Artículos de revistas: "Cyclic guanosine 3'"

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Boadu, Emmanuel, Svanhild Vaskinn, Elisabeth Sundkvist, Ragnhild Jaeger y Georg Sager. "Inhibition by guanosine cyclic monophosphate (cGMP) analogues of uptake of [3H]3′,5′-cGMP without stimulation of ATPase activity in human erythrocyte inside-out vesicles11Abbreviations: 3′,5′-cGMP, guanosine 3′,5′-cyclic monophosphate; 2′,3′-cGMP, guanosine 2′,3′-cyclic monophosphate; N-mb-cGMP, N2-monobutyryl guanosine 3′,5′-cyclic monophosphate; O-mb-cGMP, 2′-O-monobutyryl guanosine 3′,5′-cyclic monophosphate; Db-cGMP, N2,2′-O-dibutyryl guanosine 3′,5′-cyclic monophosphate; Br-cGMP, 8′-bromo guanosine 3′,5′-cyclic monophosphate; Rp-cGMPS, Rp-monophosphorothioate guanosine 3′,5′-cyclic monophosphate; Sp-cGMPS, Sp-monophosphorothioate guanosine 3′,5′-cyclic monophosphate; 3′,5′-cAMP, Adenosine 3′,5′-cyclic monophosphate; and MRP, multidrug resistance protein." Biochemical Pharmacology 62, n.º 4 (agosto de 2001): 425–29. http://dx.doi.org/10.1016/s0006-2952(01)00682-7.

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Meskini, N., O. MacOvschi, A. F. Prigent, G. Nemoz, P. Chapuy y M. Lagarde. "Decreased Cyclic Nucleotide Phosphodiesterase Activity in Human Peripheral Blood Mononuclear Cells from Elderly Women". Clinical Science 79, n.º 5 (1 de noviembre de 1990): 467–70. http://dx.doi.org/10.1042/cs0790467.

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1. Both adenosine 3′:5′-cyclic monophosphate and guanosine 3′:5′-cyclic monophosphate phosphodiesterase activities of peripheral blood mononuclear cells were markedly decreased in elderly women as compared with young control women. 2. In contrast, the ability of these cells to bind guanosine 5′-[β, γ-imido]triphosphate, a non-hydrolysable analogue of guanosine 5′-triphosphate, was the same in both groups. 3. These findings are discussed in the context of the decline in immune function which occurs with increasing age.

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3

Beste, Kerstin Y. y Roland Seifert. "cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1". Biological Chemistry 394, n.º 2 (1 de febrero de 2013): 261–70. http://dx.doi.org/10.1515/hsz-2012-0282.

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Abstract Adenosine 3′,5′-cyclic monophosphate and guanosine 3′,5′-cyclic monophosphate are second messengers that regulate multiple physiological functions. The existence of additional cyclic nucleotides in mammalian cells was postulated many years ago, but technical problems hampered development of the field. Using highly specific and sensitive mass spectrometry methods, soluble guanylyl cyclase has recently been shown to catalyze the formation of several cyclic nucleotides in vitro. This minireview discusses the broad substrate-specificity of soluble guanylyl cyclase and the possible second messenger roles of cyclic nucleotides other than adenosine 3′,5′-cyclic monophosphate and guanosine 3′,5′-cyclic monophosphate. We hope that this article stimulates productive and critical research in an area that has been neglected for many years.

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Srivastava, Uma S., Manohar Lal Thakur y C. Spach. "Cyclic 3′, 5′-adenosine monophosphate and cyclic 3′, 5′-guanosine monophosphate metabolism in malnutrition". Nutrition Research 6, n.º 5 (mayo de 1986): 589–99. http://dx.doi.org/10.1016/s0271-5317(86)80113-0.

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5

Santy, L. C. y G. Guidotti. "Reconstitution and characterization of two forms of cyclic nucleotide-gated channels from skeletal muscle". American Journal of Physiology-Endocrinology and Metabolism 271, n.º 6 (1 de diciembre de 1996): E1051—E1060. http://dx.doi.org/10.1152/ajpendo.1996.271.6.e1051.

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A cyclic nucleotide-gated channel present in skeletal muscle plasma membrane has previously been identified as being responsible for insulin-activated sodium entry into muscle cells (J. E. M. McGeoch and G. Guidotti. J. Biol. Chem. 267:832-841, 1992). We have isolated this channel activity to further study and characterize it. The channel was solubilized from rabbit skeletal muscle sarcolemma and functionally reconstituted into phospholipid vesicles, as assayed by patch-clamp analysis of the reconstituted proteins. Channel activity was isolated by 8-bromo-guanosine 3',5'-cyclic monophosphate affinity chromatography, producing two distinct peaks of cyclic nucleotide-gated channel activity. These two types of channel activity differ in guanosine 3',5'-cyclic monophosphate affinity and in the ability to be opened by adenosine 3',5'-cyclic monophosphate. The cyclic nucleotide-gated channel from rod outer segments also forms two peaks of activity when purified in this manner. The presence of two forms of channel activity could have implications for the mechanism of insulin-activated sodium entry.

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6

Seymour, Andrea A., Benoni Abboa-Offei, Magdi M. Asaad y W. Lynn Rogers. "Evaluation of SQ 28 603, an inhibitor of neutral endopeptidase, in conscious monkeys". Canadian Journal of Physiology and Pharmacology 69, n.º 10 (1 de octubre de 1991): 1609–17. http://dx.doi.org/10.1139/y91-238.

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The potent neutral endopeptidase inhibitor SQ 28 603 (N-(2-(mercaptomethyl)-1-oxo-3-phenylpropyl)-β-alanine) significantly increased excretion of sodium from 4.9 ± 2.3 to 14.3 ± 2.1 μequiv./min and cyclic 3′,5′-guanosine monophosphate from 118 ± 13 to 179 ± 18 pmol/min after intravenous administration of 300 μmol/kg (~80 mg/kg) in conscious female cynomolgus monkeys. SQ 28 603 did not change blood pressure or plasma atrial natriuretic peptide concentrations in the normal monkeys. In contrast, 1-h infusions of 3, 10, or 30 pmol∙kg−1∙min−1 of human atrial natriuretic peptide lowered blood pressure by −3 ± 4, −9 ± 4, and −27 ± 3 mmHg (1 mmHg = 133.322 Pa), increased cyclic guanosine monophosphate excretion from 78 ± 11 to 90 ± 6, 216 ± 33, and 531 ± 41 pmol/min, and raised plasma atrial natriuretic peptide from 7.2 ± 0.7 to 21 ± 4, 62 ± 12, and 192 ± 35 fmol/mL without affecting sodium excretion. In monkeys receiving 10 pmol∙kg−1∙min−1 of atrial natriuretic peptide, 300 μmol/kg of SQ 28 603 reduced mean arterial pressure by −13 ± 5 mmHg and increased sodium excretion from 6.6 ± 3.2 to 31.3 ± 6.0 μequiv./min, cyclic guanosine monophosphate excretion from 342 ± 68 to 1144 ± 418 pmol/min, and plasma atrial natriuretic peptide from 124 ± 8 to 262 ± 52 fmol/mL. In conclusion, SQ 28 603 stimulated renal excretory function in conscious monkeys, presumably by preventing the degradation of atrial natriuretic peptide by neutral endopeptidase.Key words: atrial natriuretic peptide, neutral endopeptidase, natriuresis, cyclic guanosine monophosphate.

