PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33970224-7 2022 The phosphodiesterases PDE2 and PDE3 constrained cGMP in both compartments. Cyclic GMP 49-53 phosphodiesterase 2A Rattus norvegicus 4-22 33970224-7 2022 The phosphodiesterases PDE2 and PDE3 constrained cGMP in both compartments. Cyclic GMP 49-53 phosphodiesterase 2A Rattus norvegicus 23-27 31521738-3 2019 Phosphodiesterase 2A (PDE2A), which is highly expressed in the forebrain, is one of the key phosphodiesterase enzymes that hydrolyze cAMP and cGMP. Cyclic GMP 142-146 phosphodiesterase 2A Rattus norvegicus 0-20 31521738-3 2019 Phosphodiesterase 2A (PDE2A), which is highly expressed in the forebrain, is one of the key phosphodiesterase enzymes that hydrolyze cAMP and cGMP. Cyclic GMP 142-146 phosphodiesterase 2A Rattus norvegicus 22-27 31253692-7 2019 In vitro experiments using recombinant PDE2A protein or rat brain homogenate that contains native PDE2A protein demonstrated that increased cGMP after initial PDE2A inhibition could be responsible for the activation of PDE2A enzyme via allosteric binding to the GAF-B domain, leading to positive cooperativity of the dormant PDE2A enzymes. Cyclic GMP 140-144 phosphodiesterase 2A Rattus norvegicus 98-103 31121256-11 2019 Concomitant treatment with PDE1B, PDE2A, PDE9A and PDE10A inhibitors resulted in a 4.4- and 36.7-fold increase of cGMP in rat and mouse striatum. Cyclic GMP 114-118 phosphodiesterase 2A Rattus norvegicus 34-39 31253692-1 2019 Inhibition of phosphodiesterase 2A (PDE2A) has been proposed as a potential approach to enhance cognitive functioning and memory through boosting intracellular cGMP/cAMP and enhancing neuroplasticity in memory-related neural circuitry. Cyclic GMP 160-164 phosphodiesterase 2A Rattus norvegicus 14-34 31253692-1 2019 Inhibition of phosphodiesterase 2A (PDE2A) has been proposed as a potential approach to enhance cognitive functioning and memory through boosting intracellular cGMP/cAMP and enhancing neuroplasticity in memory-related neural circuitry. Cyclic GMP 160-164 phosphodiesterase 2A Rattus norvegicus 36-41 31253692-7 2019 In vitro experiments using recombinant PDE2A protein or rat brain homogenate that contains native PDE2A protein demonstrated that increased cGMP after initial PDE2A inhibition could be responsible for the activation of PDE2A enzyme via allosteric binding to the GAF-B domain, leading to positive cooperativity of the dormant PDE2A enzymes. Cyclic GMP 140-144 phosphodiesterase 2A Rattus norvegicus 39-44 31253692-7 2019 In vitro experiments using recombinant PDE2A protein or rat brain homogenate that contains native PDE2A protein demonstrated that increased cGMP after initial PDE2A inhibition could be responsible for the activation of PDE2A enzyme via allosteric binding to the GAF-B domain, leading to positive cooperativity of the dormant PDE2A enzymes. Cyclic GMP 140-144 phosphodiesterase 2A Rattus norvegicus 98-103 31253692-7 2019 In vitro experiments using recombinant PDE2A protein or rat brain homogenate that contains native PDE2A protein demonstrated that increased cGMP after initial PDE2A inhibition could be responsible for the activation of PDE2A enzyme via allosteric binding to the GAF-B domain, leading to positive cooperativity of the dormant PDE2A enzymes. Cyclic GMP 140-144 phosphodiesterase 2A Rattus norvegicus 98-103 31253692-7 2019 In vitro experiments using recombinant PDE2A protein or rat brain homogenate that contains native PDE2A protein demonstrated that increased cGMP after initial PDE2A inhibition could be responsible for the activation of PDE2A enzyme via allosteric binding to the GAF-B domain, leading to positive cooperativity of the dormant PDE2A enzymes. Cyclic GMP 140-144 phosphodiesterase 2A Rattus norvegicus 98-103 30051530-7 2018 The effect of 17beta-estradiol on mitochondrial cAMP was prevented by inhibition of a cGMP-activated PDE2 or soluble guanylyl cyclase (sGC), suggesting a role of NO signalling. Cyclic GMP 86-90 phosphodiesterase 2A Rattus norvegicus 101-105 31100470-3 2019 In contrast to the heart ventricle where PDE4 is the major PDE, in cardiac mitochondria, cGMP-stimulated PDE2 activity was largest than PDE3 and PDE4 activities. Cyclic GMP 89-93 phosphodiesterase 2A Rattus norvegicus 41-44 31100470-3 2019 In contrast to the heart ventricle where PDE4 is the major PDE, in cardiac mitochondria, cGMP-stimulated PDE2 activity was largest than PDE3 and PDE4 activities. Cyclic GMP 89-93 phosphodiesterase 2A Rattus norvegicus 105-109 31100470-7 2019 In mitochondria isolated from PDE2 transgenic mice with a cardiac selective PDE2 overexpression, the oxidative phosphorylation (OXPHOS) was significantly lower than in wild-type mice, but stimulated by cGMP. Cyclic GMP 202-206 phosphodiesterase 2A Rattus norvegicus 30-34 31100470-7 2019 In mitochondria isolated from PDE2 transgenic mice with a cardiac selective PDE2 overexpression, the oxidative phosphorylation (OXPHOS) was significantly lower than in wild-type mice, but stimulated by cGMP. Cyclic GMP 202-206 phosphodiesterase 2A Rattus norvegicus 76-80 30651902-11 2018 Conclusion: Intrathecal administration of low-concentration oxygen/ozone alleviated mechanical allodynia and attenuated radiculitis, likely by a PDE2A-cGMP/cAMP-NF-kappaB/p65 signaling pathway in chronic radiculitis rats. Cyclic GMP 151-155 phosphodiesterase 2A Rattus norvegicus 145-150 30835157-6 2019 RESULTS: PDE2A inhibition in AR-5 cells resulted in increases in cAMP/cGMP-related pVASPser239 and pCREBser133. Cyclic GMP 70-74 phosphodiesterase 2A Rattus norvegicus 9-14 29440309-3 2018 Phosphodiesterase 2A (PDE2A) is highly expressed in the forebrain, and is a dual