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Journal articles on the topic 'CAMP/cGMP'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Jiang, Hang, John B. Shabb, and Jackie D. Corbin. "Cross-activation: overriding cAMP/cGMP selectivities of protein kinases in tissues." Biochemistry and Cell Biology 70, no. 12 (1992): 1283–89. http://dx.doi.org/10.1139/o92-175.

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cAMP- and cGMP-dependent protein kinases are homologous proteins and are predicted to exhibit very similar three-dimensional structures. Their cyclic nucleotide binding domains share a high degree of amino acid sequence identity. cAMP- and cGMP-dependent protein kinases are activated relatively specifically by cAMP and cGMP, respectively; and a single alanine–threonine difference between cAMP- and cGMP-binding domains partially accounts for this specificity. Thus, it would be expected that cAMP and cGMP mediate separate physiological effects. However, owing in part to the lack of absolute spec

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2

Inamura, Kouhei, Makoto Kashiwayanagi, and Kenzo Kurihara. "Effects of cGMP and sodium nitroprusside on odor responses in turtle olfactory sensory neurons." American Journal of Physiology-Cell Physiology 275, no. 5 (1998): C1201—C1206. http://dx.doi.org/10.1152/ajpcell.1998.275.5.c1201.

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The effects of cGMP and sodium nitroprusside (SNP) on odor responses in isolated turtle olfactory neurons were examined. The inward current induced by dialysis of a mixture of 1 mM cAMP and 1 mM cGMP was similar to that induced by dialysis of 1 mM cAMP or 1 mM cGMP alone. After the neurons were desensitized by the application of 1 mM cGMP, 3 mM 8-(4-chlorophenylthio)-cAMP, a membrane-permeable cAMP analog, did not elicit any current, indicating that both cAMP and cGMP activated the same channel. Extracellular application of SNP, a nitric oxide (NO) donor, evoked inward currents in a dose-depen

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3

Xu, Hao-Liang, Hailemariam M. Wolde, Vitaliy Gavrilyuk, Verna L. Baughman, and Dale A. Pelligrino. "cAMP modulates cGMP-mediated cerebral arteriolar relaxation in vivo." American Journal of Physiology-Heart and Circulatory Physiology 287, no. 6 (2004): H2501—H2509. http://dx.doi.org/10.1152/ajpheart.00319.2004.

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No studies have specifically addressed whether cAMP can influence nitric oxide (NO)/cGMP-induced cerebral vasodilation. In this study, we examined whether cAMP can enhance or reduce NO-induced cerebral vasodilation in vivo via interfering with cGMP efflux or through potentiating phosphodiesterase 5 (PDE5)-mediated cGMP breakdown, respectively, in cerebral vascular smooth muscle cells (CVSMCs). To that end, we evaluated, in male rats, the effects of knockdown [via antisense oligodeoxynucleotide (ODN) applications] of the cGMP efflux protein multidrug resistance protein 5 (MRP5) and PDE5 inhibit

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4

Hasegawa, K., H. Kikuchi, S. Ishizaki, et al. "Simple fluctuation of Ca2+ elicits the complex circadian dynamics of cyclic AMP and cyclic GMP in Paramecium." Journal of Cell Science 112, no. 2 (1999): 201–7. http://dx.doi.org/10.1242/jcs.112.2.201.

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The circadian dynamics of cyclic adenosine 3′,5′-monophosphate (cAMP) and cyclic guanosine 3′,5′-monophosphate (cGMP) were simulated in Paramecium multimicronucleatum. The mathematical functions determined closely mimic the Ca2+ dependence of adenylate cyclase (AC) and guanylate cyclase (GC) activities as documented in P. tetraurelia. Patterns of cAMP concentration ([cAMP]), cGMP concentration ([cGMP]), and the ratio [cGMP]/[cAMP] were calculated with respect to Ca2+ concentrations ([Ca2+]) fluctuating sinusoidally with a period of 24 hours at three different levels: low, medium, and high. The

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5

Stangherlin, Alessandra, and Manuela Zaccolo. "cGMP–cAMP interplay in cardiac myocytes: a local affair with far-reaching consequences for heart function." Biochemical Society Transactions 40, no. 1 (2012): 11–14. http://dx.doi.org/10.1042/bst20110655.

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cAMP and cGMP signalling pathways are common targets in the pharmacological treatment of heart failure, and often drugs that modulate the level of these second messengers are simultaneously administered to patients. cGMP can potentially affect cAMP levels by modulating the activity of PDEs (phosphodiesterases), the enzymes that degrade cyclic nucleotides. This biochemical cross-talk provides the means for drugs that increase cGMP to concomitantly affect cAMP signals. Recent studies using FRET (fluorescence resonance energy transfer) reporters and real-time imaging show that, in cardiac myocyte

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6

DICKINSON, Natalie T., Elliott K. JANG, and Richard J. HASLAM. "Activation of cGMP-stimulated phosphodiesterase by nitroprusside limits cAMP accumulation in human platelets: effects on platelet aggregation." Biochemical Journal 323, no. 2 (1997): 371–77. http://dx.doi.org/10.1042/bj3230371.

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cGMP enhances cAMP accumulation in platelets via cGMP-inhibited phosphodiesterase (PDE3) [Maurice and Haslam (1990) Mol. Pharmacol. 37, 671–681]. However, cGMP might also limit cAMP accumulation by activating cGMP-stimulated phosphodiesterase (PDE2). We therefore evaluated the role of PDE2 in human platelets by using erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) to inhibit this enzyme selectively. IC50 values for the inhibition of platelet PDE2 by EHNA, with 10 μM cAMP as substrate in the absence and in the presence of 1 μM cGMP, were 15 and 3 μM respectively. Changes in platelet cyclic [3H]nucl

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7

Dembinsky, A., H. Rubin, and S. Ravid. "Chemoattractant-mediated increases in cGMP induce changes in Dictyostelium myosin II heavy chain-specific protein kinase C activities." Journal of Cell Biology 134, no. 4 (1996): 911–21. http://dx.doi.org/10.1083/jcb.134.4.911.