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7

Pradelles, Philippe, Jacques Grassi, Danielle Chabardes y Nicole Guiso. "Enzyme immunoassays of adenosine cyclic 3',5'-monophosphate and guanosine cyclic 3',5'-monophosphate using acetylcholinesterase". Analytical Chemistry 61, n.º 5 (marzo de 1989): 447–53. http://dx.doi.org/10.1021/ac00180a014.

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8

Géigel, LF y LL Leon. "Cyclic 3'-5' guanosine monophosphate-dependent activity in Leishmania amazonensis". Memórias do Instituto Oswaldo Cruz 98, n.º 4 (junio de 2003): 499–500. http://dx.doi.org/10.1590/s0074-02762003000400012.

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9

Ślepokura, Katarzyna Anna. "Purine 3′:5′-cyclic nucleotides with the nucleobase in asynorientation: cAMP, cGMP and cIMP". Acta Crystallographica Section C Structural Chemistry 72, n.º 6 (6 de mayo de 2016): 465–79. http://dx.doi.org/10.1107/s2053229616006999.

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Purine 3′:5′-cyclic nucleotides are very well known for their role as the secondary messengers in hormone action and cellular signal transduction. Nonetheless, their solid-state conformational details still require investigation. Five crystals containing purine 3′:5′-cyclic nucleotides have been obtained and structurally characterized, namely adenosine 3′:5′-cyclic phosphate dihydrate, C10H12N5O6P·2H2O or cAMP·2H2O, (I), adenosine 3′:5′-cyclic phosphate 0.3-hydrate, C10H12N5O6P·0.3H2O or cAMP·0.3H2O, (II), guanosine 3′:5′-cyclic phosphate pentahydrate, C10H12N5O7P·5H2O or cGMP·5H2O, (III), sodium guanosine 3′:5′-cyclic phosphate tetrahydrate, Na+·C10H11N5O7P−·4H2O or Na(cGMP)·4H2O, (IV), and sodium inosine 3′:5′-cyclic phosphate tetrahydrate, Na+·C10H10N4O7P−·4H2O or Na(cIMP)·4H2O, (V). Most of the cyclic nucleotide zwitterions/anions [two from four cAMP present in total in (I) and (II), cGMP in (III), cGMP−in (IV) and cIMP−in (V)] aresynconformers about the N-glycosidic bond, and this nucleobase arrangement is accompanied by Crib—H...Npurhydrogen bonds (rib = ribose and pur = purine). The base orientation is tuned by the ribose pucker. An analysis of data obtained from the Cambridge Structural Database made in the context ofsyn–anticonformational preferences has revealed that among thesynconformers of various purine nucleotides, cyclic nucleotides and dinucleotides predominate significantly. The interactions stabilizing thesynconformation have been indicated. The inter-nucleotide contacts in (I)–(V) have been systematized in terms of the chemical groups involved. All five structures display three-dimensional hydrogen-bonded networks.

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10

Jackson, Edwin K., Zaichuan Mi, Keri Janesko-Feldman, Travis C. Jackson y Patrick M. Kochanek. "2′,3′-cGMP exists in vivo and comprises a 2′,3′-cGMP-guanosine pathway". American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 316, n.º 6 (1 de junio de 2019): R783—R790. http://dx.doi.org/10.1152/ajpregu.00401.2018.

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The discovery in 2009 that 2′,3′-cAMP exists in biological systems was rapidly followed by identification of 2′,3′-cGMP in cell and tissue extracts. To determine whether 2′,3′-cGMP exists in mammals under physiological conditions, we used ultraperformance LC-MS/MS to measure 2′,3′-cAMP and 2′,3′-cGMP in timed urine collections (via direct bladder cannulation) from 25 anesthetized mice. Urinary excretion rates (means ± SE) of 2′,3′-cAMP (15.5 ± 1.8 ng/30 min) and 2′,3′-cGMP (17.9 ± 1.9 ng/30 min) were similar. Mice also excreted 2′-AMP (3.6 ± 1.1 ng/20 min) and 3′-AMP (9.5 ± 1.2 ng/min), hydrolysis products of 2′,3′-cAMP, and 2′-GMP (4.7 ± 1.7 ng/30 min) and 3′-GMP (12.5 ± 1.8 ng/30 min), hydrolysis products of 2′,3′-cGMP. To validate that the chromatographic signals were from these endogenous noncanonical nucleotides, we repeated these experiments in mice ( n = 18) lacking 2′,3′-cyclic nucleotide 3′-phosphodiesterase (CNPase), an enzyme known to convert 2′,3′-cyclic nucleotides to their corresponding 2′-nucleotides. In CNPase-knockout mice, urinary excretions of 2′,3′-cAMP, 3′-AMP, 2′,3′-cGMP, and 3′-GMP were increased, while urinary excretions of 2′-AMP and 2′-GMP were decreased. Infusions of exogenous 2′,3′-cAMP increased urinary excretion of 2′,3′-cAMP, 2′-AMP, 3′-AMP, and adenosine, whereas infusions of exogenous 2′,3′-cGMP increased excretion of 2′,3′-cGMP, 2′-GMP, 3′-GMP, and guanosine. Together, these data suggest the endogenous existence of not only a 2′,3′-cAMP-adenosine pathway (2′,3′-cAMP → 2′-AMP/3′-AMP → adenosine), which was previously identified, but also a 2′,3′-cGMP-guanosine pathway (2′,3′-cGMP → 2′-GMP/3′-GMP → guanosine), observed here for the first time. Because it is well known that adenosine and guanosine protect tissues from injury, our data support the concept that both pathways may work together to protect tissues from injury.

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11

Lee, HC. "A Signaling Pathway Involving Cyclic ADP-Ribose, cGMP, and Nitric Oxide". Physiology 9, n.º 3 (1 de junio de 1994): 134–37. http://dx.doi.org/10.1152/physiologyonline.1994.9.3.134.

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Cyclic nucleotides are second messengers effecting changes mainly through protein phosphorylation. Cyclic ADP-ribose (cADPR), a newly discovered member, instead exerts its function through calcium mobilization. Increasing evidence suggests that cADPR may mediate the effects of nitric oxide on calcium, with guanosine 3', 5'-cyclic monophosphate serving as an intermediate.

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12

Liang, Xiao, Yu-Ru Chen, Wei Gao, Xing-Pan Guo, De-Wen Ding, Asami Yoshida, Kiyoshi Osatomi y Jin-Long Yang. "Effects on larval metamorphosis in the mussel Mytilus coruscus of compounds that act on downstream effectors of G-protein-coupled receptors". Journal of the Marine Biological Association of the United Kingdom 98, n.º 2 (11 de octubre de 2016): 333–39. http://dx.doi.org/10.1017/s0025315416001417.

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The metamorphic responses of mussel (Mytilus coruscus) larvae to pharmacological agents affecting G proteins and the adenylate cyclase/cyclic AMP (AC/cAMP) pathway were examined in the laboratory. The G protein activators guanosine 5′-[β,γ-imido]triphosphate trisodium salt hydrate and guanosine 5′-[γ-thio]triphosphate tetralithium salt only induced larval metamorphosis in continuous exposure assays, and the G protein inhibitor guanosine 5′-[β-thio]diphosphate trilithium salt did not exhibit inducing activity. The non-specific phosphodiesterase inhibitor theophylline and the cAMP-specific phosphodiesterase IV inhibitor 4-(3-Butoxy-4-methoxybenzyl)imidazolidin-2-one exhibited inducing activity, while the non-specific phosphodiesterase inhibitor 3-Isobutyl-1-methylxanthine only showed inducing activity at 10−4 M in continuous exposure assays. The cyclic nucleotide analogue N6,2′-O-Dibutyryladenosine 3′,5′-cyclic monophosphate sodium salt did not exhibit significant inducing activity. Both the adenylate cyclase activator forskolin and the adenylate cyclase inhibitor nitroimidazole exhibited inducing activity at 10−4 to 10−3 M concentrations in continuous exposure assays. Among these tested agents, the adenylate cyclase inhibitor (±)-miconazole nitrate salt showed the most promising inducing effect. The present results indicate that G protein-coupled receptors and signal transduction by AC/cAMP pathway could mediate metamorphosis of larvae in this species.

