eNOS activation and NO function: Structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity
Year: 2011
Type: review
Abstract: Rather than being a constitutive enzyme as was first suggested, endothelial nitric oxide synthase (eNOS) is dynamically regulated at the transcriptional, posttranscriptional, and posttranslational levels. This review will focus on how changes in eNOS function are conferred by various posttranslational modifications. The latest knowledge regarding eNOS targeting to the plasma membrane will be discussed as the role of protein phosphorylation as a modulator of catalytic activity. Furthermore, new data are presented that provide novel insights into how disruption of the eNOS dimer prevents eNOS uncoupling and the production of superoxide under conditions of elevated oxidative stress and identifies a novel regulatory region we have termed the 'flexible arm'.
Source: Journal of Endocrinology
DOI: 10.1530/joe-11-0083
Authors: Ruslan Rafikov, Fabio V Fonseca, Sanjiv Kumar, Daniel Pardo, Charles Darragh, Shawn Elms, David Fulton, Stephen M Black
Institution: Cleveland Clinic
Language: English
Subfield: Physiology (medical)
Field: Medicine
Domain: Health Sciences
Open Access status: bronze
Awards: Tyrosine phosphorylation of endothelial nitric oxide synthase, G2279855079, ROS in Pulmonary Hypertension: Role of ADMA, NO-mediated signaling in endothelial cells, G5093756712, Role of altered carnitine metabolism in perinatal endothelial dysfunction, Metabolic Determinants of Cardiovascular Dysfunction in Obesity, Perinatal regulation of TGF-beta1 during vascular remodeling, ENOS Dimer Disruption and Endothelial Dysfunction, Metabolic reprogramming of smooth muscle cells in pulmonary hypertension
OpenAlex ID: W2171689984