Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor
- 23 May 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (14) , 3159-3163
- https://doi.org/10.1016/j.febslet.2005.04.078
Abstract
We have performed the recombinant expression and purification of the reductase domain of endothelial nitric oxide synthase (eNOS) and used it as a bait in search for interacting proteins present in endothelial cells. Using mass spectrometry of the bound proteins run in a PAGE–SDS gel, we were able to identify the ryanodine receptor (RyR) as a novel eNOS-binding partner. This interaction was confirmed through immunoprecipitation of both RyR and eNOS from endothelial cells and cardiac myocytes. Immunofluorescence data indicated that a subpopulation of eNOS associates with RyR in perinuclear regions of the cell, where eNOS might be responsible for the known nitrosylation of RyRKeywords
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