substrate enzyme that hydrolyzes both cAMP and cGMP, which play pivotal roles as intracellular second messengers downstream of NMDA receptors. Cyclic GMP 128-132 phosphodiesterase 2A Rattus norvegicus 0-20 29720569-2 2018 We tested whether phosphodiesterase 2A (PDE2A), which regulates the action of BNP-activated cyclic guanosine monophosphate (cGMP), was directly involved in modulating Ca2+ handling from stellate ganglia (SG) neurons and cardiac norepinephrine (NE) release in rats and humans with an enhanced sympathetic phenotype. Cyclic GMP 92-122 phosphodiesterase 2A Rattus norvegicus 18-38 29720569-2 2018 We tested whether phosphodiesterase 2A (PDE2A), which regulates the action of BNP-activated cyclic guanosine monophosphate (cGMP), was directly involved in modulating Ca2+ handling from stellate ganglia (SG) neurons and cardiac norepinephrine (NE) release in rats and humans with an enhanced sympathetic phenotype. Cyclic GMP 92-122 phosphodiesterase 2A Rattus norvegicus 40-45 29720569-2 2018 We tested whether phosphodiesterase 2A (PDE2A), which regulates the action of BNP-activated cyclic guanosine monophosphate (cGMP), was directly involved in modulating Ca2+ handling from stellate ganglia (SG) neurons and cardiac norepinephrine (NE) release in rats and humans with an enhanced sympathetic phenotype. Cyclic GMP 124-128 phosphodiesterase 2A Rattus norvegicus 18-38 29720569-2 2018 We tested whether phosphodiesterase 2A (PDE2A), which regulates the action of BNP-activated cyclic guanosine monophosphate (cGMP), was directly involved in modulating Ca2+ handling from stellate ganglia (SG) neurons and cardiac norepinephrine (NE) release in rats and humans with an enhanced sympathetic phenotype. Cyclic GMP 124-128 phosphodiesterase 2A Rattus norvegicus 40-45 29440309-3 2018 Phosphodiesterase 2A (PDE2A) is highly expressed in the forebrain, and is a dual substrate enzyme that hydrolyzes both cAMP and cGMP, which play pivotal roles as intracellular second messengers downstream of NMDA receptors. Cyclic GMP 128-132 phosphodiesterase 2A Rattus norvegicus 22-27 28283839-9 2017 RESULTS: Intrathecal administration of the PDE2A inhibitor Bay 60-7550, significantly attenuated mechanical allodynia, down-regulated spinal TNF-alpha, IL-1beta and IL-6 over-expressions, increased the expression of spinal cAMP, as well as cGMP in a more remarkable manner, and decreased the spinal PDE2A expression in NCLDH rats in a dose-dependent manner. Cyclic GMP 240-244 phosphodiesterase 2A Rattus norvegicus 43-48 25939307-5 2015 Cortical cGMP-PDE2 (80.3 vs. 65.1 pmol/min/mg) and cGMP-PDE1 (50.7 vs. 30.1 pmol/min/mg), and cAMP-PDE2 (161 vs. 104.1 pmol/min/mg) and cAMP-PDE4 (307.5 vs. 197.2 pmol/min/mg) activities were higher in MI than in SH rats. Cyclic GMP 9-13 phosphodiesterase 2A Rattus norvegicus 14-18 26178667-7 2015 Second, we analysed the effect of PDE2A and PDE9A inhibition and their role regulating the influence that the second messengers cAMP and cGMP exert on basal transmission. Cyclic GMP 137-141 phosphodiesterase 2A Rattus norvegicus 34-39 26178667-11 2015 Moreover, this function of PDE2A is suggested to rely on an active modulation of the cAMP hydrolysis as a response to changes in cGMP levels at the presynaptic level. Cyclic GMP 129-133 phosphodiesterase 2A Rattus norvegicus 27-32 25916722-9 2015 In addition, overexpression of phosphodiesterase 2A after adenoviral gene transfer markedly decreased BNP stimulation of cGMP and abrogated the BNP responses to the calcium current, intracellular calcium transient, and neurotransmitter release. Cyclic GMP 121-125 phosphodiesterase 2A Rattus norvegicus 31-51 24837549-5 2014 Using selective phosphodiesterase 2 (PDE2) inhibitors and a synthetic cGMP analog activating PDE2, we found that PDE2 is involved in coupling the ANP-triggered signal to the cAMP metabolism. Cyclic GMP 70-74 phosphodiesterase 2A Rattus norvegicus 93-97 24899690-3 2014 Phosphodiesterases (PDEs) are a family of enzymes that break down cGMP and cAMP, which underpin the bioactivity of NO and prostacyclin. Cyclic GMP 66-70 phosphodiesterase 2A Rattus norvegicus 0-18 24899690-3 2014 Phosphodiesterases (PDEs) are a family of enzymes that break down cGMP and cAMP, which underpin the bioactivity of NO and prostacyclin. Cyclic GMP 66-70 phosphodiesterase 2A Rattus norvegicus 20-24 24837549-6 2014 We have established that ANP-induced elevated levels of cGMP as well as cGMP analog stimulate hydrolytic activity of PDE2, leading to inhibition of adenosine-induced transcription of the TH gene. Cyclic GMP 56-60 phosphodiesterase 2A Rattus norvegicus 117-121 24837549-6 2014 We have established that ANP-induced elevated levels of cGMP as well as cGMP analog stimulate hydrolytic activity of PDE2, leading to inhibition of adenosine-induced transcription of the TH gene. Cyclic GMP 72-76 phosphodiesterase 2A Rattus norvegicus 117-121 24837549-5 2014 Using selective phosphodiesterase 2 (PDE2) inhibitors and a synthetic cGMP analog activating PDE2, we found that PDE2 is involved in coupling the ANP-triggered signal to the cAMP metabolism. Cyclic GMP 70-74 phosphodiesterase 2A Rattus norvegicus 93-97 24424715-0 2014 Differential regulation of C-type natriuretic peptide-induced cGMP and functional responses by PDE2 and PDE3 in failing myocardium. Cyclic GMP 62-66 phosphodiesterase 2A Rattus norvegicus 95-99 24424715-4 2014 CNP-mediated increase in global cGMP was mainly regulated by PDE2, as reflected by a marked amplification of the cGMP increase during PDE2 inhibition and by a high PDE2 activity in cardiomyocytes. Cyclic GMP 113-117 phosphodiesterase 2A Rattus norvegicus 61-65 24424715-4 2014 CNP-mediated