| http://purl.uniprot.org/citations/10024311 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10024311 | http://www.w3.org/2000/01/rdf-schema#comment | "Vascular endothelial cells regulate vascular smooth muscle tone through Ca2+-dependent production and release of vasoactive molecules. Phospholamban (PLB) is a 24-to 27-kDa phosphoprotein that modulates activity of the sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA). Expression of PLB is reportedly limited to cardiac, slow-twitch skeletal and smooth muscle in which PLB is an important regulator of [Ca2+]i and contractility in these muscles. In the present study, we report the existence of PLB in the vascular endothelium, a nonmuscle tissue, and provide functional data on PLB regulation of vascular contractility through its actions in the endothelium. Endothelium-dependent relaxation to acetylcholine was attenuated in aorta of PLB-deficient (PLB-KO) mice compared with wild-type (WT) controls. This effect was not due to actions of nitric oxide on the smooth muscle, because sodium nitroprusside-mediated relaxation in either denuded or endothelium-intact aortas was unaffected by PLB ablation. Relative to denuded vessels, relaxation to forskolin was enhanced in WT endothelium-intact aortas. The endothelium-dependent component of this relaxation was attenuated in PLB-KO aortas. To investigate whether these changes were due to PLB, WT mouse aorta endothelial cells were isolated. Both reverse transcriptase-polymerase chain reaction and Western blot analyses revealed the presence of PLB in endothelial cells, which were shown to be >98% pure by diI-acetylated LDL uptake and nuclear counterstaining. These data indicate that PLB is present and modulates vascular function as a result of its actions in endothelial cells. The presence of PLB in endothelial cells opens new fields for investigation of Ca2+ regulatory pathways in nonmuscle cells and for modulation of endothelial-vascular interactions."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.org/dc/terms/identifier | "doi:10.1161/01.res.84.3.360"xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/author | "Kranias E.G."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/author | "Paul R.J."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/author | "Sutliff R.L."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/author | "Kadambi V.J."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/author | "Hoying J.B."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/name | "Circ Res"xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/pages | "360-364"xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/title | "Phospholamban is present in endothelial cells and modulates endothelium-dependent relaxation. Evidence from phospholamban gene-ablated mice."xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://purl.uniprot.org/core/volume | "84"xsd:string |
| http://purl.uniprot.org/citations/10024311 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10024311 |
| http://purl.uniprot.org/citations/10024311 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10024311 |
| http://purl.uniprot.org/uniprot/P61014#attribution-35DC34553F8D62519616E7D393CDA8DE | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10024311 |
| http://purl.uniprot.org/uniprot/#_P61014-mappedCitation-10024311 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10024311 |
| http://purl.uniprot.org/uniprot/P61014 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10024311 |