Endothelium-Derived Vasodilators

Moncada, Salvador; Palmer, Richard; Higgs, E. A.

doi:10.1007/978-1-4684-8532-5_22

Cited by 768 publications

(1,218 citation statements)

References 30 publications

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“…These findings suggest that the in vivo inhibition of PTPases by NO is not limited to the RAW 264.7 murine macrophages, but probably extended to all cells. NO is a small molecule involved in several physiological processes such as the inhibition of platelet aggregation, desensitisation of neurones to excess stimulation by glutamate, smooth muscle relaxation, and penile erection [1,2]. On the other hand, PTPases are known to be involved in the regulation of mitogenic signals acting on tyrosine kinase membrane receptors.…”

Section: Discussionmentioning

confidence: 99%

“…It is produced from L-arginine in macrophages, endothelial cells and other cell types, and has been implicated in several physiological processes including vascular smooth muscle relaxation, inhibition of platelet aggregation, neurotransmission, immune regulation and penile erection [1,2]. Girard and Potier suggested also that the NO-mediated S-nitrosation could play a role in interconversion of thiol groups and disulfides in chain radical or oxidation-reduction processes that improve protein structural stability, ensure enzymatic catalysis, transport of reducing equivalents, and metabolic regulation [3].…”

Section: Introductionmentioning

confidence: 99%

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In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

et al. 1995

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The effect of NO on phosphotyrosine protein phosphatases (PTPases) has been investigated in vivo. NO production is induced in interferon-y and lipopolyaccharide stimulated RAW-264.7 macrophages as indicated by the increase of NO~ in the medium. Our results demonstrate an inhibition of p-nitrophenylphosphatase activity as a consequence of macrophages activation. Under the described experimental conditions, most of the hydrolysis ofp-nitrophenylphosphate can be ascribed to the action of cellular PTPases. The presence of N~-monomethyI-L-arginine, a specific inhibitor of NO synthase decreases the inactivation rate of both membrane-bound and soluble PTPases. This evidence further confirms the ability of NO to inactivate PTPases and suggests a possible role of NO in the regulation of cellular processes involving this class of phosphatases.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

et al. 1995

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“…This enzyme catalyzes the conversion of guanosine triphosphate (GTP) to cyclic guanosine monophosphate (cGMP). Thus, a large majority of the biological signaling associated with · NO is due to the second messenger cGMP, an important messenger involved in a number of critical physiological processes in the cardiovascular system including regulation of vascular smooth muscle tone, cell proliferation, platelet aggregation and leukocyte recruitment (100,101). Thus, the regulation of cGMP levels has implications for the pathogenesis and treatment of numerous cardiovascular disorders including hypertension, sepsis, stroke and erectile dysfunction.…”

Section: Activation Of Soluble Guanylate Cyclase and Cgmp Signalingmentioning

confidence: 99%

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Forman

Fukuto

Miller

et al. 2008

Archives of Biochemistry and Biophysics

217

165

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During the past several years, major advances have been made in understanding how reactive oxygen species (ROS) and nitrogen species (RNS) participate in signal transduction. Identification of the specific targets and the chemical reactions involved still remains to be resolved with many of the signaling pathways in which the involvement of reactive species has been determined. Our understanding is that ROS and RNS have second messenger roles. While cysteine residues in the thiolate (ionized) form found in several classes of signaling proteins can be specific targets for reaction with H 2 O 2 and RNS, better understanding of the chemistry, particularly kinetics, suggests that for many signaling events in which ROS and RNS participate, enzymatic catalysis is more likely to be involved than non-enzymatic reaction. Due to increased interest in how oxidation products, particularly lipid peroxidation products, also are involved with signaling, a review of signaling by 4-hydroxy-2-nonenal (HNE) is included. This article focuses on the chemistry of signaling by ROS, RNS, and HNE and will describe reactions with selected target proteins as representatives of the mechanisms rather attempt to comprehensively review the many signaling pathways in which the reactive species are involved. Keywords signaling; glutathione; thioredoxin; oxidants; reactive oxygen species; thiols; peroxide; nitric oxide; peroxynitrite; 4-hydroxynonenal; cysteine; hydrogen peroxide; protein tyrosine phosphatase; reactive nitrogen species; eNOS; iNOS; nNOS; soluble guanylate cyclase; cGMP; tyrosine nitration; fatty acid nitration; NO-heme; NO-metal complexes; nitrite; protein kinase C; ERK; JNK; p38MAPK; tyrosine kinase receptors; calcium OVERVIEW OF SIGNALING BY REACTIVE SPECIESUnderstanding of the roles of reactive oxygen species (ROS), reactive nitrogen species (RNS) and the lipid peroxidation product, 4-hydroxy-2-nonenal (HNE) in signaling has evolved rapidly during the last decade. This has been markedly helped by identification of the specific targets in signaling pathways. In previous reviews, we defined how ROS, H 2 O 2 in particular,

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“…Although nitric oxide (NO') has many important physiological functions [11], its production in excess may contribute to the pathology of neurodegenerative disease, chronic inflammation, acute respiratory distress syndrome, atherosclerosis and septic shock [9][10][11][12][13][14]. Part of the toxicity of NO" involves its reaction with superoxide radical (02 °-) to give peroxynitrite, ONOO-…”

Section: Introductionmentioning

confidence: 99%

Protection against peroxynitrite‐dependent tyrosine nitration and α₁‐antiproteinase inactivation by oxidized and reduced lipoic acid

Whiteman

Tritschler²,

Halliwell

1996

FEBS Letters

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Peroxynitrite, formed by combination of superoxide radical with nitric oxide, is a reactive tissue-damaging species apparently involved in the pathology of several human diseases. Peroxynitrite nitrates tyrosine residues and inactivates vq-antiproteinase. We show that both lipoic acid and dihydrolipoic acid efficiently protect against damage by peroxynitrite. By contrast, other disulphides tested did not. The biological antioxidant effects of lipoateldihydrolipoate may involve scavenging of reactive nitrogen species as well as reactive oxygen species.

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Endothelium-Derived Vasodilators

Cited by 768 publications

References 30 publications

In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Protection against peroxynitrite‐dependent tyrosine nitration and α₁‐antiproteinase inactivation by oxidized and reduced lipoic acid

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Endothelium-Derived Vasodilators

Cited by 768 publications

References 30 publications

In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide

The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal

Protection against peroxynitrite‐dependent tyrosine nitration and α1‐antiproteinase inactivation by oxidized and reduced lipoic acid

Contact Info

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Protection against peroxynitrite‐dependent tyrosine nitration and α₁‐antiproteinase inactivation by oxidized and reduced lipoic acid