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13

Stolarski, Ryszard, Zygmunt Kazimierczuk, Piotr Lassota y David Shugar. "Acyclo Nucleosides and Nucleotides: Synthesis, Conformation and Other Properties, and Behaviour in Some Enzyme Systems, of 2′,3′-Seco Purine Nucleosides, Nucleotides and 3′:5′-Cyclic Phosphates, Analogues of cAMP and cGMP". Zeitschrift für Naturforschung C 41, n.º 7-8 (1 de agosto de 1986): 758–70. http://dx.doi.org/10.1515/znc-1986-7-816.

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Abstract The 3′:5′-cyclic phosphates of 2′,3′-secoadenosine and guanosine, structural analogues of cAMP and cGMP, were synthesized by cyclization of the 5′-phosphates of 2′,3′-secoadenosine and guanosine, respectively. The 2′,3′-seco-3′:5′-cAMP was converted to the IM P analogue by nitrous acid deamination, and to the 8-bromo analogue by bromination. Chemical phosphorylation of 2′,3′-secoadenosine gave four products, the major one of which, in 50% yield, was 2′,3′-seco-3′:5′-cAMP, identical to that obtained by the cyclization reaction above. The three other products have been tentatively identified. The conformations in solution of the seco nucleosides, their 5′-monophosphates, and their 3′:5′-cyclic phosphates, were determined with the aid of 1H , 13C and 31P NMR spectroscopy, particular attention being devoted to orientations about the C-O bonds and the glycosidic bond, and the results compared with crystallographic data available for the 2′,3′-seco congener of ribofuranosyl benzimidazole. The findings are briefly discussed in relation to substrate and inhibitor properties in some enzyme systems. Some of the foregoing compounds have been examined as potential enzyme substrates and inhibitors. In particular, the seco 3′:5′-cyclic phosphates are resistant to cAMP cyclic phos phodiesterase of mammalian origin, but are slowly hydrolyzed by purified higher plant cyclic nucleotide phosphodiesterase to the corresponding monophosphates.

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14

Mattana, J. y P. C. Singhal. "Effects of atrial natriuretic peptide and cGMP on uptake of IgG complexes by macrophages". American Journal of Physiology-Cell Physiology 265, n.º 1 (1 de julio de 1993): C92—C98. http://dx.doi.org/10.1152/ajpcell.1993.265.1.c92.

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Macromolecular handling by macrophages and glomerular mesangial cells may be important in the development of renal injury. We undertook the present study to determine whether atrial natriuretic peptide (ANP), a particulate guanylate cyclase stimulator, plays a direct role in uptake of immunoglobulin G (IgG) complexes by macrophages. Macrophages incubated with ANP at 10(-5) and 10(-6) M showed significantly suppressed uptake of IgG complexes compared with control. Macrophage uptake of IgG complexes was also significantly suppressed by the soluble guanylate cyclase stimulator sodium nitroprusside. Dibutyryl guanosine 3',5'-cyclic monophosphate and dibutyryl adenosine 3',5'-cyclic monophosphate both significantly suppressed IgG complex uptake as well. ANP was found to significantly enhance macrophage guanosine 3',5'-cyclic monophosphate (cGMP) levels compared with control cells, and this effect was antagonized by angiotensin II. Angiotensin II significantly enhanced uptake of IgG complexes and suppressed macrophage adenosine 3',5'-cyclic monophosphate synthesis, and both effects were antagonized by coincubation with ANP. These results suggest that ANP modulates uptake of IgG complexes by macrophages and that this effect may be mediated via cGMP.

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15

Lauria, Michele R., Cynthia A. Standley, Yoram Sorokin, Jill C. Todt, Sidney F. Bottoms, Frank D. Yelian y David B. Cotton. "Brain Natriuretic Peptide and Cyclic Guanosine-3′,5′ Monophosphate in Preeclampsia". Journal of Maternal-Fetal and Neonatal Medicine 5, n.º 3 (enero de 1996): 128–31. http://dx.doi.org/10.3109/14767059609025412.

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Son, Jong-Keun y John P. N. Rosazza. "Cyclic Guanosine-3′,5′-Monophosphate and Biopteridine Biosynthesis in Nocardia sp". Journal of Bacteriology 182, n.º 13 (1 de julio de 2000): 3644–48. http://dx.doi.org/10.1128/jb.182.13.3644-3648.2000.

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ABSTRACT Nocardia sp. strain NRRL 5646 contains a nitric oxide synthase (NOS) enzyme system capable of generating nitric oxide (NO) from arginine and arginine-containing peptides. To explain possible roles of the NOS system in this bacterium, guanylate cyclase (GC) and tetrahydrobiopterin (H4B) biosynthetic enzymes were identified in cell extracts and in culture media. Cell extracts contained GC activity, as measured by the conversion of GTP to cyclic guanosine-3′,5′-monophosphate (cGMP) at 9.56 pmol of cGMP h−1 mg of protein−1. Concentrations of extracellular cGMP in culture media were significantly increased, from average control levels of 45 pmol cGMP liter−1 to a maximum of 315 pmol liter−1, in response to additions of GTP, l-arginine, H4B, and sodium nitroprusside to growing Nocardia cultures. On the other hand, the NOS inhibitor N G-nitro-l-arginine and the GC inhibitor 1H-[1,2,4]oxadiazole[4,3-a]quinoxalin-1-one both dramatically decreased extracellular cGMP levels. Activities for GTP-cyclohydrase-1,6-pyruvoyltetrahydropterin synthase and sepiapterin reductase, enzymes essential for H4B biosynthesis, were present in Nocardia culture extracts at 77.5 pmol of neopterin and 45.8 pmol of biopterin h−1 mg of protein−1, respectively. In Nocardia spp., as in mammals, GTP is a key intermediate in H4B biosynthesis, and GTP is converted to cGMP by a GC enzyme system that is activated by NO.

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Zaffalon, F. G., C. Guimmelette, C. L. V. Leal y F. J. Richard. "268 CYCLIC GUANOSINE MONOPHOSPHATE INHIBITS PHOSPHODIESTERASE 3 ACTIVITY IN PORCINE OOCYTES". Reproduction, Fertility and Development 25, n.º 1 (2013): 282. http://dx.doi.org/10.1071/rdv25n1ab268.