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Myosin II heavy chain (MHC)-specific protein kinase C (MHC-PKC) isolated from the ameba, Dictyostelium discoideum, regulates myosin II assembly and localization in response to the chemoattractant cAMP (Abu-Elneel et al. 1996. J. Biol. Chem. 271:977- 984). Recent studies have indicated that cAMP-induced cGMP accumulation plays a role in the regulation of myosin II phosphorylation and localization (Liu, G., and P. Newell. 1991. J. Cell. Sci. 98: 483-490). This report describes the roles of cAMP and cGMP in the regulation of MHC-PKC membrane association, phosphorylation, and activity (hereafter t

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8

Krizhanovsky, Valery, Orly Agamy, and Michael Naim. "Sucrose-stimulated subsecond transient increase in cGMP level in rat intact circumvallate taste bud cells." American Journal of Physiology-Cell Physiology 279, no. 1 (2000): C120—C125. http://dx.doi.org/10.1152/ajpcell.2000.279.1.c120.

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Initial sweet taste transduction is expected to occur in the subsecond time range. We demonstrate a rapid and transient (75–250 ms) increase of cGMP (but not cAMP) level in rat intact circumvallate taste cells after stimulation by sucrose. This rapid increase does not occur in nonsensory epithelial cells. Pretreatment with a nonspecific phosphodiesterase (PDE) inhibitor (IBMX), a specific cAMP-PDE4 inhibitor (denbufylline), or an adenylyl cyclase activator (forskolin) all increased basal cAMP and abolished the sucrose-stimulated cGMP increase at 150 ms. Pretreatment with a soluble guanylyl cyc

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9

Segal, J. "Opposite regulatory effects of cAMP and cGMP on sugar uptake in rat thymocytes." American Journal of Physiology-Endocrinology and Metabolism 252, no. 5 (1987): E588—E594. http://dx.doi.org/10.1152/ajpendo.1987.252.5.e588.

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The present study provides several lines of evidence which indicate that in the rat thymocyte adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5-cyclic monophosphate (cGMP) induce opposing regulatory effects on 2-deoxyglucose (2-DG) uptake; cAMP is stimulatory, whereas cGMP is inhibitory. First, the cyclic nucleotide analogues dibutyryl cAMP (dBcAMP) and dibutyryl cGMP (dBcGMP) produced a dose-related increase and decrease in thymocyte 2-DG uptake, respectively. Second, 3,5,3'-triiodo-L-thyronine (T3) and epinephrine, which increased cellular cAMP concentration but had no effect on

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10

Stricker, Stephen A. "Inhibition of germinal vesicle breakdown by antioxidants and the roles of signaling pathways related to nitric oxide and cGMP during meiotic resumption in oocytes of a marine worm." REPRODUCTION 143, no. 3 (2012): 261–70. http://dx.doi.org/10.1530/rep-11-0358.

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In mammalian oocytes, cAMP elevations prevent the resumption of meiotic maturation and thereby block nuclear disassembly (germinal vesicle breakdown (GVBD)), whereas nitric oxide (NO) and its downstream mediator cGMP can either inhibit or induce GVBD. Alternatively, some invertebrate oocytes use cAMP to stimulate, rather than inhibit, GVBD, and in such cases, the effects of NO/cGMP signaling on GVBD remain unknown. Moreover, potential interactions between NO/cGMP and AMP-activated kinase (AMPK) have not been assessed during GVBD. Thus, this study analyzed intraoocytic signaling pathways relate

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11

Frajnt, Magdalena, Małgorzata Cytryńska, and Teresa Jakubowicz. "The effect of cAMP and cGMP on the activity and substrate specificity of protein kinase A from methylotrophic yeast Pichia pastoris." Acta Biochimica Polonica 50, no. 4 (2003): 1111–18. http://dx.doi.org/10.18388/abp.2003_3635.

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Cyclic AMP dependent protein kinase (PKA) from Pichia pastoris yeast cells was found to be activated by either cAMP or cGMP. Analogs of cAMP such as 8-chloro-cAMP and 8-bromo-cAMP were as potent as cAMP in PKA activation while N6,2'-O-dibutyryl-cAMP did not stimulate the enzyme activity. It was shown that protamine sulfate was almost equally phosphorylated in the presence of 1-2 x 10(-6)M cAMP or cGMP while other substrates such as Kemptide, ribosomal protein S6, were phosphorylated to a lower extent in the presence of cGMP. It was demonstrated that pyruvate kinase is a substrate of PKA which

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12

Golin-Bisello, Franca, Neil Bradbury, and Nadia Ameen. "STa and cGMP stimulate CFTR translocation to the surface of villus enterocytes in rat jejunum and is regulated by protein kinase G." American Journal of Physiology-Cell Physiology 289, no. 3 (2005): C708—C716. http://dx.doi.org/10.1152/ajpcell.00544.2004.

