Identification of S-nitrosylation motifs by site-specific mapping of the S -nitrosocysteine proteome in human vascular smooth muscle cells
- 9 May 2006
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 103 (19), 7420-7425
- https://doi.org/10.1073/pnas.0600729103
Abstract
S-nitrosylation, the selective modification of cysteine residues in proteins to form S-nitrosocysteine, is a major emerging mechanism by which nitric oxide acts as a signaling molecule. Even though nitric oxide is intimately involved in the regulation of vascular smooth muscle cell functions, the potential protein targets for nitric oxide modification as well as structural features that underlie the specificity of protein S-nitrosocysteine formation in these cells remain unknown. Therefore, we used a proteomic approach using selective peptide capturing and site-specific adduct mapping to identify the targets of S-nitrosylation in human aortic smooth muscle cells upon exposure to S-nitrosocysteine and propylamine propylamine NONOate. This strategy identified 20 unique S-nitrosocysteine-containing peptides belonging to 18 proteins including cytoskeletal proteins, chaperones, proteins of the translational machinery, vesicular transport, and signaling. Sequence analysis of the S-nitrosocysteine-containing peptides revealed the presence of acid/base motifs, as well as hydrophobic motifs surrounding the identified cysteine residues. High-resolution immunogold electron microscopy supported the cellular localization of several of these proteins. Interestingly, seven of the 18 proteins identified are localized within the ER/Golgi complex, suggesting a role for S-nitrosylation in membrane trafficking and ER stress response in vascular smooth muscle.Keywords
This publication has 53 references indexed in Scilit:
- PWWP Module of Human Hepatoma-derived Growth Factor Forms a Domain-swapped Dimer with Much Higher Affinity for HeparinJournal of Molecular Biology, 2007
- Hepatoma-Derived Growth Factor Is a Novel Prognostic Factor for Patients with Pancreatic CancerClinical Cancer Research, 2006
- Hepatoma-Derived Growth Factor Is a Novel Prognostic Factor for Hepatocellular CarcinomaAnnals of Surgical Oncology, 2006
- S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 bindingNature, 2005
- Protein S-nitrosylation: purview and parametersNature Reviews Molecular Cell Biology, 2005
- 14-3-3 Dimers Probe the Assembly Status of Multimeric Membrane ProteinsCurrent Biology, 2003
- Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesisNature Genetics, 2002
- Hepatoma-derived growth factor stimulates smooth muscle cell growth and is expressed in vascular developmentJCI Insight, 2000
- Reductive Assays forS-Nitrosothiols: Implications for Measurements in Biological SystemsBiochemical and Biophysical Research Communications, 1998
- Hepatoma-Derived Growth Factor Belongs to a Gene Family in Mice Showing Significant Homology in the Amino TerminusBiochemical and Biophysical Research Communications, 1997