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The level of cyclic adenosine monophosphate (cAMP) within oocytes has been shown to play a critical role in maintaining meiotic arrest. High levels of intracellular cAMP prevent spontaneous oocyte maturation in vitro, whereas a decrease in oocyte cAMP is associated with the resumption of meiosis. Another cyclic nucleotide that also was recently proposed as being involved in meiotic resumption is cyclic guanosine monophosphate (cGMP), which could be regulating phosphodiesterase (PDE) 3 activity. The aim of this study was to determine whether cGMP inhibits cAMP-PDE activity in porcine oocytes. With the method described previously by Sasseville et al. (2006 BMC Dev. Biol. 6, 47), PDE activity was measured in groups of 10 oocytes cultured in the absence (control) or presence of different concentrations of cGMP (1, 3, 10, 30, 100, 300, 1000, and 3000 nM) or with the PDE3 inhibitor cilostamide (10 µM). Before assaying PDE activity, the cumulus–oocyte complexes (COC) were matured in vitro for 24 h in the presence of pregnant mare serum gonadotropin (5 IU) and hCG (5 IU) at 38.5°C in 5% CO2. The COC were homogenised in a hypotonic buffer. Data were analysed using one-way ANOVA followed by Duncan’s post-hoc test. Differences with P < 0.05 were considered significant. Results showed that 300, 1000, and 3000 nM cGMP inhibited PDE3 activity (7.9, 5.1, and 4.1 fmol min–1 per COC; P < 0.05) at levels below the controls (13.2 fmol min–1 per COC) and were similar to the activity observed in the presence of (2.4 fmol min–1 per COC; P > 0.05). The other concentrations tested were similar to activity levels seen in the control (1 to 100 nM; 12.2, 11.3, 10.8, 11.5, and 10.4; P > 0.05). In conclusion, the results support the concept that increasing concentrations of cGMP inhibit PDE activity, suggesting the inhibition of the predominant form of cAMP-PDE present in porcine oocytes, PDE3. These results support the hypothesis that cGMP inhibits PDE activity in porcine oocytes. Further work is needed to determine the role this plays in maintaining high cAMP levels and inhibiting oocyte nuclear maturation. Financial support from FGZ FAPESP 2010/20188-6 and 2010/18023-9 is acknowledged.

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Siragy, H. M., R. A. Johns, M. J. Peach y R. M. Carey. "Nitric oxide alters renal function and guanosine 3',5'-cyclic monophosphate." Hypertension 19, n.º 6_pt_2 (junio de 1992): 775–79. http://dx.doi.org/10.1161/01.hyp.19.6.775.

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19

Navarro, José Antonio, Félix Javier Jiménez-Jiménez, José Antonio Molina, Julián Benito-León, Elena Cisneros, Teresa Gasalla, Miguel Ortı́-Pareja, Antonio Tallón-Barranco, Fernando de Bustos y Joaquı́n Arenas. "Cerebrospinal fluid cyclic guanosine 3′5′ monophosphate levels in Parkinson's disease". Journal of the Neurological Sciences 155, n.º 1 (febrero de 1998): 92–94. http://dx.doi.org/10.1016/s0022-510x(97)00267-0.

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20

Teran, Enrique, Carlos Escudero, Sandra Vivero, Armando Enriquez y Andres Calle. "Intraplatelet Cyclic Guanosine‐3′,5′‐Monophosphate Levels During Pregnancy and Preeclampsia". Hypertension in Pregnancy 23, n.º 3 (enero de 2004): 303–8. http://dx.doi.org/10.1081/prg-200030860.

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21

Wu, Chung-Pu, Hannah Woodcock, Stephen B. Hladky y Margery A. Barrand. "cGMP (guanosine 3′,5′-cyclic monophosphate) transport across human erythrocyte membranes". Biochemical Pharmacology 69, n.º 8 (abril de 2005): 1257–62. http://dx.doi.org/10.1016/j.bcp.2005.02.005.

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22

Stroiński, A. y J. Floryszak-Wieczorek. "Guanosine 3′:5′-cyclic monophosphate changes during germination of Hordeum vulgare". Plant Science 42, n.º 1 (diciembre de 1985): 1–4. http://dx.doi.org/10.1016/0168-9452(85)90020-2.

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23

Reyes-Harde, Magali, Barry V. L. Potter, Antony Galione y Patric K. Stanton. "Induction of Hippocampal LTD Requires Nitric-Oxide-Stimulated PKG Activity and Ca2+ Release From Cyclic ADP-Ribose-Sensitive Stores". Journal of Neurophysiology 82, n.º 3 (1 de septiembre de 1999): 1569–76. http://dx.doi.org/10.1152/jn.1999.82.3.1569.

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Long-term depression (LTD) of synaptic transmission can be induced by several mechanisms, one thought to involve Ca2+-dependent activation of postsynaptic nitric oxide (NO) synthase and subsequent diffusion of NO to the presynaptic terminal. We used the stable NO donor S-nitroso- N-acetylpenicillamine (SNAP) to study the NO-dependent form of LTD at Schaffer collateral-CA1 synapses in vitro. SNAP (100 μM) enhanced the induction of LTD via a cascade that was blocked by the N-methyl-d-aspartate receptor antagonist d-2-amino-5-phosphonopentanoic acid (50 μM), NO guanylyl cyclase inhibitor 1H-[1,2,4] oxadiazolo [4,3-a] quinoxalin-1-one (10 μM), and the PKG inhibitor KT5823 (1 μM). We further show that LTD induced by low-frequency stimulation in the absence of SNAP also is blocked by KT5823 or Rp-8-(4-chlorophenylthio)-guanosine 3′,5′-cyclic monophosphorothioate (10 μM), cyclic guanosine 3′,5′ monophosphate-dependent protein kinase (PKG) inhibitors with different mechanisms of action. Furthermore SNAP-facilitated LTD was blocked when release from intracellular calcium stores was inhibited by ryanodine (10 μM). Finally, two cell-permeant antagonists of the cyclic ADP-ribose binding site on ryanodine receptors also were able to block the induction of LTD. These results support a cascade for induction of homosynaptic, NO-dependent LTD involving activation of guanylyl cyclase, production of guanosine 3′,5′ cyclic monophosphate and subsequent PKG activation. This process has an additional requirement for release of Ca2+ from ryanodine-sensitive stores, perhaps dependent on the second-messenger cyclic ADP ribose.

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Garty, H., O. Yeger, A. Yanovsky y C. Asher. "Guanosine nucleotide-dependent activation of the amiloride-blockable Na+ channel". American Journal of Physiology-Renal Physiology 256, n.º 5 (1 de mayo de 1989): F965—F969. http://dx.doi.org/10.1152/ajprenal.1989.256.5.f965.

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Effects of guanosine nucleotides on the epithelial Na+ channel were studied in apical membrane vesicles derived from the toad bladder epithelium. Trapping 10 microM guanosine-5'-O-(thiotriphosphate) (GTP gamma S) in vesicles evoked two- to fourfold increase in the amiloride-sensitive (Na+ channel-mediated) 22Na+ uptake. The nucleotide had no significant effect on the amiloride-insensitive 22Na+ uptake or the valinomycin-mediated 86Rb+ uptake in the same membranes. The stimulatory action of GTP gamma S was mimicked by 5'-guanylylimidiodiphosphate (GppNHp) and could at least partly be reversed by guanosine-5'-O-(thiodiphosphate) (GDP beta S) (10-fold excess). GTP itself and adenosine-5'-O-(thiotriphosphate) (ATP gamma S) had no sustained effect on Na+ transport in vesicles. Thus it appears that the epithelial Na+ channel is directly or indirectly regulated by the occupancy of a guanosine-specific site, probably the alpha subunit of a G protein. The possibility that GTP gamma S acts indirectly by activating a membrane-bound, GTP-dependent enzyme the product of which modulates the channel conductance was assessed by measuring 22Na+ fluxes in membrane vesicles prepared to contain products of such enzymes. None of the reagents tested [adenosine 3',5' cyclic monophosphate (cAMP), guanosine 3',5y cyclic monophosphate (cGMP), inositol 1,4,5-trisphosphate (IP3), and diacylglycerol (DAG)] increased the tracer flux in vesicles or altered its response to GTP gamma S.