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The cystic fibrosis transmembrane conductance regulator (CFTR) is critical to cAMP- and cGMP-activated intestinal anion secretion and the pathogenesis of secretory diarrhea. Enterotoxins released by Vibrio cholerae (cholera toxin) and Escherichia coli (heat stable enterotoxin, or STa) activate intracellular cAMP and cGMP and signal CFTR on the apical plasma membrane of small intestinal enterocytes to elicit chloride and fluid secretion. cAMP activates PKA, whereas cGMP signals a cGMP-dependent protein kinase (cGKII) to phosphorylate CFTR in the intestine. In the jejunum, cAMP also regulates CF

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13

Cytrynska, Malgorzata, Iwona Wojda, Magdalena Frajnt, and Teresa Jakubowicz. "PKA from Saccharomyces cerevisiae can be activated by cyclic AMP and cyclic GMP." Canadian Journal of Microbiology 45, no. 1 (1999): 31–37. http://dx.doi.org/10.1139/w98-214.

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Analysis of Saccharomyces cerevisiae genome revealed no sequence homologous to cyclic GMP (cGMP) dependent protein kinase from other organisms. Here we demonstrate that cyclic AMP (cAMP) dependent protein kinase purified from S. cerevisiae was almost equally activated by cAMP and cGMP at 3 × 10-6 M concentrations of either nucleotide in the presence of Mg2+ ions. Interestingly, if Mn2+ ions were used instead of Mg2+, cGMP was only 30% as effective as cAMP in the activation of cAMP-dependent protein kinase. Analogs of cAMP such as 8-chloro-cAMP and 3':5'-cyclic monophosphate of ribofuranosylben

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14

Sheth, S. B., and R. W. Colman. "Platelet cAMP and cGMP Phosphodiesterases." Platelets 6, no. 2 (1995): 61–70. http://dx.doi.org/10.3109/09537109509078445.

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15

Henkin, R. I., and I. Velicu. "cAMP and cGMP in nasal mucus: relationships to taste and smell dysfunction, gender and age." Clinical & Investigative Medicine 31, no. 2 (2008): 71. http://dx.doi.org/10.25011/cim.v31i2.3366.

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Purpose: To evaluate the presence and concentration of cAMP and cGMP in human nasal mucus in normal volunteers, to relate these findings to age and gender, and to compare normal levels with those in patients with taste and smell dysfunction. Methods: Nasal mucus was collected over one to four days in 66 normal subjects and 203 patients with smell loss (hyposmia). Samples were centrifuged at 20,000 rpm, the supernatant removed and analyzed for cAMP and cGMP by using a 96 plate technique with a specific spectrophotometric colorimetric ELISA assay. Results: Both cAMP and cGMP were present in huma

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16

Bosgraaf, Leonard, Henk Russcher, Helena Snippe, Sonya Bader, Joyce Wind, and Peter J. M. Van Haastert. "Identification and Characterization of Two Unusual cGMP-stimulated Phoshodiesterases in Dictyostelium." Molecular Biology of the Cell 13, no. 11 (2002): 3878–89. http://dx.doi.org/10.1091/mbc.e02-05-0302.

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Recently, we recognized two genes, gbpA andgbpB, encoding putative cGMP-binding proteins with a Zn2+-hydrolase domain and two cyclic nucleotide binding domains. The Zn2+-hydrolase domains belong to the superfamily of β-lactamases, also harboring a small family of class II phosphodiesterases from bacteria and lower eukaryotes. Gene inactivation and overexpression studies demonstrate thatgbpA encodes the cGMP-stimulated cGMP-phosphodiesterase that was characterized biochemically previously and was shown to be involved in chemotaxis. cAMP neither activates nor is a substrate of GbpA. The gbpB gen

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17

Weiss, Harvey R., Gary X. Gong, Michaela Straznicka, Lin Yan, James Tse, and Peter M. Scholz. "Cyclic GMP and cyclic AMP induced changes in control and hypertrophic cardiac myocyte function interact through cyclic GMP affected cyclic-AMP phosphodiesterases." Canadian Journal of Physiology and Pharmacology 77, no. 6 (1999): 422–31. http://dx.doi.org/10.1139/y99-039.

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We tested the hypothesis that the negative functional effects of cyclic GMP (cGMP) would be greater after increasing cyclic AMP (cAMP), because of the action of cGMP-affected cAMP phosphodiesterases in cardiac myocytes and that this effect would be altered in left ventricular hypertrophy (LVH) produced by aortic valve plication. Myocyte shortening data were collected using a video edge detector, and O2 consumption was measured by O2 electrodes during stimulation (5 ms, 1 Hz, in 2 mM Ca2+) from control (n = 7) and LVH (n = 7) dog ventricular myocytes. cAMP and cGMP were determined by a competit

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18

Jackson, Edwin K., Zaichuan Mi, Keri Janesko-Feldman, Travis C. Jackson, and 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, no. 6 (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), hydrol

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19

Bkaily, G., and N. Sperelakis. "Injection of guanosine 5'-cyclic monophosphate into heart cells blocks calcium slow channels." American Journal of Physiology-Heart and Circulatory Physiology 248, no. 5 (1985): H745—H749. http://dx.doi.org/10.1152/ajpheart.1985.248.5.h745.

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The role of guanosine 5'-cyclic monophosphate (cGMP) in the regulation of the ionic slow channels in heart muscle is less well known than that of adenosine 3,'5'-cyclic monophosphate (cAMP). The effects of intracellular injection of cAMP and cGMP in cultured chick embryonic heart (ventricular) cells by the liposome method were studied. Injection of cAMP into the cells induced spontaneous slow action potentials that could be blocked by verapamil and nifedipine. Injection of cGMP blocked on-going slow action potentials, and this effect was reversed by increasing cAMP. Thus both cAMP and cGMP are

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20

MacKENZIE, Christopher J., Jill M. WAKEFIELD, Fiona CAIRNS, Anna F. DOMINICZAK, and Gwyn W. GOULD. "Regulation of glucose transport in aortic smooth muscle cells by cAMP and cGMP." Biochemical Journal 353, no. 3 (2001): 513–19. http://dx.doi.org/10.1042/bj3530513.