increase in global cGMP was mainly regulated by PDE2, as reflected by a marked amplification of the cGMP increase during PDE2 inhibition and by a high PDE2 activity in cardiomyocytes. Cyclic GMP 113-117 phosphodiesterase 2A Rattus norvegicus 134-138 24424715-4 2014 CNP-mediated increase in global cGMP was mainly regulated by PDE2, as reflected by a marked amplification of the cGMP increase during PDE2 inhibition and by a high PDE2 activity in cardiomyocytes. Cyclic GMP 113-117 phosphodiesterase 2A Rattus norvegicus 134-138 24424715-12 2014 Global cGMP levels are mainly regulated by PDE2 after CNP stimulation, whereas the functional responses are modestly regulated by both PDE2 and PDE3, indicating cGMP compartmentation by PDEs affecting CNP-induced responses in failing hearts. Cyclic GMP 7-11 phosphodiesterase 2A Rattus norvegicus 43-47 24424715-12 2014 Global cGMP levels are mainly regulated by PDE2 after CNP stimulation, whereas the functional responses are modestly regulated by both PDE2 and PDE3, indicating cGMP compartmentation by PDEs affecting CNP-induced responses in failing hearts. Cyclic GMP 161-165 phosphodiesterase 2A Rattus norvegicus 186-190 24424715-2 2014 We wanted to study whether, and if so, how phosphodiesterases (PDEs) regulate CNP-induced cyclic 3",5"-guanosine monophosphate (cGMP) elevation and functional responses. Cyclic GMP 90-126 phosphodiesterase 2A Rattus norvegicus 43-61 24424715-2 2014 We wanted to study whether, and if so, how phosphodiesterases (PDEs) regulate CNP-induced cyclic 3",5"-guanosine monophosphate (cGMP) elevation and functional responses. Cyclic GMP 90-126 phosphodiesterase 2A Rattus norvegicus 63-67 24424715-2 2014 We wanted to study whether, and if so, how phosphodiesterases (PDEs) regulate CNP-induced cyclic 3",5"-guanosine monophosphate (cGMP) elevation and functional responses. Cyclic GMP 128-132 phosphodiesterase 2A Rattus norvegicus 43-61 24424715-2 2014 We wanted to study whether, and if so, how phosphodiesterases (PDEs) regulate CNP-induced cyclic 3",5"-guanosine monophosphate (cGMP) elevation and functional responses. Cyclic GMP 128-132 phosphodiesterase 2A Rattus norvegicus 63-67 24424715-4 2014 CNP-mediated increase in global cGMP was mainly regulated by PDE2, as reflected by a marked amplification of the cGMP increase during PDE2 inhibition and by a high PDE2 activity in cardiomyocytes. Cyclic GMP 32-36 phosphodiesterase 2A Rattus norvegicus 61-65 23597790-4 2013 These newly designed PDE2 inhibitors bind to the PDE2 enzyme in a cGMP-like binding mode orthogonal to the cAMP-like binding mode found in PDE4. Cyclic GMP 66-70 phosphodiesterase 2A Rattus norvegicus 21-25 24531807-0 2014 PDE2-mediated cAMP hydrolysis accelerates cardiac fibroblast to myofibroblast conversion and is antagonized by exogenous activation of cGMP signaling pathways. Cyclic GMP 135-139 phosphodiesterase 2A Rattus norvegicus 0-4 24531807-2 2014 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. Cyclic GMP 75-79 phosphodiesterase 2A Rattus norvegicus 25-29 24531807-8 2014 Interestingly, despite persistently depressed cAMP levels, both cGMP-elevating stimuli were able to completely prevent the PDE2-induced MyoCF phenotype, arguing for a double-tracked mechanism. Cyclic GMP 64-68 phosphodiesterase 2A Rattus norvegicus 123-127 24531807-10 2014 Atrial natriuretic peptide- and sodium nitroprusside-mediated cGMP synthesis completely reverses PDE2-induced fibroblast conversion. Cyclic GMP 62-66 phosphodiesterase 2A Rattus norvegicus 97-101 24531807-11 2014 Thus PDE2 may augment cardiac remodeling, but this effect can also be overcome by enhanced cGMP. Cyclic GMP 91-95 phosphodiesterase 2A Rattus norvegicus 5-9 24184653-1 2014 3",5"-cyclic nucleotide phosphodiesterases (PDEs) are the only known enzymes to compartmentalize cAMP and cGMP, yet little is known about how PDEs are dynamically regulated across the lifespan. Cyclic GMP 106-110 phosphodiesterase 2A Rattus norvegicus 24-42 24184653-1 2014 3",5"-cyclic nucleotide phosphodiesterases (PDEs) are the only known enzymes to compartmentalize cAMP and cGMP, yet little is known about how PDEs are dynamically regulated across the lifespan. Cyclic GMP 106-110 phosphodiesterase 2A Rattus norvegicus 44-48 23810893-3 2013 Among the PDE superfamily, PDE2 has the unique property of being able to be stimulated by cGMP, thus leading to a remarkable increase in cAMP hydrolysis mediating a negative cross talk between cGMP and cAMP signaling. Cyclic GMP 90-94 phosphodiesterase 2A Rattus norvegicus 10-13 23810893-3 2013 Among the PDE superfamily, PDE2 has the unique property of being able to be stimulated by cGMP, thus leading to a remarkable increase in cAMP hydrolysis mediating a negative cross talk between cGMP and cAMP signaling. Cyclic GMP 90-94 phosphodiesterase 2A Rattus norvegicus 27-31 23810893-3 2013 Among the PDE superfamily, PDE2 has the unique property of being able to be stimulated by cGMP, thus leading to a remarkable increase in cAMP hydrolysis mediating a negative cross talk between cGMP and cAMP signaling. Cyclic GMP 193-197 phosphodiesterase 2A Rattus norvegicus 10-13 23810893-3 2013 Among the PDE superfamily, PDE2 has the unique property of being able to be stimulated by cGMP, thus leading to a remarkable increase in cAMP hydrolysis mediating a negative cross talk between cGMP and cAMP signaling. Cyclic GMP 193-197 phosphodiesterase 2A Rattus norvegicus 27-31 23810893-8 2013 In diseased cardiomyocytes, higher PDE2 activity could be further enhanced by stimulation of cGMP synthesis via nitric oxide donors, whereas specific PDE2 inhibition partially restored beta-AR responsiveness. Cyclic GMP 93-97 phosphodiesterase 2A Rattus norvegicus 35-39 23597790-4 2013 These newly designed PDE2 inhibitors bind to the PDE2 enzyme in a cGMP-like binding mode orthogonal to the cAMP-like binding mode found in PDE4. Cyclic GMP 66-70 phosphodiesterase 2A Rattus norvegicus 49-53 21330599-2 2011 cGMP can potentially affect cAMP signals via cGMP-regulated phosphodiesterases (PDEs). Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 80-84 21653225-8 2011 The expression of a number of cGMP PDE isoforms in skeletal muscle suggests that targeting specific cGMP PDE isoforms may provide a promising avenue for development of a novel class of therapeutics for enhancing muscle insulin sensitivity. Cyclic GMP 30-34 phosphodiesterase 2A Rattus norvegicus 35-38 21653225-8 2011 The expression of a number of cGMP PDE isoforms in skeletal muscle suggests that targeting specific cGMP PDE isoforms may provide a promising avenue for development of a novel class of therapeutics for enhancing muscle insulin sensitivity. Cyclic GMP 100-104 phosphodiesterase 2A Rattus norvegicus 35-38 21330599-2 2011 cGMP can potentially affect cAMP signals via cGMP-regulated phosphodiesterases (PDEs). Cyclic GMP 45-49 phosphodiesterase 2A Rattus norvegicus 80-84 21330599-7 2011 These opposing effects are determined by the cGMP-regulated PDEs, namely PDE2 and PDE3, with the local activity of these PDEs being critically important. Cyclic GMP 45-49 phosphodiesterase 2A Rattus norvegicus 60-64 21330599-7 2011 These opposing effects are determined by the cGMP-regulated PDEs, namely PDE2 and PDE3, with the local activity of these PDEs being critically important. Cyclic GMP 45-49 phosphodiesterase 2A Rattus norvegicus 73-77 21330599-7 2011 These opposing effects are determined by the cGMP-regulated PDEs, namely PDE2 and PDE3, with the local activity of these PDEs being critically important. Cyclic GMP 45-49 phosphodiesterase 2A Rattus norvegicus 121-125 21330599-9 2011 CONCLUSIONS: cGMP signals exert opposing effects on local cAMP levels via different PDEs the activity of which is exerted in spatially distinct subcellular domains. Cyclic GMP 13-17 phosphodiesterase 2A Rattus norvegicus 84-88 21330599-10 2011 Inhibition of PDE2 selectively abolishes the negative effects of cGMP on cAMP and may have therapeutic potential. Cyclic GMP 65-69 phosphodiesterase 2A Rattus norvegicus 14-18 21151982-7 2010 cAMP-PDE4 activity was specifically increased while cGMP-PDE activities were broadly increased (+130% for PDE1; +76% for PDE2; +113% for PDE5) and associated with increased expressions for PDE1A, PDE1C and PDE5A. Cyclic GMP 52-56 phosphodiesterase 2A Rattus norvegicus 121-125 21151982-10 2010 In early cardiac hypertrophy induced by angiotensin II, all specific PDE activities in left cardiac ventricles were increased, favoring an increase in cGMP hydrolysis by PDE1, PDE2 and PDE5. Cyclic GMP 151-155 phosphodiesterase 2A Rattus norvegicus 69-72 21151982-10 2010 In early cardiac hypertrophy induced by angiotensin II, all specific PDE activities in left cardiac ventricles were increased, favoring an increase in cGMP hydrolysis by PDE1, PDE2 and PDE5. Cyclic GMP 151-155 phosphodiesterase 2A Rattus norvegicus 176-180 21151982-14 2010 Nevertheless, our results suggest a potential link between PDE4 and AMPK/NOX2 and they point out that cGMP-PDEs, especially PDE1 and PDE2, may be interesting therapeutic targets in preventing cardiac hypertrophy. Cyclic GMP 102-106 phosphodiesterase 2A Rattus norvegicus 107-111 21151982-14 2010 Nevertheless, our results suggest a potential link between PDE4 and AMPK/NOX2 and they point out that cGMP-PDEs, especially PDE1 and PDE2, may be interesting therapeutic targets in preventing cardiac hypertrophy. Cyclic GMP 102-106 phosphodiesterase 2A Rattus norvegicus 133-137 20196107-3 2010 Phosphodiesterases (PDEs) degrade cyclic nucleotide second messenger cAMP and cGMP downstream of NO thereby limiting the vasodilatory response to NO. Cyclic GMP 78-82 phosphodiesterase 2A Rattus norvegicus 20-24 20213343-3 2010 Phosphodiesterases (PDEs) are enzymes for hydrolysis of cGMP in the brain, and they are mainly isoforms 2, 5, and 9. Cyclic GMP 56-60 phosphodiesterase 2A Rattus norvegicus 0-18 20213343-3 2010 Phosphodiesterases (PDEs) are enzymes for hydrolysis of cGMP in the brain, and they are mainly isoforms 2, 5, and 9. Cyclic GMP 56-60 phosphodiesterase 2A Rattus norvegicus 20-24 20196107-3 2010 Phosphodiesterases (PDEs) degrade cyclic nucleotide second messenger cAMP and cGMP downstream of NO thereby limiting the vasodilatory response to NO. Cyclic GMP 78-82 phosphodiesterase 2A Rattus norvegicus 0-18 20139324-4 2010 The two cyclic nucleotides, cAMP and cGMP, central to the regulation of vascular barrier integrity, are hydrolyzed by phosphodiesterases (PDE). Cyclic GMP 37-41 phosphodiesterase 2A Rattus norvegicus 118-136 18499090-1 2008 Our previous studies have shown that there is a lower cGMP concentration in the aged brain as well as an alteration in the activity of cGMP-hydrolyzing phosphodiesterases (PDEs) and nitric oxide synthase (NOS). Cyclic GMP 135-139 phosphodiesterase 2A Rattus norvegicus 172-176 18957291-2 2008 The present study aimed to reveal the ability of PDE5 and PDE2 inhibitors, that increase cyclic guanosine monophosphate (cGMP) and both cyclic adenosine monophosphate (cAMP) and cGMP, respectively, to reverse an object recognition deficit induced by acute tryptophan depletion. Cyclic GMP 89-119 phosphodiesterase 2A Rattus norvegicus 58-62 18957291-2 2008 The present study aimed to reveal the ability of PDE5 and PDE2 inhibitors, that increase cyclic guanosine monophosphate (cGMP) and both cyclic adenosine