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25

ERENMEMİŞOĞLU, Aydın, Cem SÜER, Sadun TEMOÇİN y Hüseyin BEYDAĞI. "The Possible Role of 3':5'- Cyclic Guanosine Monophosphate in Acetylcholine-Mediated Concraction of Isolated Rat Duodenum". European Journal of Therapeutics 5, n.º 1 (1 de enero de 1994): 16–20. http://dx.doi.org/10.58600/eurjther.1994-5-1-1369-arch.

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This study was planned to determine whether the possible role of 3':5'-cyclic guanosine monophosphate (cylic GMP) on acetylcholine(ACh) action in isolated rat duodenum. Therefore, sodium nitroprusside(SNP) and methylene blue(MB) were used as a guanylate cyclase activator and inhibitor respectively. MB caused significant fall in ACh-induced contraction peaks, whereas SNP did not alter them. These results suggested that cyclic GMP may play a role for ACh action in isolated duodenum smooth muscle. However further experiments are necessary to determine whether a causal relationship exists between cyclic GMP and ACh action.

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26

Kamynina, Alisa, Sebastian Guttzeit, Philip Eaton y Friederike Cuello. "Nitroxyl Donor CXL-1020 Lowers Blood Pressure by Targeting C195 in Cyclic Guanosine-3’,5’-Monophosphate-Dependent Protein Kinase I". Hypertension 79, n.º 5 (mayo de 2022): 946–56. http://dx.doi.org/10.1161/hypertensionaha.122.18756.

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Background: We previously demonstrated that nitroxyl causes vasodilation, at least in part, by inducing the formation of an intradisulfide bond between C117 and C195 in the high affinity cyclic guanosine monophosphate-binding site of PKGI (cyclic guanosine monophosphate-dependent protein kinase I). The aim of this study was to determine whether nitroxyl donors lower blood pressure via this novel PKGI activation mechanism in vivo. Methods: To determine this, a C195S PKGI knock-in mouse model was generated that ubiquitously and constitutively expresses a mutant kinase resistant to nitroxyl-induced intradisulfide activation. Results: Knock-in and wild-type littermates did not differ in appearance, body weight, in PKGI protein expression or blood gas content. Organ weight was similar between genotypes apart from the cecum that was significantly enlarged in knock-in animals. Mean arterial pressure and heart rate monitored in vivo over 24 hours by radio-telemetry revealed neither a significant difference between genotypes at baseline nor during angiotensin II–induced hypertension or sepsis. CXL-1020, a clinically relevant nitroxyl donor, did not lower blood pressure in normotensive animals. In contrast, administering CXL-1020 to hypertensive wild-type mice reduced their blood pressure by 10±4 mm Hg ( P =0.0184), whereas the knock-in littermates were unaffected. Conclusions: Oxidation of C195 in PKGI contributes to the antihypertensive effects observed in response to nitroxyl donors, emphasising the potential importance of nitroxyl donors in pathological scenarios when cyclic guanosine monophosphate levels are reduced and insufficient to activate PKGI.

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Prakash, Y. S., Adeyemi Iyanoye, Binnaz Ay, Gary C. Sieck y Christina M. Pabelick. "Store-operated Ca2+Influx in Airway Smooth Muscle". Anesthesiology 105, n.º 5 (1 de noviembre de 2006): 976–83. http://dx.doi.org/10.1097/00000542-200611000-00019.

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Background Volatile anesthetics produce bronchodilation in part by depleting sarcoplasmic reticulum Ca stores in airway smooth muscle (ASM). Other bronchodilatory drugs are known to act via cyclic nucleotides (cyclic adenosine 3',5'-cyclic monophosphate, cyclic guanosine 3',5'-cyclic monophosphate). Intracellular Ca regulation in ASM involves plasma membrane Ca influx, including that triggered by sarcoplasmic reticulum Ca depletion (store-operated Ca entry [SOCE]). The authors hypothesized that anesthetics and bronchodilatory agents interact in inhibiting SOCE, thus enhancing ASM relaxation. Methods In enzymatically dissociated porcine ASM cells imaged using fluorescence microscopy, sarcoplasmic reticulum Ca was depleted by 1 microm cyclopiazonic acid in 0 extracellular Ca, nifedipine, and potassium chloride (preventing Ca influx through L-type channels and SOCE). Extracellular Ca was rapidly reintroduced to selectively activate SOCE in the presence or absence of 1 minimum alveolar concentration (MAC) halothane, isoflurane, or sevoflurane. Anesthetic interference with SOCE regulation by cyclic nucleotides was examined by activating SOCE in the presence of (1) 1 microm acetylcholine, (2) 100 microm dibutryl cyclic adenosine 3',5'-cyclic monophosphate, or (3) 100 microm 8-bromo-cyclic guanosine 3',5'-cyclic monophosphate. Results SOCE was enhanced by acetylcholine, whereas volatile anesthetics and both cyclic nucleotides partially inhibited Ca influx. Preexposure to 1 or 2 MAC anesthetic (halothane > isoflurane > sevoflurane) inhibited SOCE. Only halothane and isoflurane inhibited acetylcholine-induced augmentation of Ca influx, and significantly potentiated cyclic nucleotide inhibition such that no influx was observed in the presence of anesthetics and cyclic nucleotides. Conclusions These data indicate that volatile anesthetics prevent sarcoplasmic reticulum refilling by inhibiting SOCE and enhancing cyclic nucleotide blunting of Ca influx in ASM. Such interactions likely result in substantial airway relaxation in the presence of both anesthetics and bronchodilatory agents such as beta agonists or nitric oxide.

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28

Range, Simon P., Elaine D. Holland, Graham P. Basten y Alan J. Knox. "Regulation of guanosine 3′:5′-cyclic monophosphate in ovine tracheal epithelial cells". British Journal of Pharmacology 120, n.º 7 (marzo de 1997): 1249–54. http://dx.doi.org/10.1038/sj.bjp.0701040.

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Burke-Wolin, T., C. J. Abate, M. S. Wolin y G. H. Gurtner. "Hydrogen peroxide-induced pulmonary vasodilation: role of guanosine 3',5'-cyclic monophosphate". American Journal of Physiology-Lung Cellular and Molecular Physiology 261, n.º 6 (1 de diciembre de 1991): L393—L398. http://dx.doi.org/10.1152/ajplung.1991.261.6.l393.

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Hydrogen peroxide (H2O2), but not tertbutyl hydroperoxide, produces a concentration-dependent vasodilation of the pulmonary circulation in isolated saline perfused rabbit lungs when pulmonary arterial pressures (PAP) are raised with the thromboxane analogue U-46619. This vasodilation was enhanced in the presence of indomethacin, suggesting that H2O2 possesses both a prostaglandin-mediated constrictor and an additional dilator mechanism. In isolated rabbit intrapulmonary arteries the endothelium did not alter the dose-dependent relaxation of arterial rings to H2O2, and indomethacin enhanced the relaxant response of the peroxide. The decrease in PAP and relaxation of isolated pulmonary arteries observed with H2O2 was attenuated with 10 microM methylene blue, an inhibitor of soluble guanylate cyclase activation. M & B 22948, a guanosine 3',5'-cyclic monophosphate (cGMP)-selective phosphodiesterase inhibitor, enhanced the vasodilation or relaxation to the peroxide in both preparations. These changes were not endothelium dependent. Inhibition of the cGMP-associated endothelium-derived relaxant factor (EDRF) with nitro-L-arginine, did not alter relaxation of arterial rings to peroxide. Thus H2O2 appears to produce pulmonary vasodilation through the activation of guanylate cyclase and accumulation of cGMP. Both H2O2 and EDRF may function as tonic stimulators of guanylate cyclase in the pulmonary circulation and contribute to the maintenance of low basal pressures.

