Cellular signaling with nitric oxide and cyclic GMP

Murad, Ferid

doi:10.1590/s0100-879x1999001100001

Cited by 66 publications

(45 citation statements)

References 31 publications

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“…Fourteen New Zealand white rabbits (2-3 kg) were divided into two groups: [1] Control (n=7), and [2] Chronic nitroglycerin (patched, n=7). For the patched group, the rabbits were tranquilized with subcutaneous injection of acepromazine maleate (5 mg).…”

Section: Experimental Preparationmentioning

confidence: 99%

“…Cellular effects of nitroglycerin include activation of soluble guanylyl cyclase, which increases cyclic guanosine-3′,-5′-monophosphate (cyclic GMP) levels and activates cyclic GMP-dependent protein kinases, cyclic GMP-regulated phosphodiesterases and cyclic nucleotide-gated ion channels [1]. Cyclic GMP usually exerts negative metabolic and functional effects in myocardium as well as in isolated cardiac myocytes [2].…”

Section: Introductionmentioning

confidence: 99%

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Chronic nitrates blunt the effects of not only nitric oxide but also natriuretic peptides in cardiac myocytes

Tan¹,

Zhang²,

Anyadike³

et al. 2007

Pharmacological Research

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Abstractexposure to nitrates causes tachyphylaxis to nitric oxide (NO), which reduces the effects of the second messenger cyclic GMP. We tested the hypothesis that prolonged exposure to NO would also blunt the effects of natriuretic peptides. Cardiac myocytes were isolated from control (N=7) and chronic nitroglycerin (patched, N=7) rabbits. Patched animals received a transdermal nitroglycerin patch (0.3 mg/hr for 5 days). Myocyte function was determined at baseline, after CNP (C-type natriuretic peptide, 10 −8 and 10 −7 M) or BNP (Brain natriuretic peptide, 10 −8 and 10 −7 M) or SNAP (S-nitroso-N-acetyl-penicilliamine, a NO donor, 10 −6 and 10 −5 M) followed by KT5823 (a cyclic GMP protein kinase inhibitor, 10 −6 M). Soluble and particulate guanylyl cyclase activities were measured in vitro and phosphoprotein analysis was performed. In control animals, CNP 10 −8 M (5.14±0.5%) and 10 −7 M (4.4±0.7%) significantly reduced percentage shortening from baseline (6.1±1.6%). KT5823 restored percentage shortening to 4.9±0.8%. Similar data were obtained with BNP and SNAP. In patched animals, CNP, BNP, SNAP had no significant effects on percentage shortening. The data on maximal rate of shortening and relaxation were consistent with these results. Guanylyl cyclase activities were not different in the control and patched animals. The myocytes from control and patched animals had similar protein phosphorylation patterns. Our data suggested that in addition to NO, the responses to both natriuretic peptides were downregulated after chronic exposure to nitroglycerin, but these effects were not due to changes in either guanylyl cyclase or cyclic GMP protein kinase, suggesting an altered downstream pathway.

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Section: Experimental Preparationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Chronic nitrates blunt the effects of not only nitric oxide but also natriuretic peptides in cardiac myocytes

Tan¹,

Zhang²,

Anyadike³

et al. 2007

Pharmacological Research

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show abstract

“…S ince the discovery of the first biological effects of nitric oxide (NO) more than two decades ago (1)(2)(3), NO has been identified as an important messenger molecule with diverse functions in many biological systems (4)(5)(6)(7)(8). Although many effects of NO are mediated through its direct interaction with guanylyl cyclase activation (1)(2)(3)(4)(5)(6)(7)(8), its indirect action via secondary reactions with reactive oxygen species, forming reactive nitrogen species accounts for other effects.…”

mentioning

confidence: 99%

“…Although many effects of NO are mediated through its direct interaction with guanylyl cyclase activation (1)(2)(3)(4)(5)(6)(7)(8), its indirect action via secondary reactions with reactive oxygen species, forming reactive nitrogen species accounts for other effects. The reaction of NO and its reactive intermediates with protein bound tyrosine residues causes nitrotyrosine formation (9).…”

mentioning

confidence: 99%

Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins

Irie

Saeki

Kamisaki

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

123

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Several reports have described an activity that modifies nitrotyrosinecontaining proteins and their immunoreactivity to nitrotyrosine Abs. Without knowing the product of the reaction, this new activity has been called a ''denitrase.'' In those studies, some nonspecific proteins, which have multiple tyrosine residues, e.g., albumin, were used as a substrate. Therefore, the studies were based on an unknown mechanism of reaction and potentially a high background. To solve these problems, one of the most important things is to find a more suitable substrate for assay of the enzyme. We developed an assay strategy for determining the substrate for denitrase combining 2D-gel electrophoresis and an on-blot enzyme assay. The resulting substrate from RAW 264.7 cells was Histone H1.2, an isoform protein of linker histone. Histone H1.2 has only one tyrosine residue in the entire molecule, which ensures the exact position of the substrate to be involved. It has been reported that Histones are the most prominent nitrated proteins in cancer tissues. It was also demonstrated that tyrosine nitration of Histone H1 occurs in vivo. These findings lead us to the idea that Histone H1.2 might be an intrinsic substrate for denitrase. We nitrated recombinant and purified Histone H1.2 chemically and subjected it to an on-blot enzyme assay to characterize the activity. Denitrase activity behaved as an enzymatic activity because the reaction was time dependent and was destroyed by heat or trypsin treatment. The activity was shown to be specific for Histone H1.2, to differ from proteasome activity, and to require no additional cofactors.

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“…O ON participa de mecanismos fisiológicos muito importantes, agindo como mensageiro intracelular no controle do tônus vascular, na neurotransmissão, na produção de hormônios, na diferenciação celular, na expressão gênica e na ativação de células do sistema imune (19). Estas ações dependem da produção local e da disponibilidade da ONS, já que o ON é rapidamente consumido (20). A enzima que controla a produção do ON foi encontrada sob três formas homólogas: iONS (indutora), eONS (endotelial) e nONS (neuronal) (22).…”

Section: óXido Nítricounclassified