monophosphate (cAMP) and cGMP, respectively, to reverse an object recognition deficit induced by acute tryptophan depletion. Cyclic GMP 121-125 phosphodiesterase 2A Rattus norvegicus 58-62 18957291-2 2008 The present study aimed to reveal the ability of PDE5 and PDE2 inhibitors, that increase cyclic guanosine monophosphate (cGMP) and both cyclic adenosine monophosphate (cAMP) and cGMP, respectively, to reverse an object recognition deficit induced by acute tryptophan depletion. Cyclic GMP 178-182 phosphodiesterase 2A Rattus norvegicus 58-62 18655195-1 2008 We have characterized the various phosphodiesterases (PDE) that degrade cyclic GMP in the prefrontal cortex, hippocampus, and cerebellum using the microdialysis technique to measure in vivo extracellular cyclic GMP in awake rats. Cyclic GMP 72-82 phosphodiesterase 2A Rattus norvegicus 34-52 18655195-1 2008 We have characterized the various phosphodiesterases (PDE) that degrade cyclic GMP in the prefrontal cortex, hippocampus, and cerebellum using the microdialysis technique to measure in vivo extracellular cyclic GMP in awake rats. Cyclic GMP 72-82 phosphodiesterase 2A Rattus norvegicus 54-57 18655195-1 2008 We have characterized the various phosphodiesterases (PDE) that degrade cyclic GMP in the prefrontal cortex, hippocampus, and cerebellum using the microdialysis technique to measure in vivo extracellular cyclic GMP in awake rats. Cyclic GMP 204-214 phosphodiesterase 2A Rattus norvegicus 34-52 18655195-1 2008 We have characterized the various phosphodiesterases (PDE) that degrade cyclic GMP in the prefrontal cortex, hippocampus, and cerebellum using the microdialysis technique to measure in vivo extracellular cyclic GMP in awake rats. Cyclic GMP 204-214 phosphodiesterase 2A Rattus norvegicus 54-57 18655195-7 2008 This is the first in vivo functional study showing that, in cortex, PDE1, -2, and -5/9 degrade cGMP, with PDE9 probably playing a major role; in hippocampus, PDE5/9 and PDE1 are mainly involved and seem almost equally active, but PDE2 and -3 also contribute; in cerebellum, PDE5/9 are the main cGMP hydrolyzing enzymes, but also PDE1 and -4 significantly operate. Cyclic GMP 95-99 phosphodiesterase 2A Rattus norvegicus 68-84 18655195-7 2008 This is the first in vivo functional study showing that, in cortex, PDE1, -2, and -5/9 degrade cGMP, with PDE9 probably playing a major role; in hippocampus, PDE5/9 and PDE1 are mainly involved and seem almost equally active, but PDE2 and -3 also contribute; in cerebellum, PDE5/9 are the main cGMP hydrolyzing enzymes, but also PDE1 and -4 significantly operate. Cyclic GMP 95-99 phosphodiesterase 2A Rattus norvegicus 230-241 18655195-7 2008 This is the first in vivo functional study showing that, in cortex, PDE1, -2, and -5/9 degrade cGMP, with PDE9 probably playing a major role; in hippocampus, PDE5/9 and PDE1 are mainly involved and seem almost equally active, but PDE2 and -3 also contribute; in cerebellum, PDE5/9 are the main cGMP hydrolyzing enzymes, but also PDE1 and -4 significantly operate. Cyclic GMP 294-298 phosphodiesterase 2A Rattus norvegicus 68-84 18501878-7 2008 cGMP levels in the cultured forebrain neurons were also increased when cells were stimulated with DEANO in the presence of the selective PDE inhibitors BAY 60-7550 (PDE2), sildenafil (PDE5), or the mixed type inhibitor papaverine (PDE2,5,10). Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 165-169 18501878-7 2008 cGMP levels in the cultured forebrain neurons were also increased when cells were stimulated with DEANO in the presence of the selective PDE inhibitors BAY 60-7550 (PDE2), sildenafil (PDE5), or the mixed type inhibitor papaverine (PDE2,5,10). Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 231-235 19632989-1 2009 The cGMP-stimulated PDE2A hydrolyzes both cyclic nucleotides, cGMP and cAMP. Cyclic GMP 4-8 phosphodiesterase 2A Rattus norvegicus 20-25 19632989-1 2009 The cGMP-stimulated PDE2A hydrolyzes both cyclic nucleotides, cGMP and cAMP. Cyclic GMP 62-66 phosphodiesterase 2A Rattus norvegicus 20-25 18684888-0 2008 cGMP decreases surface NKCC2 levels in the thick ascending limb: role of phosphodiesterase 2 (PDE2). Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 73-92 18684888-0 2008 cGMP decreases surface NKCC2 levels in the thick ascending limb: role of phosphodiesterase 2 (PDE2). Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 94-98 18684888-10 2008 cGMP-stimulated phosphodiesterase 2 (PDE2) mediates the inhibitory effect of NO on NaCl absorption by THALs. Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 16-35 18684888-10 2008 cGMP-stimulated phosphodiesterase 2 (PDE2) mediates the inhibitory effect of NO on NaCl absorption by THALs. Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 37-41 18684888-14 2008 We conclude that cGMP decreases NKCC2 levels in the apical membrane of THALs and that this effect is mediated by PDE2. Cyclic GMP 17-21 phosphodiesterase 2A Rattus norvegicus 113-117 17302738-3 2007 cGMP is the ligand for the GAF domains in PDEs 2, 5, 6 and 11, and cAMP is the ligand for PDE10. Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 42-46 17302738-9 2007 We were unable, however, to switch the purine specificity of the PDE2 tandem GAF domain from cGMP to cAMP in reverse constructs, i.e. by replacement of PDE2 segments with those from the cyaB1 GAF tandem domain. Cyclic GMP 93-97 phosphodiesterase 2A Rattus norvegicus 65-69 17407767-1 2007 NMDA receptor-induced cAMP and cGMP are selectively hydrolyzed by PDE4 and PDE2, respectively, in rat primary cerebral cortical and hippocampal cultures. Cyclic GMP 31-35 phosphodiesterase 2A Rattus norvegicus 75-79 17302738-7 2007 Segmental replacements in the highly divergent beta1-beta3 region of the GAF B subdomain of cyaB1 by the corresponding PDE2 regions switched signalling from cAMP to cGMP. Cyclic GMP 165-169 phosphodiesterase 2A Rattus norvegicus 119-123 17141339-2 2007 Looking for proteins potentially regulated by cGMP in rat peritoneal macrophages (PMs), in this study we analyzed expression and activity of cGMP-hydrolyzing and cGMP-regulated phosphodiesterases (PDEs). Cyclic GMP 46-50 phosphodiesterase 2A Rattus norvegicus 197-201 17141339-4 2007 Analysis of substrate specificity, sensitivity to inhibitors, and subcellular localization showed that PDE2 and PDE3 are the main cGMP-regulated PDE isoforms in PEMs. Cyclic GMP 130-134 phosphodiesterase 2A Rattus norvegicus 103-107 17141339-10 2007 Taken together, our results show that in rat PMs expression of cGMP-dependent PDEs positively correlates with the activation state of cells. Cyclic GMP 63-67 phosphodiesterase 2A Rattus norvegicus 78-82 17141339-11 2007 Moreover, the fact that most of these PDEs hydrolyze also cAMP indicates that cGMP can play a role of potent regulator of cAMP signaling in macrophages. Cyclic GMP 78-82 phosphodiesterase 2A Rattus norvegicus 38-42 12834273-2 2003 Activities of two cyclic nucleotide phosphodiesterase (PDE) isoforms, Ca2+/calmodulin-stimulated PDE (PDE1) and cGMP-stimulated PDE (PDE2), were significantly higher in rat left ventricles 14 days after aortic banding. Cyclic GMP 112-116 phosphodiesterase 2A Rattus norvegicus 133-137 16621444-9 2006 PDE2, 5, and 9 are involved in regulating NP-stimulated cGMP levels in the spinal cord. Cyclic GMP 56-60 phosphodiesterase 2A Rattus norvegicus 0-4 15599707-9 2004 In contrast, the 7-rhamnoglucoside of hesperetin, hesperidin (10 microM-0.1 mM), was inactive in practically all experiments, although it inhibited basal and cGMP-activated PDE2 isolated from platelets (IC(50) values of 32+/-4 microM and 137+/-34 microM respectively). Cyclic GMP 158-162 phosphodiesterase 2A Rattus norvegicus 173-177 12358727-3 2002 Studies on cerebellar astrocytes showed that sGC undergoes a desensitizing profile of activity, which, in league with phosphodiesterases (PDEs), was hypothesized to diversify cGMP responses in different cells. Cyclic GMP 175-179 phosphodiesterase 2A Rattus norvegicus 138-142 12358727-5 2002 Based on the effects of selective PDE inhibitors, cGMP hydrolysis following exposure to NO was attributed to a cGMP-stimulated PDE (PDE 2). Cyclic GMP 50-54 phosphodiesterase 2A Rattus norvegicus 132-137 12358727-5 2002 Based on the effects of selective PDE inhibitors, cGMP hydrolysis following exposure to NO was attributed to a cGMP-stimulated PDE (PDE 2). Cyclic GMP 111-115 phosphodiesterase 2A Rattus norvegicus 132-137 12107056-7 2002 Although NO reportedly acts by reducing AC activity in some cells, in cardiac fibroblasts NO production decreases cAMP accumulation largely by the cGMP-mediated activation of PDE2. Cyclic GMP 147-151 phosphodiesterase 2A Rattus norvegicus 175-179 12107056-0 2002 Attenuation of cAMP accumulation in adult rat cardiac fibroblasts by IL-1beta and NO: role of cGMP-stimulated PDE2. Cyclic GMP 94-98 phosphodiesterase 2A Rattus norvegicus 110-114 12221013-5 2002 In the young rat, PDE1 hydrolysed cGMP three-fold more than the control, and PDE2 (cGMP-stimulated PDE) was present, indicating that the concentration of intracellular cGMP may be enhanced, and cGMP may function in the growth pathway in the submandibular gland. Cyclic GMP 83-87 phosphodiesterase 2A Rattus norvegicus 77-81 12221013-5 2002 In the young rat, PDE1 hydrolysed cGMP three-fold more than the control, and PDE2 (cGMP-stimulated PDE) was present, indicating that the concentration of intracellular cGMP may be enhanced, and cGMP may function in the growth pathway in the submandibular gland. Cyclic GMP 83-87 phosphodiesterase 2A Rattus norvegicus 77-81 12221013-5 2002 In the young rat, PDE1 hydrolysed cGMP three-fold more than the control, and PDE2 (cGMP-stimulated PDE) was present, indicating that the concentration of intracellular cGMP may be enhanced, and cGMP may function in the growth pathway in the submandibular gland. Cyclic GMP 83-87 phosphodiesterase 2A Rattus norvegicus 77-81 12065724-0 2002 Hydrolysis of N-methyl-D-aspartate receptor-stimulated cAMP and cGMP by PDE4 and PDE2 phosphodiesterases in primary neuronal cultures of rat cerebral cortex and hippocampus. Cyclic GMP 64-68 phosphodiesterase 2A Rattus norvegicus 81-85 12065724-5 2002 In contrast, only the PDE2 inhibitor erythro-9-(2-hydroxy-3-nonyl) adenine (EHNA) enhanced the ability of NMDA to increase cGMP. Cyclic GMP 123-127 phosphodiesterase 2A Rattus norvegicus 22-26 12065724-9 2002 Overall, the present findings indicate that cAMP and cGMP formed in neurons as a result of NMDA receptor stimulation are hydrolyzed by PDE4 and PDE2, respectively. Cyclic GMP 53-57 phosphodiesterase 2A Rattus norvegicus 144-148 9756358-3 1998 We identified the activity of five distinct cAMP-PDE isozymes: two calcium/calmodulin-dependent forms (PDE 1), one PDE 2 isozyme stimulated by guanosine-3",5"-monophosphate (cGMP), one cGMP-inhibited form (PDE 3) and a cAMP-specific, rolipram-sensitive form (PDE 4). Cyclic GMP 174-178 phosphodiesterase 2A Rattus norvegicus 49-52 12003819-5 2002 Modulation of cGMP accumulation by phosphodiesterases (PDEs) was cell specific as determined by antagonist pharmacological profiles, PDE1 in fibroblasts, PDE2 in A7r5 cells, and PDE3 in myocytes, suggesting that significant but low-level cGMP response to CNP measured in heart myocytes is not due to nonmyocyte contamination. Cyclic GMP 14-18 phosphodiesterase 