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30

Hegde, V. R., H. Wittreich, M. G. Patel, A. C. Horan, R. F. Hart, J. J. Troyanovich, M. S. Puar y V. P. Gullo. "Naturally produced isocoumarins: inhibitors of calmodulinsensitive cyclic guanosine 3′,5′-monophosphate phosphodiesterase". Journal of Industrial Microbiology 4, n.º 3 (mayo de 1989): 209–13. http://dx.doi.org/10.1007/bf01574078.

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31

Cummings, James J. y Huamei Wang. "Nitric oxide decreases lung liquid production via guanosine 3′,5′-cyclic monophosphate". American Journal of Physiology-Lung Cellular and Molecular Physiology 280, n.º 5 (1 de mayo de 2001): L923—L929. http://dx.doi.org/10.1152/ajplung.2001.280.5.l923.

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We studied the role of cGMP in nitric oxide (NO)-induced changes in lung liquid production ( J v ) in chronically instrumented fetal sheep. Forty-five studies were done in which J v was measured by a tracer dilution technique. Left pulmonary arterial flow (Qlpa) was measured by a Doppler flow probe. There were two series of experiments. In the first, we gave 8-bromo-cGMP, a cGMP analog, by either the pulmonary vascular or intraluminal route; in the second, we used agents to inhibit or enhance endogenous cGMP activity. When infused directly into the pulmonary circulation, 8-bromo-cGMP significantly increased Qlpa but had no effect on J v. Conversely, when instilled into the lung liquid, 8-bromo-cGMP had no effect on Qlpa but significantly reduced J v. Inhibition of guanylate cyclase activity with methylene blue totally blocked, whereas phosphodiesterase inhibition with Zaprinast significantly enhanced, the effect of instilled NO on J v. Thus the reduction in lung liquid caused by NO appears to be mediated by cGMP, perhaps through a direct effect on the pulmonary epithelium.

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32

Sugawa, Makoto, Kazuhiko Tamura, Tohru Koide y Shigetaka Naitoh. "Functional roles of cyclic guanosine 3′,5′-monophosphate analogue in cerebral vasodilation". General Pharmacology: The Vascular System 24, n.º 3 (mayo de 1993): 577–84. http://dx.doi.org/10.1016/0306-3623(93)90214-i.

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33

Lauria, Michele R., Cynthia A. Standley, Yoram Sorokin, Jill C. Todt, Sidney F. Bottoms, Frank D. Yellan y David B. Cotton. "Brain natriuretic peptide and cyclic guanosine-3?,5? monophosphate in pre-eclampsia". Journal of Maternal-Fetal Medicine 5, n.º 3 (mayo de 1996): 128–31. http://dx.doi.org/10.1002/(sici)1520-6661(199605/06)5:3<128::aid-mfm6>3.0.co;2-o.

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34

Henrich, W. L., E. A. McAllister, P. B. Smith y W. B. Campbell. "Guanosine 3',5'-cyclic monophosphate as a mediator of inhibition of renin release". American Journal of Physiology-Renal Physiology 255, n.º 3 (1 de septiembre de 1988): F474—F478. http://dx.doi.org/10.1152/ajprenal.1988.255.3.f474.

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The role of guanosine 3',5'-cyclic monophosphate (cGMP) as an inhibitory mediator of tissue renin release was examined in two different in vitro preparations. In rat superficial cortical slices, renin release stimulated by isoproterenol (10(-5) M) was ablated by atriopeptin III (ANP, 2.1 x 10(-8) M), nitroprusside (NP, 10(-3) M), and 8-bromoguanosine 3',5'-cyclic monophosphate (8-BrcGMP, 10(-3) and 10(-6) M). Arachidonic acid (10(-3) M)-stimulated renin release was also inhibited by ANP and 8-BrcGMP (10(-3) and 10(-6) M). Both ANP and NP increased tissue cGMP concentrations significantly (P less than 0.05), but neither had an effect on adenosine 3',5'-cyclic monophosphate (cAMP) concentrations. When methylene blue (10(-5) M), an inhibitor of guanylate cyclase, was added to slices incubated with isoproterenol and ANP, the inhibition of renin release by ANP was abolished. These results were confirmed in a preparation of isolated cultured rat juxtaglomerular cells. In these cells, isoproterenol induced a significant increase (58%, P less than 0.01) in renin release, which was inhibited by the addition of 8-BrcGMP (10(-6) M). These data demonstrate a direct inhibitory effect of ANP on isoproterenol- and arachidonic acid-induced renin release. The results with NP, 8-BrcGMP, and methylene blue suggest that cGMP is an intracellular mediator of this inhibition.

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35

De Vente, J., H. W. M. Steinbusch y J. Schipper. "A new approach to immunocytochemistry of 3′,5′-cyclic guanosine monophosphate: Preparation, specificity, and initial application of a new antiserum against formaldehyde-fixed 3′,5′-cyclic guanosine monophosphate". Neuroscience 22, n.º 1 (julio de 1987): 361–73. http://dx.doi.org/10.1016/0306-4522(87)90226-0.

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36

Engelhardt, MD, PhD, FRCA, Thomas, Christian Zaarour, MD y Mark W. Crawford, MBBS, FRCPC. "Plasma cyclic guanosine 3′,5′-monophosphate levels: A marker of glutamate-nitric oxide-guanyl cyclase activity?" Journal of Opioid Management 7, n.º 6 (1 de noviembre de 2017): 462–66. http://dx.doi.org/10.5055/jom.2011.0087.

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Objectives: Remifentanil-based anesthesia can lead to acute opioid tolerance and/or hyperalgesia. A low-dose intraoperative infusion of the N-methyl-D-aspartate (NMDA) receptor antagonist ketamine did not result in reduced postoperative morphine consumption after remifentanil-based anesthesia in adolescents. This study investigates the potential role of the glutamate-nitric oxide-cyclic guanosine 3′,5′-monophosphate (cyclic GMP) pathway in the failure of low-dose ketamine to prevent remifentanil-induced acute opioid tolerance and/or hyperalgesia.Design and setting: Prospective, double-blind, placebo-controlled randomized clinical trial at a university teaching hospital.Patients, participants, and interventions: Thirty-four adolescents receiving remifentanil-based anesthesia for surgical correction of idiopathic scoliosis were randomly assigned to receive either intraoperative ketamine administered as a bolus dose of 0.5 mg/kg in 10 mL of normal saline and a continuous intravenous infusion of 4.0 μg/kg/min or an equal volume of saline.Main outcome measures: Blood samples were collected before and after the administration of ketamine for analyzing the concentrations of cyclic GMP, ketamine, and norketamine. Blood samples were analyzed using high-performance liquid chromatography and an enzyme immunoassay.Results: The median (interquartile range) value of the concentration of plasma cyclic GMP decreased from 23.7 (17.4-26.7) to 14.8 (14.0-17.3) nmol/L after ketamine infusion (p 0.005) and from 23.9 (16.3-29.2) to 16.3 (14.5-18.6) nmol/L after saline infusion (p 0.005). The median value of the concentration of plasma cyclic GMP at the end of ketamine infusion did not differ significantly when compared with that after saline infusion (p = 0.07). The concentration of plasma cyclic GMP was inversely correlated with the concentration of plasma ketamine (r = −0.61).Conclusions: This study suggests that the low dose of intraoperative ketamine infused was insufficient to suppress the NMDA receptor pathway. The concentrations of plasma cyclic GMP may serve as an indirect biological marker of ketamine-induced NMDA receptor antagonism.

