| S-nitrosylation of proteins: a new insight into endothelial cell function regulated by eNOS-derived NO. | |
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MedLine Citation:
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PMID: 21554971 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Nitric oxide (NO) is a messenger molecule that is highly diffusible and short-lived. Despite these two characteristics, seemingly unsuitable for intracellular reactions, NO modulates a variety of cellular processes via the mechanism of S-nitrosylation. An important factor that determines the specificity of S-nitrosylation as a signaling mechanism is the compartmentalization of nitric oxide synthase (NOS) with its target proteins. Endothelial NOS (eNOS) is unique among the NOS family members by being localized mainly near specific intracellular membrane domains including the cytoplasmic face of the Golgi apparatus and plasma membrane caveolae. Nitric oxide produced by eNOS localized on the Golgi apparatus can react with thiol groups on nearby Golgi proteins via a redox mechanism resulting in S-nitrosylation of these proteins. This modification influences their function as regulators of cellular processes such as protein trafficking (e.g., exocytosis and endocytosis), redox state, and cell cycle. Thus, eNOS-derived NO regulates a wide range of endothelial cell functions, such as inflammation, apoptosis, permeability, migration, and cell growth. |
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Authors:
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Yasuko Iwakiri |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2011-04-30 |
Journal Detail:
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Title: Nitric oxide : biology and chemistry / official journal of the Nitric Oxide Society Volume: 25 ISSN: 1089-8611 ISO Abbreviation: Nitric Oxide Publication Date: 2011 Aug |
Date Detail:
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Created Date: 2011-08-08 Completed Date: 2011-12-05 Revised Date: 2013-04-30 |
Medline Journal Info:
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Nlm Unique ID: 9709307 Medline TA: Nitric Oxide Country: United States |
Other Details:
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Languages: eng Pagination: 95-101 Citation Subset: IM |
Copyright Information:
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Copyright © 2011 Elsevier Inc. All rights reserved. |
Affiliation:
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Section of Digestive Diseases, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520, USA. yasuko.iwakiri@yale.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Cycle Cell Membrane Permeability Cell Movement Cysteine / metabolism Endocytosis Endothelial Cells / metabolism* Exocytosis Golgi Apparatus / metabolism Humans Nitric Oxide / metabolism* Nitric Oxide Synthase Type III / metabolism* Oxidation-Reduction Protein Transport S-Nitrosothiols / metabolism* Signal Transduction |
| Grant Support | |
ID/Acronym/Agency:
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K01 DK067933/DK/NIDDK NIH HHS; K01 DK067933-01/DK/NIDDK NIH HHS; K01 DK067933-02/DK/NIDDK NIH HHS; K01 DK067933-03/DK/NIDDK NIH HHS; K01 DK067933-04/DK/NIDDK NIH HHS; K01 DK067933-05/DK/NIDDK NIH HHS; K01DK067933/DK/NIDDK NIH HHS; R01 DK082600/DK/NIDDK NIH HHS; R01 DK082600-01A1/DK/NIDDK NIH HHS; R01 DK082600-02/DK/NIDDK NIH HHS; R01DK082600/DK/NIDDK NIH HHS; ULRR024139//PHS HHS |
| Chemical | |
Reg. No./Substance:
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0/S-Nitrosothiols; 10102-43-9/Nitric Oxide; 52-90-4/Cysteine; EC 1.14.13.39/Nitric Oxide Synthase Type III |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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