Bibliographies thématiques / Adenosine receptors, A1, A2B

Littérature scientifique sur le sujet « Adenosine receptors, A1, A2B »

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Publié le 10 mars 2023

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Articles de revues sur le sujet "Adenosine receptors, A1, A2B"

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Dubey, Raghvendra K., Delbert G. Gillespie et Edwin K. Jackson. « A2B Adenosine Receptors Mediate the Anti-Mitogenic Effects of Adenosine in Cardiac Fibroblasts ». Hypertension 36, suppl_1 (octobre 2000) : 708. http://dx.doi.org/10.1161/hyp.36.suppl_1.708-b.

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P85 Adenosine inhibits growth of CFs; however, the adenosine receptor subtype that mediates this anti-mitogenic effect remains undefined. Using specific ADE receptor antagonists and agonists and antisense oligonucleotides (OLIGO) against A2B receptors, we investigated the role of A2B receptors in inhibiting cardiac fibroblast growth. PDGF (25ng/ml)-induced DNA synthesis, cell number and collagen synthesis in CFs were inhibited by A2 (chloroadenosine [Cl-Ad]and MECA), but not by A1 (CPA), A2a ( CGS21680 ) or A3 (AB-MECA),receptor agonists.The inhibitory effects of 1μM MECA and Cl-Ad were reversed by A1/A2 (DPSPX; 10nM), but not by A1 (DPCPX; 10nM), receptor antagonists. In CFs treated with antisense, but not sense or scrambled, OLIGOs to the A2B receptor, both basal and PDGF-induced DNA synthesis was enhanced by 70±4% and 64±5% respectively. Moreover, the inhibitory effects of Cl-Ad and MECA were completely abolished in CFs treated with antisense, but not sense and scrambled, OLIGOs. In conclusion, A2B receptors mediate the anti-mitogenic effects of adenosine suggesting that A2B receptors are importantly involved in the regulation of CF biology. Thus, A2B receptors may play a critical role in regulating cardiac remodeling associated with CF proliferation.
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Borgland, Stephanie L., Maria Castañón, Walter Spevak et Fiona E. Parkinson. « Effects of propentofylline on adenosine receptor activity in Chinese hamster ovary cell lines transfected with human A1, A2A, or A2B receptors and a luciferase reporter gene ». Canadian Journal of Physiology and Pharmacology 76, no 12 (1 décembre 1998) : 1132–38. http://dx.doi.org/10.1139/y98-143.

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Propentofylline is neuroprotective in vivo, but its mechanism of action is not completely understood. Previously, propentofylline was shown to block adenosine transport processes, to inhibit three adenosine receptor subtypes, and to inhibit cAMP phosphodiesterase. We tested the effect of propentofylline on adenosine receptor function in Chinese hamster ovary (CHO) cells transfected with human adenosine A1, A2A, or A2B receptors and a luciferase reporter gene under control of a promoter sequence containing several copies of the cAMP response element. We investigated the concentration-dependent inhibitory effects of propentofylline on cAMP phosphodiesterase, adenosine transport processes, and adenosine A1, A2A, and A2B receptors. At concentrations >= 1 mM, propentofylline increased luciferase activity probably as a result of inhibition of cAMP phosphodiesterase. Inhibition of [3H]adenosine uptake by propentofylline was concentration dependent, with IC50 values of 37-39 µM for the three cell types. Agonist-activated adenosine A1 receptors were antagonized by 100 µM propentofylline, but inhibition of agonist-stimulated A2A or A2B receptors was not observed. In contrast, A1 and A2A receptor mediated effects of adenosine were enhanced by propentofylline at concentrations of 1 and 100 µM, respectively. These data indicate that the net effects of propentofylline in vivo will be dependent on the concentrations of propentofylline and adenosine available and on the subtypes of adenosine receptors, phosphodiesterases, and nucleoside transporters present.Key words: adenosine receptors, nucleoside transport, propentofylline.
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Wolska, Nina, et Marcin Rozalski. « Blood Platelet Adenosine Receptors as Potential Targets for Anti-Platelet Therapy ». International Journal of Molecular Sciences 20, no 21 (3 novembre 2019) : 5475. http://dx.doi.org/10.3390/ijms20215475.