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Bell, Gordon M., Steven A. Atlas, Mark Pecker, Jean E. Sealey, Gary James y John H. Laragh. "Diurnal and Postural Variations in Plasma Atrial Natriuretic Factor, Plasma Guanosine 3′:5′-Cyclic Monophosphate and Sodium Excretion". Clinical Science 79, n.º 4 (1 de octubre de 1990): 371–76. http://dx.doi.org/10.1042/cs0790371.

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1. We studied diurnal patterns of plasma atrial natriuretic factor, plasma guanosine 3′:5′-cyclic monophosphate and urinary sodium excretion in normal subjects after 3 days on a 200 mmol of sodium/60 mmol of potassium diet. On the fourth day blood samples and urine were collected every 3 h. 2. Two studies were performed. In study 1, normal subjects (n = 8) were recumbent for 23 h from 09.00 hours to 08.00 hours the next day. In study 2, normal subjects (n = 10) were permitted to ambulate from 09.00 hours to 23.00 hours and then were recumbent until 08.00 hours the next day. 3. In study 1, assumption of the recumbent posture was associated with increases in plasma atrial natriuretic factor (P < 0.01), plasma guanosine 3′:5′-cyclic monophosphate (P < 0.05) and urinary sodium excretion (P < 0.05). 4. In contrast, in study 2 there were no significant changes in plasma atrial natriuretic factor during the day; instead, plasma atrial natriuretic factor increased overnight, reaching a peak at 24.00 hours after 1 h of recumbency (P < 0.01). A smaller rise in plasma guanosine 3′:5′-cyclic monophosphate (P < 0.05) occurred; urinary sodium excretion decreased markedly (P < 0.01) and there was no change in creatinine clearance. 5. In both studies, recumbency was associated with an initial drop, followed by a rise, in packed cell volume. 6. These data demonstrate that assumption of the supine position induces a rise in plasma atrial natriuretic factor and accounts for most of the observed variation. This is associated with natriuresis during the day, but it does not reverse the pattern of antinatriuresis that occurs at night. Instead, changes in plasma atrial natriuretic factor appear to reflect and, in turn, influence changes in intravascular volume.

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38

Lewis, Helen M., M. R. Wilkins, M. J. Kendall y M. R. Lee. "Carbidopa Does Not Affect the Renal Response to Atrial Natriuretic Factor in Man". Clinical Science 77, n.º 3 (1 de septiembre de 1989): 281–85. http://dx.doi.org/10.1042/cs0770281.

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1. The dependence of atrial natriuretic factor on renal dopamine for its renal effects in man was examined in 10 healthy volunteers using the dopa decarboxylase inhibitor carbidopa. 2. Each volunteer attended on two occasions, and received an infusion of atrial natriuretic factor (4 pmol min−1 kg−1) for 60 min after pretreatment with either placebo or carbidopa orally. These were administered in random, double-blind fashion. 3. A similar increase in plasma atrial natriuretic factor concentration was seen after atrial natriuretic factor infusion on both visits. 4. Infusion of atrial natriuretic factor produced a small unsustained rise in urinary dopamine excretion. This increase in urinary dopamine excretion was blocked by carbidopa with no effect on the natriuresis. 5. Urinary guanosine 3′:5′-cyclic monophosphate excretion increased in response to the atrial natriuretic factor infusion whether placebo or carbidopa was given. Guanosine 3′:5′-cyclic monophosphate, but not dopamine, may be a mediator of the renal response to atrial natriuretic factor in man.

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39

Jarratt-Barnham, Edwin, Limin Wang, Youzheng Ning y Julia M. Davies. "The Complex Story of Plant Cyclic Nucleotide-Gated Channels". International Journal of Molecular Sciences 22, n.º 2 (16 de enero de 2021): 874. http://dx.doi.org/10.3390/ijms22020874.

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Plant cyclic nucleotide-gated channels (CNGCs) are tetrameric cation channels which may be activated by the cyclic nucleotides (cNMPs) adenosine 3′,5′-cyclic monophosphate (cAMP) and guanosine 3′,5′-cyclic monophosphate (cGMP). The genome of Arabidopsis thaliana encodes 20 CNGC subunits associated with aspects of development, stress response and immunity. Recently, it has been demonstrated that CNGC subunits form heterotetrameric complexes which behave differently from the homotetramers produced by their constituent subunits. These findings have widespread implications for future signalling research and may help explain how specificity can be achieved by CNGCs that are known to act in disparate pathways. Regulation of complex formation may involve cyclic nucleotide-gated channel-like proteins.

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40

Cousson, A. "Indolyl-3-butyric acid-induced Arabidopsis stomatal opening mediated by 3′,5′-cyclic guanosine-monophosphate". Plant Physiology and Biochemistry 48, n.º 12 (diciembre de 2010): 977–86. http://dx.doi.org/10.1016/j.plaphy.2010.09.007.

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41

Xiao, Linsheng, Carl-Gustaf Nilsson y Peter H. E. Eneroth. "Cyclic guanosine 3′,5′-monophosphate mediates 3-morpholinosydnonimine-induced inhibition of human natural killer cells". Biochemical Pharmacology 50, n.º 2 (julio de 1995): 147–53. http://dx.doi.org/10.1016/0006-2952(95)00125-j.

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42

Babic, Goran, Slobodan Novokmet y Slobodan Jankovic. "Changes of platelets’ function in preeclampsia". Open Medicine 6, n.º 6 (1 de diciembre de 2011): 696–700. http://dx.doi.org/10.2478/s11536-011-0076-3.

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AbstractIncreased aggregation of platelets during preeclampsia was shown in several studies, yet several others reported no change. The aim of our study was to investigate platelet aggregation in a group of patients suffering from preeclampsia. In a cross-sectional study blood samples were taken from 89 hospitalized patients in the third trimester of pregnancy: 38 were suffering from mild to moderate preeclampsia and 51 patients were without preeclampsia. From the blood samples platelet aggregation, secretion of adenine nucleotides from platelets, concentration of energy-rich adenine compounds and levels of cyclic adenosine-mono-phosphate and cyclic guanosine mono-phosphate in platelets were measured. In the patients with preeclampsia, the adenosine diphosphate threshold for biphasic aggregation [odds ratio (OR):.75; 95% Confidence Interval (CI): 0.55–1.02; p<0.05], total adenine nucleotides concentration in the metabolic pool of platelets (OR:0.99; CI: 0.62–1.57; p<0.01) and cyclic adenosine-mono-phosphate (OR:0.81; CI: 0.57, 1.14; p<0.05) and cyclic guanosine mono-phosphate (OR:.78; CI: 0.55–1.09; p<0.05) levels in platelets were decreased in comparison with the control group, while adenylate energy charge in the metabolic pool of platelets (OR: >100.00; CI: 0.00->100.00; p<0.05) and secretion of adenosine triphosphate (OR:.13; CI: 0.00–14.26; p<0.05) and adenosine diphosphate (OR:.77; CI: 0.08–36.79; p<0.05) were increased. The results of our study show increased activation and aggregation of platelets in pregnant females with preeclampsia.

