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J. Biol. Chem., Vol. 277, Issue 12, 9637-9640, March 22, 2002
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From the There is substantial evidence 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
nitrosothiol (SNO) moiety to provide an immunohistochemical demonstration that protein S-nitrosylation is coupled to
the activity of each of the major forms of NOS. In cultured endothelial
cells, SNO-protein immunoreactivity increases in response to
Ca2+-stimulated endothelial NOS (eNOS) activity, and in
aortic rings, endothelium-derived and eNOS-mediated relaxation (EDRF)
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
induced NOS (iNOS), and in PC12 cells, increased protein
S-nitrosylation is linked to nerve growth factor induction
of neuronal NOS (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 post-translational protein modification serves as
a major effector of NO-related bioactivity.
Department of Medicine and Howard Hughes
Medical Institute, Duke University Medical Center, Durham, North
Carolina 27710 and § Stokes Research Institute, Children's
Hospital of Pennsylvania, Philadelphia, Pennsylvania 19140
To whom correspondence may be addressed: Dept. of Medicine,
Box 2612, Duke University Medical Center, Durham, NC 27710. E-mail: staml001@duke.mc.edu.
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