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We have studied the ability of cGMP and cAMP to modulate platelet-derived growth factor (PDGF)-stimulated 2-deoxy-d-glucose (deGlc) transport in primary cultures of vascular smooth muscle cells (VMSC) from rat aorta. PDGF stimulated deGlc transport in a time- and concentration-dependent manner. 8-Bromo-cGMP and atrial natriuretic peptide(1–28) [ANP(1–28)] were found to reduce PDGF-stimulated deGlc transport without affecting basal (unstimulated) transport activity. In contrast, 8-bromo-cAMP and dibutyryl-cAMP stimulated basal deGlc transport 2-fold and were without effect on PDGF-stimulated de

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Assender, J. W., K. M. Southgate, M. B. Hallett, and A. C. Newby. "Inhibition of proliferation, but not of Ca2+ mobilization, by cyclic AMP and GMP in rabbit aortic smooth-muscle cells." Biochemical Journal 288, no. 2 (1992): 527–32. http://dx.doi.org/10.1042/bj2880527.

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The effects on cellular proliferation and Ca2+ mobilization of analogues of cyclic AMP (cAMP) and cyclic GMP (cGMP) and of agents that elevate the intracellular concentrations of cyclic nucleotides were compared in closely similar preparations of first-passage rabbit aortic vascular smooth-muscle cells. Proliferation induced by foetal-bovine serum was inhibited by 78% by 1 mM-8-bromo cAMP and by 42% by 1 mM-8-bromo cGMP. In the presence of 100 microM-isobutylmethylxanthine, 100 microM-forskolin increased intracellular cAMP concentration 5-fold and inhibited proliferation by 87%, but did not af

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22

Cornwell, T. L., E. Arnold, N. J. Boerth, and T. M. Lincoln. "Inhibition of smooth muscle cell growth by nitric oxide and activation of cAMP-dependent protein kinase by cGMP." American Journal of Physiology-Cell Physiology 267, no. 5 (1994): C1405—C1413. http://dx.doi.org/10.1152/ajpcell.1994.267.5.c1405.

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Recent studies indicate that nitric oxide (NO) and guanosine 3',5'-cyclic monophosphate (cGMP) may inhibit the proliferation of vascular smooth muscle cells (SMC) in vitro. The purpose of this study was to investigate the mechanism of NO- and cGMP-dependent inhibition of cultured rat aortic SMC. The cytokine interleukin-1 beta (IL-1 beta) inhibited serum- and platelet-derived growth factor-stimulated [3H]thymidine incorporation into DNA in subcultured rat aortic SMC. Incubation with IL-1 beta for 24 h markedly increased cGMP levels but not adenosine 3',5'-cyclic monophosphate (cAMP) levels. Ho

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23

Chakder, S., and S. Rattan. "Involvement of cAMP and cGMP in relaxation of internal anal sphincter by neural stimulation, VIP, and NO." American Journal of Physiology-Gastrointestinal and Liver Physiology 264, no. 4 (1993): G702—G707. http://dx.doi.org/10.1152/ajpgi.1993.264.4.g702.

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We examined simultaneous changes in resting tension and tissue levels of the two second messengers, adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP), in the opossum internal anal sphincter (IAS). The influence of the nonadrenergic noncholinergic (NANC) nerve stimulation (NS) by electrical field stimulation (EFS) and the putative neurotransmitters nitric oxide (NO) and vasoactive intestinal peptide (VIP) on the above modalities was investigated. The fall in resting IAS tension in response to NS, NO, and VIP was accompanied by significant rises in both

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Sadek, Mirna S., Eleder Cachorro, Ali El-Armouche, and Susanne Kämmerer. "Therapeutic Implications for PDE2 and cGMP/cAMP Mediated Crosstalk in Cardiovascular Diseases." International Journal of Molecular Sciences 21, no. 20 (2020): 7462. http://dx.doi.org/10.3390/ijms21207462.

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Phosphodiesterases (PDEs) are the principal superfamily of enzymes responsible for degrading the secondary messengers 3′,5′-cyclic nucleotides cAMP and cGMP. Their refined subcellular localization and substrate specificity contribute to finely regulate cAMP/cGMP gradients in various cellular microdomains. Redistribution of multiple signal compartmentalization components is often perceived under pathological conditions. Thereby PDEs have long been pursued as therapeutic targets in diverse disease conditions including neurological, metabolic, cancer and autoimmune disorders in addition to numero

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Tian, Yuehui, Shang Yang, and Shiqiang Gao. "Advances, Perspectives and Potential Engineering Strategies of Light-Gated Phosphodiesterases for Optogenetic Applications." International Journal of Molecular Sciences 21, no. 20 (2020): 7544. http://dx.doi.org/10.3390/ijms21207544.

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The second messengers, cyclic adenosine 3′-5′-monophosphate (cAMP) and cyclic guanosine 3′-5′-monophosphate (cGMP), play important roles in many animal cells by regulating intracellular signaling pathways and modulating cell physiology. Environmental cues like temperature, light, and chemical compounds can stimulate cell surface receptors and trigger the generation of second messengers and the following regulations. The spread of cAMP and cGMP is further shaped by cyclic nucleotide phosphodiesterases (PDEs) for orchestration of intracellular microdomain signaling. However, localized intracellu

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26

Parfenova, H., M. Shibata, S. Zuckerman, R. Mirro, and C. W. Leffler. "Cyclic nucleotides and cerebrovascular tone in newborn pigs." American Journal of Physiology-Heart and Circulatory Physiology 265, no. 6 (1993): H1972—H1982. http://dx.doi.org/10.1152/ajpheart.1993.265.6.h1972.