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Adenosine receptors are a subfamily of highly-conserved G-protein coupled receptors. They are found in the membranes of various human cells and play many physiological functions. Blood platelets express two (A2A and A2B) of the four known adenosine receptor subtypes (A1, A2A, A2B, and A3). Agonization of these receptors results in an enhanced intracellular cAMP and the inhibition of platelet activation and aggregation. Therefore, adenosine receptors A2A and A2B could be targets for anti-platelet therapy, especially under circumstances when classic therapy based on antagonizing the purinergic receptor P2Y12 is insufficient or problematic. Apart from adenosine, there is a group of synthetic, selective, longer-lasting agonists of A2A and A2B receptors reported in the literature. This group includes agonists with good selectivity for A2A or A2B receptors, as well as non-selective compounds that activate more than one type of adenosine receptor. Chemically, most A2A and A2B adenosine receptor agonists are adenosine analogues, with either adenine or ribose substituted by single or multiple foreign substituents. However, a group of non-adenosine derivative agonists has also been described. This review aims to systematically describe known agonists of A2A and A2B receptors and review the available literature data on their effects on platelet function.
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Feng, Ming-Guo, et L. Gabriel Navar. « Afferent arteriolar vasodilator effect of adenosine predominantly involves adenosine A2B receptor activation ». American Journal of Physiology-Renal Physiology 299, no 2 (août 2010) : F310—F315. http://dx.doi.org/10.1152/ajprenal.00149.2010.

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Adenosine is an important paracrine agent regulating renal vascular tone via adenosine A1 and A2 receptors. While A2B receptor message and protein have been localized to preglomerular vessels, functional evidence on the role of A2B receptors in mediating the vasodilator action of adenosine on afferent arterioles is not available. The present study determined the role of A2B receptors in mediating the afferent arteriolar dilation and compared the effects of A2B and A2A receptor blockade on afferent arterioles. We used the rat in vitro blood-perfused juxtamedullary nephron technique combined with videomicroscopy. Single afferent arterioles of Sprague-Dawley rats were visualized and superfused with solutions containing adenosine or adenosine A2 receptor agonist (CV-1808) along with adenosine A2B and A2A receptor blockers. Adenosine (10 μmol/l) caused modest constriction and subsequent superfusion with SCH-58261 (SCH), an A2A receptor blocker, at concentrations up 10 μmol/l elicited only slight additional decreases in afferent arteriolar diameter with maximum effect at a concentration of 1 μmol/l (−11.0 ± 2.5%, n = 6, P < 0.05). However, superfusion of adenosine-treated vessels with MRS-1754 (MRS), an A2B receptor blocker, elicited greater decreases in afferent arteriolar diameter (−26.0 ± 4.7%, n = 5, P < 0.01). SCH did not significantly augment the adenosine-mediated afferent constriction elicited by MRS; however, adding MRS after SCH caused further significant vasoconstriction. Superfusion with CV-1808 dilated afferent arterioles (17.2 ± 2.4%, n = 6, P < 0.01). This effect was markedly attenuated by MRS (−22.6 ± 2.0%, n = 5, P < 0.01) but only slightly reduced by SCH (−9.0 ± 1.1%, n = 5, P < 0.05) and completely prevented by adding MRS after SCH (−24.7 ± 1.8%, n = 5, P < 0.01). These results indicate that, while both A2A and A2B receptors are functionally expressed in juxtamedullary afferent arterioles, the powerful vasodilating action of adenosine predominantly involves A2B receptor activation, which counteracts A1 receptor-mediated vasoconstriction.
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Zhan, Enbo, Victoria J. McIntosh et Robert D. Lasley. « Adenosine A2A and A2B receptors are both required for adenosine A1 receptor-mediated cardioprotection ». American Journal of Physiology-Heart and Circulatory Physiology 301, no 3 (septembre 2011) : H1183—H1189. http://dx.doi.org/10.1152/ajpheart.00264.2011.