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43

Chen, Da-Chung, Shyng-Shiou F. Yuan, Her-Young Su, Shin-Chieh Lo, Shin-Sia Ren y Gwo-Jang Wu. "Urinary cyclic guanosine 3′,5′-monophosphate and cyclic adenosine 3′,5′-monophosphate changes in spontaneous and induced onset active labor". Acta Obstetricia et Gynecologica Scandinavica 84, n.º 11 (17 de octubre de 2005): 1081–86. http://dx.doi.org/10.1111/j.0001-6349.2005.00831.x.

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44

Horton, J. K., R. C. Martin, S. Kalinka, A. Cushing, J. P. Kitcher, M. J. O'Sullivan y P. M. Baxendale. "Enzyme immunoassays for the estimation of adenosine 3',5'cyclic monophosphate and guanosine 3',5'cyclic monophosphate in biological fluids". Journal of Pharmacological and Toxicological Methods 29, n.º 4 (agosto de 1993): 234. http://dx.doi.org/10.1016/1056-8719(93)90032-a.

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45

Horton, J. K., R. C. Martin, S. Kalinka, A. Cushing, J. P. Kitcher, M. J. O'Sullivan y P. M. Baxendale. "Enzyme immunoassays for the estimation of adenosine 3′,5′ cyclic monophosphate and guanosine 3′,5′ cyclic monophosphate in biological fluids". Journal of Immunological Methods 155, n.º 1 (octubre de 1992): 31–40. http://dx.doi.org/10.1016/0022-1759(92)90268-x.

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46

Münzel, Thomas, Robert Feil, Alexander Mülsch, Suzanne M. Lohmann, Franz Hofmann y Ulrich Walter. "Physiology and Pathophysiology of Vascular Signaling Controlled by Cyclic Guanosine 3′,5′-Cyclic Monophosphate–Dependent Protein Kinase". Circulation 108, n.º 18 (4 de noviembre de 2003): 2172–83. http://dx.doi.org/10.1161/01.cir.0000094403.78467.c3.

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47

Devlin, A. M. y B. J. Leckie. "Second messengers involved in the control of renin secretion in cultured human nephroblastoma cells". American Journal of Physiology-Renal Physiology 266, n.º 4 (1 de abril de 1994): F667—F673. http://dx.doi.org/10.1152/ajprenal.1994.266.4.f667.

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We aimed to study the intracellular signaling mechanisms involved in the stimulation and suppression of renin secretion from human nephroblastoma cells. Isoproterenol and forskolin increased intracellular adenosine 3',5'-cyclic monophosphate (cAMP) concentration and stimulated renin secretion as did the addition of dibutyryl-cAMP. Atrial natriuretic peptide (ANP) suppressed basal renin secretion and increased the concentration of extracellular guanosine 3',5'-cyclic monophosphate (cGMP). When ANP was added in the presence of isoproterenol or forskolin, the increase in cGMP was reduced. ANP attenuated the cAMP response to isoproterenol but not forskolin. Nephroblastoma cell membranes contained the guanosine-binding proteins Gs and Gi2, and the isoforms were similar to those in vascular smooth muscle. A functional role for Gi was indicated because the ANP-induced suppression of basal renin secretion was blocked by pertussis toxin. We conclude that cAMP stimulates and cGMP suppresses basal renin secretion, but neither fully accounts for the suppression of stimulated renin secretion by ANP.

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48

Lee, S. L., W. W. Wang y B. L. Fanburg. "Nitroprusside inhibits serotonin-induced mitogenesis and tyrosine phosphorylation of smooth muscle cells". American Journal of Physiology-Lung Cellular and Molecular Physiology 270, n.º 3 (1 de marzo de 1996): L362—L367. http://dx.doi.org/10.1152/ajplung.1996.270.3.l362.

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Serotonin (5-hydroxytryptamine, 5-HT) produces hyperplasia and hypertrophy of bovine pulmonary artery smooth muscle cells (SMC) in culture. The growth responses are associated with early elevations of c-myc and actin gene expressions and are blocked by agents that elevate cellular adenosine 3',5'-cyclic monophosphate or inhibit 5-HT transport or tyrosine phosphorylation. A rapid enhancement of tyrosine phosphorylation of a 120-kDa protein (p120) is associated with the 5-HT-induced mitogenesis. In the present studies, sodium nitroprusside (SNP, 10-100 micromol/l), a NO-generating agent, dose dependently inhibited 5-HT-induced thymidine incorporation by SMC. Inhibition of the 5-HT stimulatory effect was also observed with isosorbide dinitrate and nitroglutathione, which are also NO donors. Incubation of cells with 8-bromoguanosine 3',5'-cyclic monophosphate (1 micromol/l) mimicked the antimitogenic action of SNP. The antiproliferative effect of SNP was inhibited by hemoglobin (50 micromol/l) and potentiated by superoxide dismutase (200 U/ml), supporting the role of NO in the process. Enhancement of tyrosine phosphorylation of p120 by 5-HT was prevented by preincubation with SNP or exogenously added guanosine 3',5'-cyclic monophosphate. The data indicate that 5-HT acts as a mitogen for SMC through a signal transduction pathway involving tyrosine phosphorylation. SNP likely prevents the 5-HT-induced mitogenesis of SMC through elevation of intracellular guanosine 3',5'-cyclic monophosphate and inhibition of tyrosine phosphorylation of p120.

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49

Itoh, H., N. Sagawa, M. Hasegawa, T. Mori, S. Suga, M. Mukoyama, T. Yoshimasa, H. Itoh y K. Nakao. "Umbilical venous guanosine 3',5'-cyclic phosphate (cGMP) concentration increases in asphyxiated newborns". Reproduction, Fertility and Development 7, n.º 6 (1995): 1515. http://dx.doi.org/10.1071/rd9951515.

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Guanosine 3',5'-cyclic phosphate (cGMP) is known to be the second messenger of natriuretic peptides and nitric oxide (NO). To investigate the involvement of natriuretic peptides in the regulation of the feto-placental circulation, specific radioimmunoassays were used to measure the concentrations of atrial natriuretic peptide (ANP), brain natriuretic peptide (BNP) and cGMP in the umbilical venous plasma of normal and asphyxiated newborns. The plasma concentrations of ANP, BNP and cGMP in asphyxiated newborns were 48.3 +/- 12.9 pm, 24.5 +/- 9.4 pm and 4.4 +/- 1.6 nM (mean +/- s.e.m., n = 10), respectively. These values were significantly higher than those in the normal newborns (17.4 +/- 1.9 pm, 4.7 +/- 1.0 pm, and 0.78 +/- 0.14 nM, respectively). Moreover, the expression of both ANP-A and ANP-B receptor, biologically active receptors for natriuretic peptides, was detected in term human placenta by Northern bolt analysis. The expression of natriuretic peptide receptors was further confirmed by binding assay using [125I]-labelled ANP and solubilized crude membrane preparations of placental tissue. These findings suggest that cGMP is produced in the placenta, at least partly, by the action of ANP and BNP secreted from fetal heart, in pathophysiological conditions such as fetal hypoxia.

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50

Ho, A. K., K. Hashimoto y C. L. Chik. "3′,5′-Cyclic Guanosine Monophosphate Activates Mitogen-Activated Protein Kinase in Rat Pinealocytes". Journal of Neurochemistry 73, n.º 2 (18 de enero de 2002): 598–604. http://dx.doi.org/10.1046/j.1471-4159.1999.0730598.x.

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