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Relationships between cyclic nucleotides and cerebrovascular tone were investigated using closed cranial windows in anesthetized newborn pigs. Pial arteriolar diameter was monitored and cerebrospinal fluid (CSF) was collected from beneath the cranial window. Adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP) concentrations in CSF were 1,690 +/- 200 and 730 +/- 40 fmol/ml, respectively. Topically applied isozyme-selective and nonselective inhibitors [3-isobutyl-1-methylxanthine (IBMX), theophylline, Ro 201724, dipyridamole, zaprinast, calmidazolium, and

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Kokate, T. G., J. A. Heiny, and N. Sperelakis. "Stimulation of the slow calcium current in bullfrog skeletal muscle fibers by cAMP and cGMP." American Journal of Physiology-Cell Physiology 265, no. 1 (1993): C47—C53. http://dx.doi.org/10.1152/ajpcell.1993.265.1.c47.

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The effects of adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP) on slow calcium currents (ICa) were investigated using the Vaseline-gap voltage-clamp technique in bullfrog skeletal muscle cut fibers. Both cAMP and cGMP induced a pronounced increase in the amplitude of ICa when applied to the cut ends of fibers. Both cyclic nucleotides also decreased time to peak current at all membrane potentials. The current-voltage relationship was shifted toward more negative potentials by cAMP as well as cGMP. The potentiating effects of cAMP and cGMP on ICa were

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El-Daher, Samer S., Martin Eigenthaler, Ulrich Walter, et al. "Distribution and Activation of cAMP- and cGMP-Dependent Protein Kinases in Highly Purified Human Platelet Plasma and Intracellular Membranes." Thrombosis and Haemostasis 76, no. 06 (1996): 1063–71. http://dx.doi.org/10.1055/s-0038-1650707.

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SummaryPreviously cAMP- and cGMP-dependent protein kinases (cAMP-PK, cGMP-PK) have been found predominantly associated with the particulate fraction in human platelets. We now report the distribution and activation of cAMP-PK and cGMP-PK in highly purified fractions of human platelet plasma (PM) and intracellular membranes (IM) prepared using high voltage free flow electrophoresis. Two non-hydrolys-able analogues of cAMP and cGMP namely Sp-5,6-DCl-cBiMPS and 8-p-CPT-cGMP have been used to activate cAMP-PK and cGMP-PK respectively. Addition of either agonist with [γ32P]ATP stimulated the endoge

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Gupta, Mahesh P., Michael D. Ober, Carolyn Patterson, Mohammed Al-Hassani, Viswanathan Natarajan, and C. Michael Hart. "Nitric oxide attenuates H2O2-induced endothelial barrier dysfunction: mechanisms of protection." American Journal of Physiology-Lung Cellular and Molecular Physiology 280, no. 1 (2001): L116—L126. http://dx.doi.org/10.1152/ajplung.2001.280.1.l116.

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Nitric oxide (·NO) attenuates hydrogen peroxide (H2O2)-mediated injury in porcine pulmonary artery endothelial cells (PAECs) and modulates intracellular levels of cGMP and cAMP. We hypothesized that ·NO attenuates H2O2-induced PAEC monolayer barrier dysfunction through cyclic nucleotide-dependent signaling mechanisms. To examine this hypothesis, cultured PAEC monolayers were treated with H2O2, and barrier function was measured as transmonolayer albumin clearance. H2O2caused significant PAEC barrier dysfunction that was attenuated by intracellular as well as extracellular ·NO generation. ·NO in

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Wyatt, Todd A., Mary A. Forgèt, Jennifer M. Adams, and Joseph H. Sisson. "Both cAMP and cGMP are required for maximal ciliary beat stimulation in a cell-free model of bovine ciliary axonemes." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 3 (2005): L546—L551. http://dx.doi.org/10.1152/ajplung.00107.2004.

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Previously, we have shown that the ATPase-dependent motion of cilia in bovine bronchial epithelial cells (BBEC) can be regulated through the cyclic nucleotides, cAMP via the cAMP-dependent protein kinase (PKA) and cGMP via the cGMP-dependent protein kinase (PKG). Both cyclic nucleotides cause an increase in cilia beat frequency (CBF). We hypothesized that cAMP and cGMP may act directly at the level of the ciliary axoneme in BBEC. To examine this, we employed a novel cell-free system utilizing detergent-extracted axonemes. Axoneme movement was whole-field analyzed digitally with the Sisson-Ammo

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Tang, K. M., J. L. Sherwood, and R. J. Haslam. "Photoaffinity labelling of cyclic GMP-binding proteins in human platelets." Biochemical Journal 294, no. 2 (1993): 329–33. http://dx.doi.org/10.1042/bj2940329.

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The photoaffinity labelling of platelet cyclic GMP (cGMP)-binding proteins by [32P]cGMP was studied; at least five labelled proteins (110, 80, 55, 49 and 38 kDa) were detected in platelet cytosol and four (80, 65, 49 and 38 kDa) in platelet membranes. The 110 kDa species was identified as cGMP-inhibited cyclic AMP (cAMP) phosphodiesterase (PDE III) by immunoprecipitation and by the inhibition of photolabelling by specific inhibitors of this enzyme. Similarly, the 80 kDa species was identified as cGMP-dependent protein kinase by immunoprecipitation and by the effects of cGMP analogues on photol

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Yamaki, M., S. McIntyre, M. E. Rassier, J. H. Schwartz, and T. P. Dousa. "Cyclic 3',5'-nucleotide diesterases in dynamics of cAMP and cGMP in rat collecting duct cells." American Journal of Physiology-Renal Physiology 262, no. 6 (1992): F957—F964. http://dx.doi.org/10.1152/ajprenal.1992.262.6.f957.