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All four adenosine receptor subtypes have been shown to play a role in cardioprotection, and there is evidence that all four subtypes may be expressed in cardiomyocytes. There is also increasing evidence that optimal adenosine cardioprotection requires the activation of more than one receptor subtype. The purpose of this study was to determine whether adenosine A2A and/or A2B receptors modulate adenosine A1 receptor-mediated cardioprotection. Isolated perfused hearts of wild-type (WT), A2A knockout (KO), and A2BKO mice, perfused at constant pressure and constant heart rate, underwent 30 min of global ischemia and 60 min of reperfusion. The adenosine A1 receptor agonist N6-cyclohexyladenosine (CHA; 200 nM) was administrated 10 min before ischemia and for the first 10 min of reperfusion. Treatment with CHA significantly improved postischemic left ventricular developed pressure (74 ± 4% vs. 44 ± 4% of preischemic left ventricular developed pressure at 60 min of reperfusion) and reduced infarct size (30 ± 2% with CHA vs. 52 ± 5% in control) in WT hearts, effects that were blocked by the A1 antagonist 8-cyclopentyl-1,3-dipropylxanthine (100 nM). Treatments with the A2A receptor agonist CGS-21680 (200 nM) and the A2B agonist BAY 60-6583 (200 nM) did not exert any beneficial effects. Deletion of adenosine A2A or A2B receptor subtypes did not alter ischemia-reperfusion injury, but CHA failed to exert a cardioprotective effect in hearts of mice from either KO group. These findings indicate that both adenosine A2A and A2B receptors are required for adenosine A1 receptor-mediated cardioprotection, implicating a role for interactions among receptor subtypes.
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Darlington, Daniel N., Xiaowu Wu, Kevin L. Chang, James Bynum et Andrew P. Cap. « Regulation of Platelet Function By Adenosine Receptors ». Blood 134, Supplement_1 (13 novembre 2019) : 2348. http://dx.doi.org/10.1182/blood-2019-131129.

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Introduction: We have recently shown that severe trauma and hemorrhage lead to inhibition of platelet aggregation and an elevation in cyclic adenosine monophosphate (cAMP). Adenosine is one of the few humoral agents known to stimulate cAMP in platelets. Because adenosine is released from damaged tissue, it may contribute to the platelet dysfunction seen after severe trauma. Platelets have four adenosine receptors (A1, A2a, A2b and A3). These receptors are G-Protein Coupled Receptors and have been proposed to stimulate adenylyl cyclase and increase intracellular cAMP. Although studies have shown that stimulate A2a can inhibit platelet aggregation and elevate cAMP, there is little data elucidating the function of the other receptors. Objective: Define which adenosine receptors affects platelet aggregation and cAMP production. Methods: Platelet-rich plasma (PRP) was isolated from whole blood of human volunteers, and centrifuged at 200g for 10min. Light transmission aggregometry was performed using a plate reader (Synergy Neo2 Multimode Reader, BioTek) with constant agitation. PRP was stimulated with adenosine diphosphate (ADP) with or without various adenosine agonists or antagonists, including the non-metabolizable adenosine agonist 5-(N-ethyl-carboxamido) adenosine (NECA), antagonists to receptors A1 (DPCPX), A2a (Sch 58261), A2b (GS 6201) and A3 (MRS 1220), or agonists for A2a (CGS 21680) A2b (BAY 60-6583) or agonist A1 (CCPA), A2a (CGS 21680), A2b (Bay 60-6583), A3 (2-Cl-IB-Meca). Cyclic AMP was extracted from 100ul of PRP after adding 1ml of EtOH, 10mM ammonium formate, with 10ug/ml cGMP-Br as an internal control. Samples were centrifuged at 20K g for 10min, and supernatant dried. Samples were brought up in 200ul of 0.1% formic acid for analysis by Reverse Phase liquid chromatography/ Tandem Mass Spectroscopy (Quantiva, ThrermoFisher). N-8/group. Results: Adenosine diphosphate (100uM) leads to platelet aggregation (change in mAbsorbance units, Table 1). The adenosine agonist NECA inhibited aggregation to ADP and elevated cAMP in a dose dependent manner (pg/ml per 1000 plt, Table 1). Platelet aggregation was inhibited and cAMP was elevated after stimulation with agonists for adenosine receptor A2a agonist, but not A1, A2b, or A3 (Table 2). Antagonists for A2a, but not A1, A2b, A3, blocked NECA inhibition of ADP aggregation (Table 3). Agonist for adenosine receptor A2a inhibited the ADP-induced aggregation and elevated cAMP in a dose response manner (Table 4). Discussion: Adenosine inhibits platelet aggregation to ADP. The mechanism appears to be due to elevation in intracellular cAMP, and works through the A2a receptor. These data suggest that the A2a receptor could be potential target for a resuscitation strategy that could attenuate or prevent platelet dysfunction after trauma by preventing stimulation of adenylate cyclase and synthesis of cAMP. This study was funded by the US Army medical Research and Development Command. Disclosures No relevant conflicts of interest to declare.
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Marquardt, D. L., L. L. Walker et S. Heinemann. « Cloning of two adenosine receptor subtypes from mouse bone marrow-derived mast cells. » Journal of Immunology 152, no 9 (1 mai 1994) : 4508–15. http://dx.doi.org/10.4049/jimmunol.152.9.4508.

