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Nitric oxide‐mediated protein modification in cardiovascular physiology and pathology
Author(s) -
Gödecke Axel,
Schrader Jürgen,
Reinartz Michael
Publication year - 2008
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200780079
Subject(s) - cyclic guanosine monophosphate , nitric oxide , regulator , vascular tone , peroxynitrite , contractility , guanosine , mediator , chemistry , nitrosylation , pathophysiology , microbiology and biotechnology , biochemistry , biology , neuroscience , endocrinology , enzyme , superoxide , gene
Abstract Nitric oxide (NO) is a key regulator of cardiovascular functions including the control of vascular tone, anti‐inflammatory properties of the endothelium, cardiac contractility, and thrombocyte activation and aggregation. Numerous experimental data support the view that NO not only acts via cyclic guanosine monophosphate (cGMP)‐dependent mechanisms but also modulates protein function by nitrosation, nitrosylation, glutathiolation, and nitration, respectively. To understand how NO regulates all of these diverse biological processes on the molecular level a comprehensive assessment of NO‐mediated cGMP‐dependent and independent targets is required. Novel proteomic approaches allow the simultaneous identification of large quantities of proteins modified in an NO‐dependent manner and thereby will considerably deepen our understanding of the role NO plays in cardiovascular physiology and pathophysiology.