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We studied cyclic 3',5'-nucleotide phosphodiesterase (PDE) isozymes and their role in adenosine 3',5'-cyclic monophosphate (cAMP) and cGMP metabolism in a rat inner medullary collecting duct (IMCD) cell line. The homogenized and fractionated IMCD cells of cAMP-PDE and all of cGMP-PDE activity were found in the cytosol. The majority of cytosolic cAMP-PDE (greater than 50%) was isozyme PDE-IV; the Ca(2+)-calmodulin-sensitive PDE-I was present only in cytosol. Preincubation of IMCD cells with PDE-IV inhibitor rolipram markedly (5x) enhanced levels of cAMP both basal and in the presence of [Arg8]v

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Zhang, Qihang, Michael Lazar, Bruno Molino, et al. "Reduction in interaction between cGMP and cAMP in dog ventricular myocytes with hypertrophic failure." American Journal of Physiology-Heart and Circulatory Physiology 289, no. 3 (2005): H1251—H1257. http://dx.doi.org/10.1152/ajpheart.01234.2003.

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Baseline function and signal transduction are depressed in hearts with hypertrophic failure. We tested the hypothesis that the effects of cGMP and its interaction with cAMP would be reduced in cardiac myocytes from hypertrophic failing hearts. Ventricular myocytes were isolated from control dogs, dogs with aortic valve stenosis hypertrophy, and dogs with pacing hypertrophic failure. Myocyte function was measured using a video edge detector. Cell contraction data were obtained at baseline, with 8-bromo-cGMP (10−7, 10−6, and 10−5 M), with erythro-9-(2-hydroxy-3-nonyl)adenine [EHNA; a cAMP phosph

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Sirotkin, A. V. "Inter-relationships between nonapeptide hormones and cyclic nucleotides within cultured porcine granulosa cells." Journal of Endocrinology 150, no. 2 (1996): 343–48. http://dx.doi.org/10.1677/joe.0.1500343.

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Abstract The reciprocal control of nonapeptide hormone (oxytocin, vasopressin) and cyclic nucleotide (cAMP, cGMP) release by porcine granulosa cells was studied. In particular, the influence of vasopressin and oxytocin treatment (10–10 000 ng/ml) on basal and LH-induced cAMP and cGMP output, as well as the effects of dibutyryl cAMP (dbcAMP; cAMP analogue) and forskolin (a stimulator of cAMP formation; 0·1–1000 ng/ml) on vasopressin and oxytocin secretion by cultured porcine granulosa cells were examined. It was observed that the addition of arginine-8-vasopressin or oxytocin stimulated both cA

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Dhanakoti, Srinivas N., Yuansheng Gao, Minh Q. Nguyen, and J. Usha Raj. "Involvement of cGMP-dependent protein kinase in the relaxation of ovine pulmonary arteries to cGMP and cAMP." Journal of Applied Physiology 88, no. 5 (2000): 1637–42. http://dx.doi.org/10.1152/jappl.2000.88.5.1637.

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Agonist-induced smooth muscle relaxation occurs following an increase in intracellular concentrations of cGMP or cAMP. However, the role of protein kinase G (PKG) and/or protein kinase A (PKA) in cGMP- or cAMP-mediated pulmonary vasodilation is not clearly elucidated. In this study, we examined the relaxation responses of isolated pulmonary arteries of lambs (age = 10 ± 1 days), preconstricted with endothelin-1, to increasing concentrations of 8-bromo-cGMP (8-BrcGMP) or 8-BrcAMP (cell-permeable analogs), in the presence or absence of Rp-8-β-phenyl-1, N 2-etheno-bromoguanosine cyclic monosphord

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Kruuse, C., E. Frandsen, S. Schifter, LL Thomsen, S. Birk, and J. Olesen. "Plasma Levels of cAMP, cGMP and CGRP in Sildenafil-Induced Headache." Cephalalgia 24, no. 7 (2004): 547–53. http://dx.doi.org/10.1111/j.1468-2982.2003.00712.x.

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Sildenafil, a selective inhibitor of the cyclic guanosine monophosphate (cGMP) degrading phosphodiestrase 5 (PDE5), induced migraine without aura in 10 of 12 migraine patients and in healthy subjects it induced significantly more headache than placebo. The aim of the present study was to determine whether the pain-inducing effects of sildenafil would be reflected in plasma levels of important signalling molecules in migraine: cGMP, cyclic adenosine monophosphate (cAMP) and calcitonin gene-related peptide (CGRP). Ten healthy subjects (four women, six men) and 12 patients (12 women) suffering fr

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Steiner, Alexandre A., Maria J. A. Rocha, and Luiz G. S. Branco. "A neurochemical mechanism for hypoxia-induced anapyrexia." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 283, no. 6 (2002): R1412—R1422. http://dx.doi.org/10.1152/ajpregu.00328.2002.

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Hypoxia evokes a regulated decrease in body temperature, a response that has been termed anapyrexia, but the mechanisms involved are poorly understood. Therefore, the present study was undertaken to test the hypothesis that hypoxia-induced anapyrexia results from the activation of cAMP- and cGMP-dependent pathways in the preoptic region (PO). Adult male Wistar rats weighing 230–260 g were used. Body temperature was monitored by biotelemetry, and the levels of cAMP and cGMP were determined in the anteroventral third ventricular region (AV3V), where the PO is located. Using immunohistochemistry,

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Guimaraes, Danielle, Rafael Portella, Christelle Kamga-Pride, Jose Eduardo Tanus-Santos, and Sruti Shiva. "Nitrite Differently Activates cGMP versus cAMP." Free Radical Biology and Medicine 112 (November 2017): 164–65. http://dx.doi.org/10.1016/j.freeradbiomed.2017.10.255.