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Abstract Adenosine potentiates the stimulated release of mast cell mediators. Pharmacologic studies suggest the presence of two adenosine receptors, one positively coupled to adenylate cyclase and the other coupled to phospholipase C activation. To identify mast cell adenosine receptor subtypes, cDNAs for the A1 and A2a adenosine receptors were obtained by screening a mouse brain cDNA library with the use of PCR-derived probes. Mouse bone marrow-derived mast cell cDNA libraries were constructed and screened with the use of A1 and A2a cDNA probes, which revealed the presence of A2a, but not A1, receptor clones. A putative A2b receptor was identified by using low stringency mast cell library screening. Northern blotting of mast cell poly(A)+ RNA with the use of receptor subtype probes labeled single mRNA bands of 2.4 kb and 1.8 kb for the A2a and A2b receptors, respectively. In situ cells. An A2a receptor-specific agonist failed to enhance mast cell mediator release, which suggests that the secretory process is modulated through the A2b and/or another receptor subtype. By using RNase protection assays, we found that mast cells that had been cultured in the presence of N-ethylcarboxamidoadenosine for 24 h exhibited a decrease in both A2a and A2b receptor RNA levels. Cells that had been cultured for 1 to 2 days in the presence of dexamethasone demonstrated increased amounts of A2a receptor mRNA, but no identifiable change in A2b receptor mRNA. Mast cells possess at least two adenosine receptor subtypes that may be differentially regulated.
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Rees, D. A., M. D. Lewis, B. M. Lewis, P. J. Smith, M. F. Scanlon et J. Ham. « Adenosine-Regulated Cell Proliferation in Pituitary Folliculostellate and Endocrine Cells : Differential Roles for the A1 and A2B Adenosine Receptors ». Endocrinology 143, no 6 (1 juin 2002) : 2427–36. http://dx.doi.org/10.1210/endo.143.6.8837.

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Abstract A1 and A2 adenosine receptors have been identified in the pituitary gland, but the cell type(s) on which they are located and their effects on pituitary cell growth are not known. Therefore, we analyzed the expression of A1 and A2 receptors in primary rat anterior pituitary cells, two pituitary folliculostellate (TtT/GF and Tpit/F1) and two pituitary endocrine (GH3 and AtT20) cell lines, and compared their effects on cell proliferation. In anterior pituitary and folliculostellate cells, adenosine and adenosine receptor agonists (5′-N-ethylcarboxamidoadenosine, a universal agonist, and CGS 21680, an A2A receptor agonist) stimulated cAMP levels with a rank order of potency that indicates the presence of functional A2B receptors. This stimulation, however, was not observed in either GH3 or AtT20 cells, where adenosine and the A1 receptor agonist 2-chloro-N6-cyclopentyladenosine inhibited VIP/forskolin-stimulated cAMP production. Expression of A2B and A1 receptors in the folliculostellate cells and that of the A1 receptor in the endocrine cells were confirmed by RT-PCR, immunocytochemistry, and ligand binding. Adenosine and 5′-N-ethylcarboxamidoadenosine dose-dependently (10 nm to 10 μm) stimulated growth in the folliculostellate, but not in the endocrine, cells, whereas in the latter, 100 μm adenosine and 2-chloro-N6-cyclopentyladenosine inhibited cell proliferation by slowing cell cycle progression. These data highlight the differential expression of A1 and A2B adenosine receptors in pituitary cells and provide evidence for opposing effects of adenosine on pituitary folliculostellate and endocrine cell growth.
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Kreisberg, M. S., E. P. Silldorff et T. L. Pallone. « Localization of adenosine-receptor subtype mRNA in rat outer medullary descending vasa recta by RT-PCR ». American Journal of Physiology-Heart and Circulatory Physiology 272, no 3 (1 mars 1997) : H1231—H1238. http://dx.doi.org/10.1152/ajpheart.1997.272.3.h1231.

