Basal and stimulated protein S-nitrosylation in multiple cell types and tissues

Andrew J. Gow, Qiping Chen, Douglas T. Hess, Brian J. Day, Harry Ischiropoulos, Jonathan S. Stamler

Research output: Contribution to journalArticle

249 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)9637-9640
Number of pages4
JournalJournal of Biological Chemistry
Volume277
Issue number12
DOIs
Publication statusPublished - 22 Mar 2002
Externally publishedYes

Fingerprint

Protein S
Tissue
Nitric Oxide Synthase
Nitric Oxide
Bioactivity
Proteins
Cytokines
Nitric Oxide Synthase Type III
Macrophages
PC12 Cells
Endothelial cells
Nerve Growth Factor
Post Translational Protein Processing
Smooth Muscle Myocytes
Endothelium
Muscle
Cultured Cells
Intercellular Signaling Peptides and Proteins
Demonstrations
Endothelial Cells

ASJC Scopus subject areas

  • Biochemistry

Cite this

Gow, A. J., Chen, Q., Hess, D. T., Day, B. J., Ischiropoulos, H., & Stamler, J. S. (2002). Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. Journal of Biological Chemistry, 277(12), 9637-9640. https://doi.org/10.1074/jbc.C100746200

Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. / Gow, Andrew J.; Chen, Qiping; Hess, Douglas T.; Day, Brian J.; Ischiropoulos, Harry; Stamler, Jonathan S.

In: Journal of Biological Chemistry, Vol. 277, No. 12, 22.03.2002, p. 9637-9640.

Research output: Contribution to journalArticle

Gow, AJ, Chen, Q, Hess, DT, Day, BJ, Ischiropoulos, H & Stamler, JS 2002, 'Basal and stimulated protein S-nitrosylation in multiple cell types and tissues', Journal of Biological Chemistry, vol. 277, no. 12, pp. 9637-9640. https://doi.org/10.1074/jbc.C100746200
Gow, Andrew J. ; Chen, Qiping ; Hess, Douglas T. ; Day, Brian J. ; Ischiropoulos, Harry ; Stamler, Jonathan S. / Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 12. pp. 9637-9640.
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