Interaction Between Nitric Oxide and Prostaglandin H Synthase

Tsai, Ah‐Lim; Wei, Chunhong; Kulmacz, Richard J.

doi:10.1006/abbi.1994.1400

Cited by 128 publications

(95 citation statements)

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“…To ascribe the reduced enhancement of PAF-induced pulmonary hypertension by L-NNA in the presence of NS 398 to an eect of NOS on COX activity may also be a matter of speculation. Anyway, our data from HLPs provide evidence that PAF-stimulated COX and NOS activities interact with each other, as reported for dierent stimulating agents in vitro (Tsai et al, 1994;Mollace et al, 1998;Watkins et al, 1997) and in vivo (Sautebin et al, 1995).…”

Section: Discussionsupporting

confidence: 79%

Nitric oxide (NO) modulation of PAF‐induced cardiopulmonary action: interaction between NO synthase and cyclo‐oxygenase‐2 pathways

Fabi¹,

Calabrese²,

Stati³

et al. 2001

British J Pharmacology

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1 To further investigate into the mechanisms of PAF-induced cardiopulmonary actions, we examined the eects of the nitric oxide synthase (NOS) inhibitor L-N o -nitro-L-arginine (L-NNA), of the speci®c cyclooxygenase-2 (COX-2) inhibitor NS 398, and of the combined presence of both COX and NOS inhibitors on the PAF responses in the heart lung preparation of guinea-pig (HLP). 2 In HLPs perfused with homologous blood, dose-response curves for the haemodynamic and bronchial eects of PAF (1 ± 32 ng) were carried out in the absence or presence of L-NNA (200 mM). L-NNA caused an increase in the resting pulmonary arterial pressure (PAP) without aecting the other basal values, and strongly potentiated the bronchoconstriction and pulmonary hypertension elicited by PAF. An enhancement of the PAF-induced actions on right atrial pressure (RAP) and cardiac output (CO) was also observed. All the eects of L-NNA were antagonized by L-arginine (2 mM).3 The presence of L-NNA in the perfusing blood of HLPs failed to aect the pulmonary hypertensive and bronchoconstrictor responses induced by the thromboxane A 2 mimetic U46619 (0.05 ± 1.6 mg), 5-hydroxytryptamine (0.1 ± 1.6 mg), and histamine (0.1 ± 1.6 mg), thus suggesting that these PAF secondary mediators are not responsible for the hyper-responsiveness to PAF induced by L-NNA.4 Blocking COX-2 pathway with NS 398 (15 ± 30 mM) did not alter the cardiopulmonary resting variables. However, a reduction of the PAF-mediated pulmonary hypertension, but not of bronchoconstriction, was observed. When L-NNA was added to the perfusing medium of HLPs pretreated with NS 398 or with indomethacin (15 mM), the basal PAP values were enhanced. However, in the combined presence of COX and NOS inhibitors, only a slight increase in the hypertensive responses to the highest doses of PAF was observed, whereas the PAF mediated actions at bronchial and cardiac level were unaected. 5 This study indicates that (i) the cardiopulmonary actions induced by PAF are speci®cally modulated by endogenous NO through the NOS pathway, and (ii) COX-2 isoform is involved in the pulmonary hypertensive, but not bronchoconstrictor, eects of PAF. Furthermore, an interaction between PAF stimulated COX, particularly COX-2, and NOS pathways appears to take a functional role at both bronchial and cardiovascular level.

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Section: Discussionsupporting

confidence: 79%

Nitric oxide (NO) modulation of PAF‐induced cardiopulmonary action: interaction between NO synthase and cyclo‐oxygenase‐2 pathways

Fabi¹,

Calabrese²,

Stati³

et al. 2001

British J Pharmacology

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“…PGI 2 is known to regulate processes such as vasodilation and inhibition of both platelet aggregation and smooth muscle cell proliferation (10,11). Investigations of the effect of NO • on purified PGHS-1 enzyme activity have been controversial with reports of activation (6,12,13) as well as inhibition (14)(15)(16). The reason for these reported differences may be due, in part, to the complexity of NO • chemistry, with the result that various NO x species are formed, that include (but are not limited to): nitrosonium ion (NO ϩ ), nitroxyl anion (NO Ϫ ), nitrite (NO 2 Ϫ ), nitrate (NO 3 Ϫ ), and peroxynitrite (ONOO Ϫ ) (17).…”

Section: Supplementary Abstract Peroxynitrite • Atherosclerosis • Cymentioning

confidence: 99%

“…These reactions were conducted in ammonium bicarbonate buffer (20 mM; pH 7.4) at ambient temperature for 1 h. For the reaction with 15 NO 2 • , the peptide was deaerated in a Thunberg cuvette using a vacuum/argon gas manifold and exposed to 15 NO 2 • gas (1 atm). When using ONOO Ϫ , we added ONOO Ϫ from a stock solution directly to the peptide; for experiments using TNM, we prepared a stock solution (200 mM) in ethanol; and when using NOC-7, we prepared a stock solution (10 mM) in deionized water.…”

