Source:http://linkedlifedata.com/resource/pubmed/id/21145921
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2011-1-24
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| pubmed:abstractText |
Decreasing the temperature to 30°C is accompanied by significant enhancement of ?(2C)-AR plasma membrane levels in several cell lines with fibroblast phenotype, as demonstrated by radioligand binding in intact cells. No changes were observed on the effects of low-temperature after blocking receptor internalization in ?(2C)-AR transfected HEK293T cells. In contrast, two pharmacological chaperones, dimethyl sulfoxide and glycerol, increased the cell surface receptor levels at 37°C, but not at 30°C. Further, at 37°C ?(2C)-AR is co-localized with endoplasmic reticulum markers, but not with the lysosomal markers. Treatment with three distinct HSP90 inhibitors, radicicol, macbecin and 17-DMAG significantly enhanced ?(2C)-AR cell surface levels at 37°C, but these inhibitors had no effect at 30°C. Similar results were obtained after decreasing the HSP90 cellular levels using specific siRNA. Co-immunoprecipitation experiments demonstrated that ?(2C)-AR interacts with HSP90 and this interaction is decreased at 30°C. The contractile response to endogenous ?(2C)-AR stimulation in rat tail artery was also enhanced at reduced temperature. Similar to HEK293T cells, HSP90 inhibition increased the ?(2C)-AR contractile effects only at 37°C. Moreover, exposure to low-temperature of vascular smooth muscle cells from rat tail artery decreased the cellular levels of HSP90, but did not change HSP70 levels. These data demonstrate that exposure to low-temperature augments the ?(2C)-AR transport to the plasma membrane by releasing the inhibitory activity of HSP90 on the receptor traffic, findings which may have clinical relevance for the diagnostic and treatment of Raynaud Phenomenon.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/17-(dimethylaminoethylamino)-17-deme...,
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha-2,
http://linkedlifedata.com/resource/pubmed/chemical/macbecin I,
http://linkedlifedata.com/resource/pubmed/chemical/monorden
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0006-3002
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| pubmed:author | |
| pubmed:copyrightInfo |
2010 Elsevier B.V. All rights reserved.
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| pubmed:issnType |
Print
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| pubmed:volume |
1813
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
346-57
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| pubmed:dateRevised |
2011-8-17
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| pubmed:meshHeading |
pubmed-meshheading:21145921-Animals,
pubmed-meshheading:21145921-Arteries,
pubmed-meshheading:21145921-Benzoquinones,
pubmed-meshheading:21145921-Cell Membrane,
pubmed-meshheading:21145921-Cells, Cultured,
pubmed-meshheading:21145921-Enzyme Inhibitors,
pubmed-meshheading:21145921-HSP90 Heat-Shock Proteins,
pubmed-meshheading:21145921-Humans,
pubmed-meshheading:21145921-Kidney,
pubmed-meshheading:21145921-Lactams, Macrocyclic,
pubmed-meshheading:21145921-Macrolides,
pubmed-meshheading:21145921-Male,
pubmed-meshheading:21145921-Muscle, Smooth, Vascular,
pubmed-meshheading:21145921-Protein Transport,
pubmed-meshheading:21145921-Protein-Tyrosine Kinases,
pubmed-meshheading:21145921-RNA, Small Interfering,
pubmed-meshheading:21145921-Rats,
pubmed-meshheading:21145921-Rats, Wistar,
pubmed-meshheading:21145921-Receptors, Adrenergic, alpha-2,
pubmed-meshheading:21145921-Subcellular Fractions,
pubmed-meshheading:21145921-Temperature
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| pubmed:year |
2011
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| pubmed:articleTitle |
Modulation of ?(2C) adrenergic receptor temperature-sensitive trafficking by HSP90.
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| pubmed:affiliation |
Department of Pharmacology and Experimental Therapeutics, Louisiana State University Health Sciences Center, 1901 Perdido Street, New Orleans, Louisiana, LA-70112, USA. cfilip@lsuhsc.edu
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| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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