Document Detail


S-nitrosylation of proteins: a new insight into endothelial cell function regulated by eNOS-derived NO.
MedLine Citation:
PMID:  21554971     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Yasuko Iwakiri
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2011-04-30
Journal Detail:
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:
Created Date:  2011-08-08     Completed Date:  2011-12-05     Revised Date:  2013-06-30    
Medline Journal Info:
Nlm Unique ID:  9709307     Medline TA:  Nitric Oxide     Country:  United States    
Other Details:
Languages:  eng     Pagination:  95-101     Citation Subset:  IM    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Affiliation:
Section of Digestive Diseases, Department of Internal Medicine, Yale University School of Medicine, New Haven, CT 06520, USA. yasuko.iwakiri@yale.edu
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MeSH Terms
Descriptor/Qualifier:
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:
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:
0/S-Nitrosothiols; 10102-43-9/Nitric Oxide; 52-90-4/Cysteine; EC 1.14.13.39/Nitric Oxide Synthase Type III
Comments/Corrections

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