Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2053237 | FEBS Letters | 2005 | 5 Pages |
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 RyR.
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Authors
Mónica Martínez-Moreno, Alberto Álvarez-Barrientos, Fernando Roncal, Juan Pablo Albar, Francisco Gavilanes, Santiago Lamas, Ignacio Rodríguez-Crespo,