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Zaccolo, Manuela, and Matthew A. Movsesian. "cAMP and cGMP Signaling Cross-Talk." Circulation Research 100, no. 11 (2007): 1569–78. http://dx.doi.org/10.1161/circresaha.106.144501.

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Vettel, C., S. Lämmle, S. Ewens, et al. "PDE2-mediated cAMP hydrolysis accelerates cardiac fibroblast to myofibroblast conversion and is antagonized by exogenous activation of cGMP signaling pathways." American Journal of Physiology-Heart and Circulatory Physiology 306, no. 8 (2014): H1246—H1252. http://dx.doi.org/10.1152/ajpheart.00852.2013.

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Recent studies suggest that the signal molecules cAMP and cGMP have antifibrotic effects by negatively regulating pathways associated with fibroblast to myofibroblast (MyoCF) conversion. The phosphodiesterase 2 (PDE2) has the unique property to be stimulated by cGMP, which leads to a remarkable increase in cAMP hydrolysis and thus mediates a negative cross-talk between both pathways. PDE2 has been recently investigated in cardiomyocytes; here we specifically addressed its role in fibroblast conversion and cardiac fibrosis. PDE2 is abundantly expressed in both neonatal rat cardiac fibroblasts (

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Rodriguez, Roberto, Bruno Molino, Harvey R. Weiss, and Peter M. Scholz. "Negative metabolic and coronary flow effects of decreases in cAMP and increases in cGMP in control and renal hypertensive rabbit hearts." Journal of Applied Physiology 97, no. 1 (2004): 439–45. http://dx.doi.org/10.1152/japplphysiol.01115.2003.

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The interaction during stimulation of cGMP and inhibition of cAMP was investigated in control and renal hypertensive hearts. Control and hypertensive [1 kidney, 1 clip (1K1C)] rabbits were used. The anesthetized open-chest groups were vehicle, 8-bromo-cGMP (8-Br-cGMP; 10−3M), propranolol (Prop; 2 mg/kg), and Prop + 8-Br-cGMP. O2 consumption levels (V̇o2) in the subepicardium (Epi) and subendocardium (Endo) were determined from coronary flow (microspheres) and O2 extraction (microspectrophotometry). Wall thickening and cAMP levels were also determined. In control, no significant change in V̇o2

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Wang, Q., J. Bryowsky, R. D. Minshall, and D. A. Pelligrino. "Possible obligatory functions of cyclic nucleotides in hypercapnia-induced cerebral vasodilation in adult rats." American Journal of Physiology-Heart and Circulatory Physiology 276, no. 2 (1999): H480—H487. http://dx.doi.org/10.1152/ajpheart.1999.276.2.h480.

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Current evidence suggests that nitric oxide (NO) and vasodilating prostanoids, possibly via the actions of cGMP and cAMP, play permissive roles in hypercapnic cerebral vasodilation. The present study examined whether cGMP and cAMP have obligatory functions in hypercapnia. Using a closed cranial window in adult rats, we measured pial arteriolar diameters and periarachnoid cerebrospinal fluid (pCSF) cyclic nucleotide levels during normo- and hypercapnia and in the presence or absence of inhibitors of neuronal NO synthase (nNOS) or cyclooxygenase (COX). Also, we measured cGMP and cAMP contents in

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Magness, R. R., C. R. Rosenfeld, A. Hassan, and P. W. Shaul. "Endothelial vasodilator production by uterine and systemic arteries. I. Effects of ANG II on PGI2 and NO in pregnancy." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 6 (1996): H1914—H1923. http://dx.doi.org/10.1152/ajpheart.1996.270.6.h1914.

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Uterine vasculature is less responsive than systemic vasculature to angiotensin II (ANG II)-induced vasoconstriction. We hypothesized that pregnancy augments basal and ANG II-stimulated endothelial prostacyclin (PGI2) and/or nitric oxide (NO) production, which locally increase vascular smooth muscle (VSM) adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP), respectively. Uterine (UA) and systemic arteries (SA) from pregnant (P) and nonpregnant (NP) sheep were incubated with isobutylmethylxanthine. Basal PGI2, cAMP, and cGMP production was 2.4-, 1.6-, and

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Dickinson, Natalie, Elliott Jang, and Richard Haslam. "Cyclic Nucleotides and Phosphodiesterases in Platelets." Thrombosis and Haemostasis 82, no. 08 (1999): 412–23. http://dx.doi.org/10.1055/s-0037-1615861.

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IntroductionIt is now almost 30 years since the discovery that prostaglandin E1 (PGE1) inhibits platelet responses to aggregating agents, together with finding that the effects of this compound are mediated by adenosine 3′, 5′-cyclic monophosphate (cAMP) initiated interest in the physiological and pharmacological regulation of platelet function by other agents that increase platelet cAMP, as reviewed elsewhere.1 The most important agonists that stimulate cAMP formation in platelets have now been identified as prostacyclin (PGI2), prostaglandin D2 (PGD2), and adenosine, which exert their effect

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Rybalkin, Sergei, and Karin Bornfeldt. "Cyclic Nucleotide Phosphodiesterases and Human Arterial Smooth Muscle Cell Proliferation." Thrombosis and Haemostasis 82, no. 08 (1999): 424–34. http://dx.doi.org/10.1055/s-0037-1615862.

