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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2008-7-28
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pubmed:abstractText |
P2X(4) and P2X(7) receptors are abundantly expressed in alveolar epithelial cells, and are thought to play a role in regulating fluid haemostasis. Here, we analyzed the expression and localization of the P2X(4)R, and characterized the interaction between Cav-1 and both P2X(4)R and P2X(7)R in the mouse alveolar epithelial cell line E10. Using the biotinylation assay, we found that only glycosylated P2X(4)R is exposed at the cell surface. Triton X-100 solubility experiments and sucrose gradient centrifugation revealed that P2X(4)R was partially localized in Cav-1 rich membrane fractions. Cholesterol depletion with Mbeta-CD displaced Cav-1 and P2X(4)R from the low-density to the high-density fractions. Suppression of Cav-1 protein expression using short hairpin RNAs resulted in a large reduction in P2X(4)R levels. Double immunofluorescence showed that P2X(4)R and Cav-1 partially colocalize in vitro. Using the GST pull-down assay, we showed that Cav-1 interacts in vitro with both P2X(4)R and P2X(7)R. Co-immunoprecipitation experiments confirmed the interaction between P2X(7)R and Cav-1. ATP stimulation increased the level of P2X(4)R in the lipid raft/caveolae fraction, whereas Cav-1 content remained constant. Our results support recent evidence that P2X receptors are present in both raft and non-raft compartments of the plasma membrane and thus exhibit variable ATP sensitivity.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/P2rx7 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2X4,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P2X7,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/betadex
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pubmed:status |
MEDLINE
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pubmed:issn |
1357-2725
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2230-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18407780-Adenosine Triphosphate,
pubmed-meshheading:18407780-Animals,
pubmed-meshheading:18407780-Caveolae,
pubmed-meshheading:18407780-Caveolin 1,
pubmed-meshheading:18407780-Cell Line,
pubmed-meshheading:18407780-Cholesterol,
pubmed-meshheading:18407780-Down-Regulation,
pubmed-meshheading:18407780-Epithelial Cells,
pubmed-meshheading:18407780-Glycosylation,
pubmed-meshheading:18407780-Lung,
pubmed-meshheading:18407780-Membrane Microdomains,
pubmed-meshheading:18407780-Mice,
pubmed-meshheading:18407780-Protein Binding,
pubmed-meshheading:18407780-Protein Processing, Post-Translational,
pubmed-meshheading:18407780-Protein Transport,
pubmed-meshheading:18407780-Pulmonary Alveoli,
pubmed-meshheading:18407780-RNA, Small Interfering,
pubmed-meshheading:18407780-Receptors, Purinergic P2,
pubmed-meshheading:18407780-Receptors, Purinergic P2X4,
pubmed-meshheading:18407780-Receptors, Purinergic P2X7,
pubmed-meshheading:18407780-beta-Cyclodextrins
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pubmed:year |
2008
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pubmed:articleTitle |
Characterization of the molecular interaction between caveolin-1 and the P2X receptors 4 and 7 in E10 mouse lung alveolar epithelial cells.
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pubmed:affiliation |
Institute of Anatomy, Medical Faculty "Carl Gustav Carus", Dresden University of Technology, Fiedlerstr. 42, D-01307 Dresden, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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