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Adenosine has a multitude of functions in the kidney, including vasoregulation of the renal vasculature. The actions of adenosine are mediated by its binding to specific receptors. Four adenosine-receptor subtypes have been cloned and sequenced, the A1, A2a, A2b, and the A3. In this study, the expression of individual adenosine-receptor subtype RNAs in outer medullary descending vasa recta (OMDVR) was investigated. Total RNA isolated from the outer medulla and microdissected, permeabilized OMDVR were subjected to reverse transcription-polymerase chain reaction (RT-PCR) with primers specific for each of the adenosine-receptor subtypes. Subtype-specific probes were used to verify the PCR products by Southern hybridization. Our studies, performed in triplicate on five different rats, indicate the presence of A1, A2a, and A2b adenosine-receptor subtype mRNAs. These products were not attributable to extraneous RNA contamination from other tissue sources, nor did they result from genomic DNA amplification. These data are consistent with pharmacological evaluations, favor A1, A2a, and A2b adenosine-receptor subtype expression in OMDVR, and support a role for adenosine in the regulation of medullary blood flow.
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Gebremedhin, Debebe, Brian Weinberger, David Lourim et David R. Harder. « Adenosine Can Mediate its Actions through Generation of Reactive Oxygen Species ». Journal of Cerebral Blood Flow & ; Metabolism 30, no 10 (9 juin 2010) : 1777–90. http://dx.doi.org/10.1038/jcbfm.2010.70.

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Adenosine is an important cerebral vasodilator, but mediating mechanisms are not understood. We investigated the expression of adenosine receptor subtypes in isolated cerebral arterial muscle cells (CAMCs), and their role in adenosine-induced superoxide (O2−) generation and reduction in cerebral arterial tone. Reverse transcriptase-PCR, western blotting, and immunofluorescence studies have shown that CAMCs express transcript and protein for A1, A2A, A2B, and A3 adenosine receptors. Stimulation of CAMCs with adenosine or the A2A agonist CGS-21680 increased the generation of O2− that was attenuated by the inhibition of A2A and A2B adenosine receptor subtypes, or by the peptide inhibitor of nicotinamide adenine dinucleotide phosphate (NADPH)-oxidase gp91ds-tat, or by the mitochondria uncoupler 2,4-dinitrophenol. Application of adenosine or CGS-21680 dilated pressure-constricted cerebral arterial segments that were prevented by the antioxidants superoxide dismutase (SOD) conjugated to polyethylene glycol (PEG) and PEG-catalase or by the A2B adenosine receptor antagonist MRS-1754, or by the mixed A2A and A2B antagonist ZM-241385. Antagonism of the A2A and A2B adenosine receptors had no effect on cerebral vasodilatation induced by nifedipine. These findings indicate that adenosine reduces pressure-induced cerebral arterial tone through stimulation of A2A and A2B adenosine receptors and generation of O2− from NADPH oxidase and mitochondrial sources. This signaling pathway could be one of the mediators of the cerebral vasodilatory actions of adenosine.
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Thèses sur le sujet "Adenosine receptors, A1, A2B"

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Halldner, Henriksson Linda. « Physiology and pathophysiology of central adenosine A1 and A2A receptors / ». Stockholm, 2003. http://diss.kib.ki.se/2003/91-628-5732-0/.

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BANGALORE, REVANNA CHANDRASHEKAR. « Ischemia/Reperfusion injury on mice steatotic Hapatocites and differential effect of adenosine A2A and A1 receptors stimulation ». Doctoral thesis, Università del Piemonte Orientale, 2016. http://hdl.handle.net/11579/115194.