2A Rattus norvegicus 55-59 12003819-5 2002 Modulation of cGMP accumulation by phosphodiesterases (PDEs) was cell specific as determined by antagonist pharmacological profiles, PDE1 in fibroblasts, PDE2 in A7r5 cells, and PDE3 in myocytes, suggesting that significant but low-level cGMP response to CNP measured in heart myocytes is not due to nonmyocyte contamination. Cyclic GMP 14-18 phosphodiesterase 2A Rattus norvegicus 154-158 12003819-5 2002 Modulation of cGMP accumulation by phosphodiesterases (PDEs) was cell specific as determined by antagonist pharmacological profiles, PDE1 in fibroblasts, PDE2 in A7r5 cells, and PDE3 in myocytes, suggesting that significant but low-level cGMP response to CNP measured in heart myocytes is not due to nonmyocyte contamination. Cyclic GMP 238-242 phosphodiesterase 2A Rattus norvegicus 55-59 10913949-1 2000 OBJECTIVE: In order to determine the mechanism by which nitric oxide (NO) inhibits prolactin release, we investigated the participation of cGMP-dependent cAMP-phosphodiesterases (PDEs) and protein kinase G (PKG) in this effect of NO. Cyclic GMP 139-143 phosphodiesterase 2A Rattus norvegicus 179-183 10913949-9 2000 The activation of PDE2 by cGMP may mediate the inhibitory effect of NO on cAMP concentration and therefore on prolactin release. Cyclic GMP 26-30 phosphodiesterase 2A Rattus norvegicus 18-22 10704943-8 2000 Separation of the PDEs by Q-Sepharose chromatography revealed three cGMP-hydrolyzing peaks. Cyclic GMP 68-72 phosphodiesterase 2A Rattus norvegicus 18-22 10704943-11 2000 The third peak was sensitive to the PDE2 (cGMP-stimulated PDE) isoenzyme-selective inhibitor 9-[2-hydroxy-3-nonyl]adenine (EHNA) (IC(50) = 3 microM), and was activated by over 300% in the presence of 4 microM cGMP. Cyclic GMP 42-46 phosphodiesterase 2A Rattus norvegicus 36-40 10704943-11 2000 The third peak was sensitive to the PDE2 (cGMP-stimulated PDE) isoenzyme-selective inhibitor 9-[2-hydroxy-3-nonyl]adenine (EHNA) (IC(50) = 3 microM), and was activated by over 300% in the presence of 4 microM cGMP. Cyclic GMP 209-213 phosphodiesterase 2A Rattus norvegicus 36-40 10704943-14 2000 Three distinct cGMP-hydrolyzing PDEs, namely PDE5, PDE1, and PDE2, are present in the studied cells. Cyclic GMP 15-19 phosphodiesterase 2A Rattus norvegicus 61-65 10092879-10 1999 These results suggest that PKC selectively activates a PDE2, cGMP-stimulated isoform in the GE fraction. Cyclic GMP 61-65 phosphodiesterase 2A Rattus norvegicus 55-59 11532906-5 2001 Neither pertussis toxin treatment nor exposure to the cGMP-stimulated phosphodiesterase (PDE2) inhibitor erythro-9-(2-hydroxy-3-nonyl)adenine or the nonselective PDE inhibitor 3-isobutyl-1-methylxanthine nor the phosphatase inhibitors okadaic acid or calyculin A unmasked an ISO-mimicking response of GLP-1. Cyclic GMP 54-58 phosphodiesterase 2A Rattus norvegicus 89-93 11181844-2 2001 In our studies, NGF causes over 50% loss of PDE 2 activity (cyclic GMP-stimulated cyclic nucleotide phosphodiesterase) in PC12 cells within 24 h. After 72 h of NGF treatment, cyclic AMP hydrolysis in PC12 extracts is no longer cyclic GMP-stimulated. Cyclic GMP 60-70 phosphodiesterase 2A Rattus norvegicus 44-49 11150485-1 2001 The effects of selective and non-selective 3",5"-cyclic nucleotide phosphodiesterase (PDE) inhibitors on cGMP and cAMP accumulation were studied in rat hippocampal slices incubated in vitro. Cyclic GMP 105-109 phosphodiesterase 2A Rattus norvegicus 86-89 11150485-4 2001 cGMP immunocytochemistry showed that incubation with different inhibitors in the presence and/or absence of sodium nitroprusside resulted in pronounced differences in the extent and regional localization of the cGMP response and indicate that PDE activity in the hippocampus is high and diverse in nature. Cyclic GMP 0-4 phosphodiesterase 2A Rattus norvegicus 243-246 11150485-4 2001 cGMP immunocytochemistry showed that incubation with different inhibitors in the presence and/or absence of sodium nitroprusside resulted in pronounced differences in the extent and regional localization of the cGMP response and indicate that PDE activity in the hippocampus is high and diverse in nature. Cyclic GMP 211-215 phosphodiesterase 2A Rattus norvegicus 243-246 10984544-2 2000 However, a small number of olfactory neurons specifically express cGMP-signaling components, namely a guanylyl cyclase (GC-D) and a cGMP-stimulated phosphodiesterase (PDE2). Cyclic GMP 66-70 phosphodiesterase 2A Rattus norvegicus 167-171 10984544-2 2000 However, a small number of olfactory neurons specifically express cGMP-signaling components, namely a guanylyl cyclase (GC-D) and a cGMP-stimulated phosphodiesterase (PDE2). Cyclic GMP 132-136 phosphodiesterase 2A Rattus norvegicus 167-171 10984544-3 2000 Here, we show that this subset of olfactory neurons expressing GC-D and PDE2 does also express the subunit of a cGMP-selective cyclic nucleotide-gated (CNG) channel that has been previously identified in cone photoreceptors. Cyclic GMP 112-116 phosphodiesterase 2A Rattus norvegicus 72-76 10433216-6 1999 Indeed, time-course studies indicated that ACTH induced a rapid decrease in cGMP production, resulting in PDE2 inhibition, which in turn, contributed [with adenylyl cyclase (AC) activation] to an accumulation in cAMP for 15 min. Cyclic GMP 76-80 phosphodiesterase 2A Rattus norvegicus 106-110 10433216-8 1999 Hence, we demonstrate that the ACTH-induced increase in intracellular cAMP is the result of a balance between activation of AC and direct modulation of PDE2 activity, an effect mediated by cGMP content. Cyclic GMP 189-193 phosphodiesterase 2A Rattus norvegicus 152-156 10419011-2 1999 We demonstrate