- Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor.
Direct interaction between the reductase domain of endothelial nitric oxide synthase and the ryanodine receptor.
FEBS letters (2005-06-01)
Mónica Martínez-Moreno, Alberto Alvarez-Barrientos, Fernando Roncal, Juan Pablo Albar, Francisco Gavilanes, Santiago Lamas, Ignacio Rodríguez-Crespo
PMID15922337
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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Anti-Nitric Oxide Synthase, Endothelial (1185-1205) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
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