Journal
FEBS LETTERS
Volume 579, Issue 14, Pages 3159-3163Publisher
WILEY
DOI: 10.1016/j.febslet.2005.04.078
Keywords
nitric oxide synthase; calcium channels; ryanodine receptors
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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 RyR. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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