ArticlePloS one2012
Proteomic identification of S-nitrosylated Golgi proteins: new insights into endothelial cell regulation by eNOS-derived NO.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025Review
- Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024Review
- Extracellular Matrix Stiffness-Induced Mechanotransduction of Capillarized Liver Sinusoidal Endothelial Cells.Pharmaceuticals (Basel, Switzerland) · 2024Article
- S-nitrosylation of EMMPRIN influences the migration of HSCs and MMP activity in liver fibrosis.Acta biochimica et biophysica Sinica · 2023Article
- Intracellular Sources of ROS/HCells · 2021Review
- A clickable probe for versatile characterization of S-nitrosothiols.Redox biology · 2020Article
- S-Nitrosylation: An Emerging Paradigm of Redox Signaling.Antioxidants (Basel, Switzerland) · 2019Review
- Mechanisms of Blood-Brain Barrier Disruption in Herpes Simplex Encephalitis.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2019Review
- Non-Invasive Detection of Extracellular Matrix Metalloproteinase Inducer EMMPRIN, a New Therapeutic Target against Atherosclerosis, Inhibited by Endothelial Nitric Oxide.International journal of molecular sciences · 2018Article
- The eNOS signalosome and its link to endothelial dysfunction.Pflugers Archiv : European journal of physiology · 2016Review
- The Expanding Landscape of the Thiol Redox Proteome.Molecular & cellular proteomics : MCP · 2016Review
- Distinct Biochemical Pools of Golgi Phosphoprotein 3 in the Human Breast Cancer Cell Lines MCF7 and MDA-MB-231.PloS one · 2016Article
- Article
- Nitric oxide in liver fibrosis: The role of inducible nitric oxide synthase.Clinical and molecular hepatology · 2015Review
- Nitric oxide in liver diseases.Trends in pharmacological sciences · 2015Review
- Increased Expression of GOLPH3 is Associated with the Proliferation of Prostate Cancer.Journal of Cancer · 2015Article
- Post-translational regulation of endothelial nitric oxide synthase in vascular endothelium.Frontiers in physiology · 2013Review
- Specificity in S-nitrosylation: a short-range mechanism for NO signaling?Antioxidants & redox signaling · 2013Review
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
backgroundEndothelial nitric oxide synthase (eNOS) is primarily localized on the Golgi apparatus and plasma membrane caveolae in endothelial cells. Previously, we demonstrated that protein S-nitrosylation occurs preferentially where eNOS is localized. Thus, in endothelial cells, Golgi proteins are likely to be targets for S-nitrosylation. The aim of this study was to identify S-nitrosylated Golgi proteins and attribute their S-nitrosylation to eNOS-derived nitric oxide in endothelial cells.
methodsGolgi membranes were isolated from rat livers. S-nitrosylated Golgi proteins were determined by a modified biotin-switch assay coupled with mass spectrometry that allows the identification of the S-nitrosylated cysteine residue. The biotin switch assay followed by Western blot or immunoprecipitation using an S-nitrosocysteine antibody was also employed to validate S-nitrosylated proteins in endothelial cell lysates.
resultsSeventy-eight potential S-nitrosylated proteins and their target cysteine residues for S-nitrosylation were identified; 9 of them were Golgi-resident or Golgi/endoplasmic reticulum (ER)-associated proteins. Among these 9 proteins, S-nitrosylation of EMMPRIN and Golgi phosphoprotein 3 (GOLPH3) was verified in endothelial cells. Furthermore, S-nitrosylation of these proteins was found at the basal levels and increased in response to eNOS stimulation by the calcium ionophore A23187. Immunofluorescence microscopy and immunoprecipitation showed that EMMPRIN and GOLPH3 are co-localized with eNOS at the Golgi apparatus in endothelial cells. S-nitrosylation of EMMPRIN was notably increased in the aorta of cirrhotic rats.
conclusionOur data suggest that the selective S-nitrosylation of EMMPRIN and GOLPH3 at the Golgi apparatus in endothelial cells results from the physical proximity to eNOS-derived nitric oxide.
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