that the increase in cAMP production induced by ACTH is the result of a balance between activation of adenylyl cyclase and direct modulation of a PDE2 phosphodiestease activity, an effect mediated by inhibition of cGMP content. Cyclic GMP 229-233 phosphodiesterase 2A Rattus norvegicus 161-165 9756358-3 1998 We identified the activity of five distinct cAMP-PDE isozymes: two calcium/calmodulin-dependent forms (PDE 1), one PDE 2 isozyme stimulated by guanosine-3",5"-monophosphate (cGMP), one cGMP-inhibited form (PDE 3) and a cAMP-specific, rolipram-sensitive form (PDE 4). Cyclic GMP 174-178 phosphodiesterase 2A Rattus norvegicus 115-120 9756358-3 1998 We identified the activity of five distinct cAMP-PDE isozymes: two calcium/calmodulin-dependent forms (PDE 1), one PDE 2 isozyme stimulated by guanosine-3",5"-monophosphate (cGMP), one cGMP-inhibited form (PDE 3) and a cAMP-specific, rolipram-sensitive form (PDE 4). Cyclic GMP 185-189 phosphodiesterase 2A Rattus norvegicus 49-52 9756358-3 1998 We identified the activity of five distinct cAMP-PDE isozymes: two calcium/calmodulin-dependent forms (PDE 1), one PDE 2 isozyme stimulated by guanosine-3",5"-monophosphate (cGMP), one cGMP-inhibited form (PDE 3) and a cAMP-specific, rolipram-sensitive form (PDE 4). Cyclic GMP 185-189 phosphodiesterase 2A Rattus norvegicus 115-120 8869231-4 1996 In frog ventricular myocytes, cGMP inhibits ICa by stimulation of a cGMP-stimulated cAMP phosphodiesterase (PDE2), whereas in rat ventricular myocytes, cGMP predominantly inhibits ICa via a mechanism involving activation of a cGMP-dependent protein kinase (cGMP-PK). Cyclic GMP 68-72 phosphodiesterase 2A Rattus norvegicus 108-112 8869231-4 1996 In frog ventricular myocytes, cGMP inhibits ICa by stimulation of a cGMP-stimulated cAMP phosphodiesterase (PDE2), whereas in rat ventricular myocytes, cGMP predominantly inhibits ICa via a mechanism involving activation of a cGMP-dependent protein kinase (cGMP-PK). Cyclic GMP 30-34 phosphodiesterase 2A Rattus norvegicus 108-112 8869231-4 1996 In frog ventricular myocytes, cGMP inhibits ICa by stimulation of a cGMP-stimulated cAMP phosphodiesterase (PDE2), whereas in rat ventricular myocytes, cGMP predominantly inhibits ICa via a mechanism involving activation of a cGMP-dependent protein kinase (cGMP-PK). Cyclic GMP 68-72 phosphodiesterase 2A Rattus norvegicus 108-112 8869231-4 1996 In frog ventricular myocytes, cGMP inhibits ICa by stimulation of a cGMP-stimulated cAMP phosphodiesterase (PDE2), whereas in rat ventricular myocytes, cGMP predominantly inhibits ICa via a mechanism involving activation of a cGMP-dependent protein kinase (cGMP-PK). Cyclic GMP 68-72 phosphodiesterase 2A Rattus norvegicus 108-112 9500857-1 1998 Phosphodiesterases (PDEs) include a large group of structurally related enzymes that belong to at least seven related gene families (PDEs 1-7) that differ in their primary structure, affinity for cAMP and cGMP, response to specific effectors, sensitivity to specific inhibitors, and regulatory mechanism. Cyclic GMP 205-209 phosphodiesterase 2A Rattus norvegicus 0-18 9500857-1 1998 Phosphodiesterases (PDEs) include a large group of structurally related enzymes that belong to at least seven related gene families (PDEs 1-7) that differ in their primary structure, affinity for cAMP and cGMP, response to specific effectors, sensitivity to specific inhibitors, and regulatory mechanism. Cyclic GMP 205-209 phosphodiesterase 2A Rattus norvegicus 20-24 9500857-1 1998 Phosphodiesterases (PDEs) include a large group of structurally related enzymes that belong to at least seven related gene families (PDEs 1-7) that differ in their primary structure, affinity for cAMP and cGMP, response to specific effectors, sensitivity to specific inhibitors, and regulatory mechanism. Cyclic GMP 205-209 phosphodiesterase 2A Rattus norvegicus 133-141 8869231-7 1996 Biochemical characterization of the endogenous phosphodiesterases and cGMP-PK in purified cardiac myocytes provide further evidence in support of these mechanisms of cGMP action on ICa. Cyclic GMP 166-170 phosphodiesterase 2A Rattus norvegicus 47-65 1664725-6 1991 Patch-clamp measurements of ICa indicate that in isolated frog myocytes cGMP inhibits ICa by stimulation of cAMP phosphodiesterase (cGS-PDE), whereas in purified rat ventricular myocytes, cGMP predominantly inhibits ICa via a mechanism involving cGMP-dependent protein kinase (cGMP-PK). Cyclic GMP 72-76 phosphodiesterase 2A Rattus norvegicus 132-139 8305078-11 1993 These studies demonstrate the presence of cyclic GMP-stimulated phosphodiesterase messenger RNA in specific regions of the rat brain, and suggest that the cyclic GMP-stimulated phosphodiesterase might modulate neuronal activity by regulating intracellular cyclic AMP levels in response to changes in intracellular cyclic GMP levels. Cyclic GMP 42-52 phosphodiesterase 2A Rattus norvegicus 155-194 1664725-8 1991 Biochemical characterization of the endogenous PDEs and cGMP-PK in purified cardiac myocytes provided further evidence in support of these mechanisms of cGMP action on ICa. Cyclic GMP 153-157 phosphodiesterase 2A Rattus norvegicus 47-51 35506379-3 2022 METHODS: Using a combination of single-cell RNA sequencing together with forster resonance energy transfer-based sensors to monitor cyclic adenosine 3",5"-monophosphate, PKA (protein kinase A)-dependent phosphorylation and cGMP (cyclic guanosine 3",5"-monophosphate), we tested the hypothesis that dysregulation occurs in a sub-family of PDEs in the cytosol and outer mitochondrial membrane of neurons from the stellate ganglion. Cyclic GMP 229-265 phosphodiesterase 2A Rattus norvegicus 338-342