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Stumpf, Anette D. [Verfasser], et Carsten [Gutachter] Hoffmann. « Development of fluorescent FRET receptor sensors for investigation of conformational changes in adenosine A1 and A2A receptors / Anette D. Stumpf. Gutachter : Carsten Hoffmann ». Würzburg : Universität Würzburg, 2016. http://d-nb.info/1111887357/34.

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Tikh, Eugene I. « Regulation of Contractility by Adenosine A1 and A2A Receptors in the Murine Heart : Role of Protein Phosphatase 2A : A Dissertation ». eScholarship@UMMS, 2006. https://escholarship.umassmed.edu/gsbs_diss/130.

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Adenosine is a nucleoside that plays an important role in the regulation of contractility in the heart. Adenosine receptors are G-protein coupled and those implicated in regulation of contractility are presumed to act via modulating the activity of adenylyl cyclase and cAMP content of cardiomyocytes. Adenosine A1 receptors (A1R) reduce the contractile response of the myocardium to β-adrenergic stimulation. This is known as anti adrenergic action. The A2A adenosine receptor (A2AR) has the opposite effect of increasing contractile responsiveness of the myocardium. The A2AR also appears to attenuate the effects of A1R. The effects of these receptors have been primarily studied in the rat heart and with the utilization of cardiomyocyte preparations. With the increasing use of receptor knockout murine models and murine models of various pathological states, it is of importance to comprehensively study the effects of adenosine receptors on regulation of contractility in the murine heart. The following studies examine the adenosinergic regulation of myocardial contractility in isolated murine hearts. In addition, adenosinergic control of contractility is examined in hearts isolated from A2AR knockout animals. Responses to adenosinergic stimulation in murine isolated hearts are found to be comparable to those observed in the rat, with A1R exhibiting an anti adrenergic action and A2AR conversely enhancing contractility. A significant part of the A2AR effect was found to occur via inhibition of the A1R antiadrenergic action. A part of the anti adrenergic action of A1R has previously been shown to be the result of protein phosphatase 2A activation and localization to membranes. Additional experiments in the present study examine the effect of adenosinergic signaling on PP2A in myocardial extracts from wild type and A2AR knockout hearts. A2AR activation was found to decrease the activity of PP2A and enhance localization of the active enzyme to the cytosol; away from its presumed sites of action. In the A2AR knockout the response to A1R activation was enhanced compared with the wild type and basal PP2A activity was reduced. It is concluded that A2AR modulation of PP2A activity may account for the attenuation of the A1R effect by A2AR observed in the contractile studies.
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Pagnussat, Natália. « O envolvimento dos receptores de adenosina A1 e A2A na memória em camundongos machos adultos ». reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2015. http://hdl.handle.net/10183/131897.