Section: Preparation Of Samples For Mass Spectrometric and Uv/vis Spementioning

confidence: 99%

“…When using ONOO Ϫ , we added ONOO Ϫ from a stock solution directly to the peptide; for experiments using TNM, we prepared a stock solution (200 mM) in ethanol; and when using NOC-7, we prepared a stock solution (10 mM) in deionized water. Unless otherwise indicated, 5 mM peptide was reacted with equimolar concentrations of the NO x compound (in the case of 15 NO 2 • , we exposed 5 mM peptide to 1 atm 15 NO 2…”

Section: Preparation Of Samples For Mass Spectrometric and Uv/vis Spementioning

confidence: 99%

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Tyrosine nitration in prostaglandin H2 synthase

Deeb

Resnick

Mittar

et al. 2002

Journal of Lipid Research

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In this study, we investigated the effects of various nitrogen oxide (NO x ) species on the extent of prostaglandin H 2 synthase-1 (PGHS-1) nitration in purified protein and in vascular smooth muscle cells. We also examined PGHS-1 activity under these conditions and found the degree of nitration to correlate inversely with enzyme activity. In addition, since NO x species are thought to invoke damage during the pathogenesis of atherosclerosis, we examined human atheromatous tissue for PGHS-1 nitration. Both peroxynitrite and tetranitromethane induced Tyr nitration of purified PGHS-1, whereas 1-hydroxy-2-oxo-3-( Nmethyl-aminopropyl)-3-methyl-1-triazene (NOC-7; a nitric oxide-releasing compound) did not. Smooth muscle cells treated with peroxynitrite showed PGHS-1 nitration. The extent of nitration by specific NO x species was determined by electrospray ionization mass spectrometry. Tetranitromethane was more effective than peroxynitrite, NOC-7, and nitrogen dioxide at nitrating a tyrosine-containing peptide (12%, 5%, 1%, and Ͻ 1% nitration, respectively). Nitrogen dioxide and, to a lesser extent, peroxynitrite, induced dityrosine formation. Using UV/Vis spectroscopy, it was estimated that the reaction of PGHS-1 with excess peroxynitrite yielded two nitrated tyrosines/PGHS-1 subunit. Finally, atherosclerotic tissue obtained from endarterectomy patients was shown to contain nitrated PGHS-1.Thus, prolonged exposure to elevated levels of peroxynitrite may cause oxidative damage through tyrosine nitration. -Deeb, R.

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“…Previous reports showed that when inducible NO synthase (iNOS) was upregulated in inflammatory cells, COX-2 expression increased in a similar pattern (Surh et al, 2001). NO has been reported to activate or inhibit COX-2 activity, depending on the concentration of NO, the timing of its induction, and the investigated cell type (Salvemini et al, 1993;Stadler et al, 1993;Tsai et al, 1994;Habib et al, 1997).…”

Section: Introductionmentioning

confidence: 92%

Nitric oxide upregulates the cyclooxygenase-2 expression through the cAMP-response element in its promoter in several cancer cell lines

et al. 2005

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We previously showed that nitric oxide (NO) induces overexpression of cyclooxygenase-2 (COX-2) and production of prostaglandin E 2 in cancer cells. Here, we investigated the mechanisms by which NO induces COX-2 expression in cancer cells. We found that the cAMP-response element (CRE) is a critical factor in NOinduced COX-2 expression in all cells tested. We found that in cancer cells, three transcription factors (TFs) -cAMP response element-binding protein (CREB), activating transcription factor-2 (ATF-2) and c-jun, bound the CRE in the COX-2 promoter, and their activities were increased by addition of the NO donor, S-nitroso-Nacetyl-D,L-penicillamine (SNAP). NO-induced activation of soluble guanylate cyclase (sGC), p38 and c-Jun NH 2 -terminal kinase (JNK) upregulated the three TFs, leading to COX-2 overexpression. Addition of dibutyryl-cGMP (db-cGMP) induced COX-2 expression in a manner similar to SNAP; this induction was blocked by a p38 inhibitor (SB202190), but not by a JNK inhibitor (SP600125). NO-induced cGMP was found to activate CREB and ATF-2 in a p38, but not c-jun-dependent manner, while NO induced JNK in a cGMP-independent manner, leading to subsequent activation of c-jun and ATF-2. These results suggest that the low concentrations of endogenous NO present in cancer cell may induce the expression of many genes, including COX-2, which promotes the growth and survival of tumor cells.

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Interaction Between Nitric Oxide and Prostaglandin H Synthase

Cited by 128 publications

References 0 publications

Nitric oxide (NO) modulation of PAF‐induced cardiopulmonary action: interaction between NO synthase and cyclo‐oxygenase‐2 pathways

Nitric oxide (NO) modulation of PAF‐induced cardiopulmonary action: interaction between NO synthase and cyclo‐oxygenase‐2 pathways

Tyrosine nitration in prostaglandin H2 synthase

Nitric oxide upregulates the cyclooxygenase-2 expression through the cAMP-response element in its promoter in several cancer cell lines

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