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Papers In Press, published online ahead of print January 16, 2002
J. Biol. Chem, 10.1074/jbc.C100746200
Submitted on December 20, 2001
Revised on January 10, 2002
Accepted on January 16, 2002
Deptartment of Medicine/HHMI, Duke University Medical Center, DURHAM, NC 27710
Corresponding Author: staml001{at}mc.duke.edu
Substantial evidence has accrued that protein S-nitrosylation provides a significant route through which nitric oxide (NO)-derived bioactivity is conveyed. However, most examples of S-nitrosylation have been characterized on the basis of analysis in vitro, and relatively little progress has been made in assessing the participant forms of nitric oxide synthase (NOS) or the dynamics of protein S-nitrosylation in situ. Here we utilize antibodies specific for the SNO moiety to provide an immunohistochemical demonstration that protein S-nitrosylation is coupled to activity of each of the major forms of NOS. In cultured endothelial cells, SNO-protein immunoreactivity increases in response to Ca2+-stimulated eNOS activity, and in aortic rings, endothelium-derived and eNOS-mediated relaxation is coupled to increased protein S-nitrosylation in both endothelial and associated smooth muscle cells. In cultured macrophages, SNO-protein levels increase upon cytokine induction of iNOS, and in PC12 cells, increased protein S-nitrosylation is linked to NGF induction of nNOS. In addition, we describe developmental and pathophysiological increases in SNO-protein immunoreactivity within human lung. These results, which demonstrate Ca2+, neurohumoral, growth factor, cytokine and developmental regulation of protein S-nitrosylation that is coupled to NOS expression and activity, provide unique evidence for the proposition that this ubiquitous NO-derived posttranslational protein modification serves as a major effector of NO-related bioactivity.
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