with a consequent increase in their activity. Consistently, cholesterol enrichment of the cells increased the proportion of BK(Ca) channels in rafts and decreased their activity. Immunocytochemical analysis showed that BK(Ca) channels co-localize with Na(+)/K(+)-ATPase in a cholesterol-dependent manner, thus suggesting their co-presence in rafts. Supporting this, ouabain, a specific blocker of Na(+)/K(+)-ATPase, inhibited BK(Ca) whole-cell current markedly in control cells but not in cholesterol-depleted ones. This inhibition required the presence of external Na(+). Collectively, these data indicate that the presence of Na(+)/K(+)-ATPase in rafts is essential for efficient functioning of BK(Ca) channels, presumably because the pump maintains a low intracellular Na(+) proximal to the BK(Ca) channel. In conclusion, cholesterol could play an important role in cellular ion homeostasis and thus modulate many cellular functions and cell proliferation.
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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/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Large-Conductance...,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Paxillin,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Exchanging ATPase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5624-38
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pubmed:meshHeading |
pubmed-meshheading:21135099-Caveolins,
pubmed-meshheading:21135099-Cell Line, Tumor,
pubmed-meshheading:21135099-Cell Proliferation,
pubmed-meshheading:21135099-Cholesterol,
pubmed-meshheading:21135099-Humans,
pubmed-meshheading:21135099-Ion Transport,
pubmed-meshheading:21135099-Large-Conductance Calcium-Activated Potassium Channels,
pubmed-meshheading:21135099-Melanoma,
pubmed-meshheading:21135099-Membrane Microdomains,
pubmed-meshheading:21135099-Membrane Potentials,
pubmed-meshheading:21135099-Neoplasm Proteins,
pubmed-meshheading:21135099-Paxillin,
pubmed-meshheading:21135099-Sodium-Potassium-Exchanging ATPase
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pubmed:year |
2011
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pubmed:articleTitle |
Activity of BK(Ca) channel is modulated by membrane cholesterol content and association with Na+/K+-ATPase in human melanoma IGR39 cells.
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pubmed:affiliation |
Department of Medical Biochemistry and Developmental Biology, Institute of Biomedicine, University of Helsinki, Helsinki FI-00014, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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