Key result
Bradykinin induces serine phosphorylation of endothelial nitric oxide synthase and its translocation from the particulate to the cytosolic fraction in cultured bovine aortic endothelial cells.
Population
Cultured bovine aortic endothelial cells (BAECs) between passages 6 and 12
Comparison
Exposure to agonists, primarily bradykinin vs Untreated (basal) cells
Design
Preclinical
Authors
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Agonist-linked eNOS phosphorylation may regulate endothelial NO; hypothesis-generating in vitro finding leaves clinical translation open.
Agonist-induced phosphorylation of endothelial NO synthase is associated with its translocation from the membrane to the cytosol, which may regulate its biological activity in situ.
Michel et al. (1993) studied this question. Bradykinin vs. Untreated (basal) cells was evaluated on Phosphorylation and subcellular translocation of endothelial NO synthase. Bradykinin induces serine phosphorylation of endothelial nitric oxide synthase and its translocation from the particulate to the cytosolic fraction in cultured bovine aortic endothelial cells.
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