ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2010
Beta-arrestin 2 is required for B1 receptor-dependent post-translational activation of inducible nitric oxide synthase.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- The Critical Gene Screening to Prevent Chromophobe Cell Renal Carcinoma Metastasis through TCGA and WGCNA.Journal of oncology · 2022Article
- Nitric Oxide and S-Nitrosylation in Cardiac Regulation: G Protein-Coupled Receptor Kinase-2 and β-Arrestins as Targets.International journal of molecular sciences · 2021Review
- Arrb2 promotes endothelial progenitor cell-mediated postischemic neovascularization.Theranostics · 2020Article
- Effects of Post-translational Modifications on Membrane Localization and Signaling of Prostanoid GPCR-G Protein Complexes and the Role of Hypoxia.The Journal of membrane biology · 2019Review
- S-Nitrosylation of β-Arrestins Biases Receptor Signaling and Confers Ligand Independence.Molecular cell · 2018Article
- The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.Pharmacological reviews · 2017Review
- Kinin-stimulated B1 receptor signaling depends on receptor endocytosis whereas B2 receptor signaling does not.Neurochemical research · 2014Article
- Inducible NOS mediates CNP-induced relaxation of intestinal myofibroblasts.American journal of physiology. Gastrointestinal and liver physiology · 2013Article
- Carboxypeptidase M augments kinin B1 receptor signaling by conformational crosstalk and enhances endothelial nitric oxide output.Biological chemistry · 2013Review
- Endothelial nitric-oxide synthase activation generates an inducible nitric-oxide synthase-like output of nitric oxide in inflamed endothelium.The Journal of biological chemistry · 2013Article
- Characterization of dual agonists for kinin B1 and B2 receptors and their biased activation of B2 receptors.Cellular signalling · 2012Article
- S-nitrosylation-regulated GPCR signaling.Biochimica et biophysica acta · 2012Article
- Heterologous down-regulation of angiotensin type 1 receptors by purinergic P2Y2 receptor stimulation through S-nitrosylation of NF-kappaB.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Therapeutic potential of β-arrestin- and G protein-biased agonists.Trends in molecular medicine · 2011Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A major source of "high-output" NO in inflammation is inducible nitric oxide synthase (iNOS). iNOS is primarily transcriptionally regulated and is thought to function as an uncontrolled generator of high NO. We found that iNOS in cytokine-stimulated human lung microvascular endothelial cells (HLMVECs) is highly regulated post-translationally via activation of the B1 kinin G protein-coupled receptor (B1R). We report here that B1R-mediated iNOS activation was significantly inhibited by knockdown of beta-arrestin 2 with siRNA in cytokine-treated HLMVECs or HEK293 cells transfected with iNOS and B1R. In contrast, beta-arrestin 1 siRNA had no effect. The prolonged phase of B1R-dependent ERK activation was also inhibited by beta-arrestin 2 knockdown. Furthermore, robust ERK activation by the epidermal growth factor receptor (a beta-arrestin 2 independent pathway) had no effect on iNOS-derived NO production. beta-arrestin 2 and iNOS coimmunoprecipitated, and there was significant fluorescence resonance energy transfer between CFP-iNOS and beta-arrestin 2-YFP (but not beta-arrestin 1-YFP) that increased 3-fold after B1R stimulation. These data show that beta-arrestin 2 mediates B1R-dependent high-output NO by scaffolding iNOS and ERK to allow post-translational activation of iNOS. This could play a critical role in mediating endothelial function in inflammation.
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