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IntroductionSmooth muscle cells (SMCs) in the arterial wall are normally found in a contractile, nonproliferative state. These SMCs are continuously exposed to agents that elevate cyclic AMP (cAMP) and cyclic GMP (cGMP), such as prostacyclin and nitric oxide (NO) released from the endothelium. Both cAMP and cGMP potently inhibit SMC proliferation by antagonizing major signaling pathways induced by growth factors, such as platelet-derived growth factor. Different forms of injury to the endothelium result in proliferation of the SMCs and can develop into atherosclerosis, restenosis, or arterial

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Abdollahi, Mohammad, Foreshteh Mashayekhi, Farzaneh Agha-hoseini, Ali Rezaie, Mohammad J. Zamani, and Reza Khorasani. "Alteration of Cyclic Nucleotides Levels and Oxidative Stress in Saliva of Human Subjects with Periodontitis." Journal of Contemporary Dental Practice 6, no. 4 (2005): 46–53. http://dx.doi.org/10.5005/jcdp-6-4-46.

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Abstract Experimental findings suggest a protective role for cyclic nucleotides against induction of oxidative stress in saliva. Oxidative stress is a major contributor to the pathogenesis of inflammatory diseases. This study was conducted to evaluate salivary oxidative stress along with cGMP and cAMP levels in periodontitis subjects. cAMP and cGMP are second messengers that have important roles in salivary gland functions. Unstimulated whole saliva samples were obtained from periodontitis patients and age- and sex-matched healthy individuals. Saliva samples were analyzed for thiobarbituric re

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Haynes, J., P. A. Kithas, A. E. Taylor, and S. J. Strada. "Selective inhibition of cGMP-inhibitable cAMP phosphodiesterase decreases pulmonary vasoreactivity." American Journal of Physiology-Heart and Circulatory Physiology 261, no. 2 (1991): H487—H492. http://dx.doi.org/10.1152/ajpheart.1991.261.2.h487.

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Guanosine 3',5'-cyclic monophosphate (cGMP) and adenosine 3',5'-cyclic monophosphate (cAMP) are mediators of smooth muscle relaxation. In this study, selective inhibitors of phosphodiesterase (PDE) isozymes were used to assess the role of cyclic nucleotide hydrolysis in angiotensin II (ANG II) and hypoxic pulmonary vasoconstriction. In isolated rat lungs, the hypoxic pressor response (HPR) was induced with a 95% N2-5% CO2 gas mixture. When administered during the plateau of the HPR, trequinsin (nonselective PDE inhibitor) and indolidan (cGMP-inhibitable cAMP PDE inhibitor) significantly (P = 0

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Delporte, C., P. Poloczek, and J. Winand. "Role of phosphodiesterase II in cross talk between cGMP and cAMP in human neuroblastoma NB-OK-1 cells." American Journal of Physiology-Cell Physiology 270, no. 1 (1996): C286—C292. http://dx.doi.org/10.1152/ajpcell.1996.270.1.c286.

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Cyclic nucleotides levels and cyclic nucleotide phosphodiesterase (PDE) activities were measured in human neuroblastoma NB-OK-1 cells possessing atrial natriuretic peptide (ANP) receptors of the A type and pituitary adenylate cyclase activating polypeptide (PACAP)-preferring receptors. Adenosine 3',5'-cyclic monophosphate (cAMP) and guanosine 3',5'-cyclic monophosphate (cGMP) degradation were interrelated since the increase in cGMP, induced by ANP-(99-126), stimulated the hydrolysis of cAMP by PDE isoenzyme II. In intact NB-OK-1 cells, the levels of cAMP and cGMP attained in the presence of, r

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Ignarro, L. J., R. E. Byrns, G. M. Buga, and K. S. Wood. "Mechanisms of endothelium-dependent vascular smooth muscle relaxation elicited by bradykinin and VIP." American Journal of Physiology-Heart and Circulatory Physiology 253, no. 5 (1987): H1074—H1082. http://dx.doi.org/10.1152/ajpheart.1987.253.5.h1074.

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The objective of this study was to elucidate the mechanisms by which bradykinin and vasoactive intestinal polypeptide (VIP) relax bovine intrapulmonary artery and bradykinin, but not VIP, relaxes intrapulmonary vein. Bradykinin and VIP elicited entirely endothelium-dependent relaxation of phenylephrine-precontracted arterial rings, and this was associated with arterial accumulation of both guanosine 3',5'-cyclic monophosphate (cGMP) and adenosine 3',5'-cyclic monophosphate (cAMP). Bradykinin, but not VIP, relaxed precontracted venous rings and increased cGMP, but not cAMP levels, by endotheliu

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Witwicka, Hanna, Marcin Kobiałka, and Wojciech A. Gorczyca. "Hydrolysis of cyclic GMP in rat peritoneal macrophages." Acta Biochimica Polonica 49, no. 4 (2002): 891–97. http://dx.doi.org/10.18388/abp.2002_3748.

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Intact rat peritoneal macrophages (rPM) treated with 3-isobutyl-1-methylxanthine (IBMX), an inhibitor of phosphodiesterases (PDEs), accumulated more cGMP than untreated cells. A PDE activity toward [(3)H]cGMP was detected in the soluble and particulate fractions of rPM. The hydrolysis of cGMP was Ca(2+)/calmodulin-independent but increased in the presence of cGMP excess. Similar results were obtained when [(3)H]cAMP was used as a substrate. The hydrolytic activity towards both nucleotides was inhibited in the presence of IBMX. Therefore, the PDEs of families 2, 5, 10 and 11 are potential candi

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