| pubmed-article:21145921 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21145921 | lifeskim:mentions | umls-concept:C0034783 | lld:lifeskim |
| pubmed-article:21145921 | lifeskim:mentions | umls-concept:C0243044 | lld:lifeskim |
| pubmed-article:21145921 | lifeskim:mentions | umls-concept:C1825534 | lld:lifeskim |
| pubmed-article:21145921 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:21145921 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:21145921 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21145921 | pubmed:dateCreated | 2011-1-24 | lld:pubmed |
| pubmed-article:21145921 | 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. | lld:pubmed |
| pubmed-article:21145921 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21145921 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21145921 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21145921 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:21145921 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:21145921 | pubmed:author | pubmed-author:de VriesRenéR | lld:pubmed |
| pubmed-article:21145921 | pubmed:author | pubmed-author:DanserA H... | lld:pubmed |
| pubmed-article:21145921 | pubmed:author | pubmed-author:KapustaDaniel... | lld:pubmed |
| pubmed-article:21145921 | pubmed:author | pubmed-author:FilipeanuCata... | lld:pubmed |
| pubmed-article:21145921 | pubmed:copyrightInfo | 2010 Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:21145921 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:21145921 | pubmed:volume | 1813 | lld:pubmed |
| pubmed-article:21145921 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21145921 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21145921 | pubmed:pagination | 346-57 | lld:pubmed |
| pubmed-article:21145921 | pubmed:dateRevised | 2011-8-17 | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:meshHeading | pubmed-meshheading:21145921... | lld:pubmed |
| pubmed-article:21145921 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21145921 | pubmed:articleTitle | Modulation of ?(2C) adrenergic receptor temperature-sensitive trafficking by HSP90. | lld:pubmed |
| pubmed-article:21145921 | 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 | lld:pubmed |
| pubmed-article:21145921 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21145921 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