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A cafeína é o psicoestimulante mais consumido mundialmente. Sua ação farmacológica consiste em bloquear os receptores de adenosina A1 e A2A. A administração crônica de cafeína previne déficits cognitivos decorrentes da idade e em modelos experimentais da doença de Alzheimer. Esses efeitos preventivos são também observados pela administração do antagonista seletivo do receptor de adenosina A2A. Nesse trabalho investigou-se a participação dos receptores de adenosina A1 e A2A na prevenção dos déficits cognitivos induzidos por escopolamina. Também foi investigado se a manipulação dos receptores A2A teria algum impacto na memória em camundongos naive. Para isso, foram utilizadas três tarefas comportamentais que avaliaram três tipos de memória: a tarefa de reconhecimento de objetos (RO), a esquiva inibitória (EI) e o labirinto em Y. A administração intraperitoneal de escopolamina (1,0 mg/kg) prejudicou o desempenho da memória de curto prazo nas três tarefas utilizadas. O antagonista de receptores A1 (DPCPX, 1,0 mg / kg, i.p.) preveniu a amnésia induzida por escopolamina no RO e na EI, enquanto o antagonista de receptores A2A (SCH 58261, 0,5 mg / kg, i.p.) preveniu a amnésia em todos os testes. Além disso, ambos os antagonistas não apresentaram efeitos sobre a memória ou a locomoção em animais naive. Também foi observado que a ativação dos receptores A2A, a partir da administração de CGS 21680 (0,1 mg/kg, i.p.) antes da sessão de treino, foi suficiente para provocar prejuízos na memória em animais naive também nas três tarefas, e este efeito foi prevenido por meio da administração de SCH 58261 (0,5 mg/kg, i.p.). Por fim, a administração intracerebroventricular (i.c.v) de CGS 21680 (50 nmol) também prejudicou o desempenho dos animais na tarefa de RO. Em conjunto, estes resultados sugerem que a ativação dos receptores A2A é suficiente para provocar déficits de memória e ainda sugerem que os receptores A1 também participam de maneira seletiva no controle dos déficits de memória relacionados ao sistema colinérgico.
Caffeine, a non-selective adenosine receptor antagonist, prevents memory deficits, an effect mimicked by adenosine A2A receptor (A2AR), but not receptor A1 (A1R), antagonists upon aging and Alzheimer´s disease. We tested if A2AR were also necessary for the memory impairment upon direct perturbation of the cholinergic system with scopolamine and if A2AR activation was sufficient to trigger memory deficits in naive mice using 3 tests, to probe for short-term memory, namely the object recognition task, inhibitory avoidance and modified Y-maze. The intra-peritoneal (i.p.) administration of scopolamine (1.0 mg/kg) impaired short-term memory performance in 3 tests, namely the object recognition task, inhibitory avoidance and modified Y-maze. The scopolamine-induced amnesia was prevented by the A2AR (SCH 58261, 0.5 mg/kg, i.p.) as well as by A1R antagonist (DPCPX, 1 mg/kg, i.p.) in all tests, except for the modified Y-maze, and both antagonists were devoid of effects on memory or locomotion in naive rats. Notably, the activation of A2AR with CGS 21680 (0.1 mg/kg, i.p.) before the training session was sufficient to trigger memory impairment in the 3 tests in naive mice, and effect prevented by SCH 58261 (0.5 mg/kg, i.p.). Furthermore, the intracerebroventricular administration of CGS 21680 (50 nmol) also impaired recognition memory in the object recognition task. These results show that A2AR are necessary and sufficient to trigger memory impairment and they further suggest that A1R might also be selectively engaged to control the cholinergic driven memory impairment.
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Sorrentino, Claudia. « Role of CD73 - A2A/A2B receptors axis in cancer ». Doctoral thesis, Universita degli studi di Salerno, 2018. http://hdl.handle.net/10556/3116.

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2016 - 2017
The adenosinergic pathway plays a critical role in cancer development and progression, as well as in drug resistance to chemotherapy and/or targeted-therapy. The goal of this PhD thesis was to investigate and fully characterize the role of CD73/adenosine A2A-A2B receptors axis in cancer, highlighting the therapeutic potential of inhibitors of the adenosinergic pathway. We firstly characterized the mechanism/s by which A2BR promotes immunosuppression and angiogenesis in tumor-bearing hosts, focusing on the role of myeloid-derived suppressor cells (MDSCs) and cancer-associated fibroblasts (CAFs). The results revealed that treatment of melanoma-bearing mice with Bay60-6583, a selective A2BR agonist, is associated with 1. increased tumor VEGF-A expression and vessel density, and 2. increased accumulation of tumor-infiltrating CD11b+Gr1+cells (MDSCs). MDSCs strongly contribute to the immunosuppressive and angiogenic effects of Bay60-6583. Melanoma-bearing mice treated with a selective A2BR antagonist PSB1115 showed reduced tumor growth compared to controls and this effect was associated with reduced tumor angiogenesis, low levels of MDSCs and increased number of tumor-infiltrating CD8+ T cells. Furthermore, blockade of A2BR increased the anti-tumor effects of VEGF-A inhibitors. Next, we verified that A2BR activation also drives fibroblasts activation within melanoma tissues, by increasing the number of FAP positive cells within tumor lesions. FAP is a common marker of activated fibroblasts also named cancer-associated fibroblasts. These cells produce and secrete various tumor-promoting factors, including fibroblast growth factor (FGF)-2 and CXCL12 or stromal-derived factor 1 α (SDF1α), that were increased both in melanoma tissue and fibroblasts isolated from melanoma tissue or from skin upon Bay60-6583 treatment. Bay60-6583-induced FGF-2 from fibroblasts contributed to melanoma cells proliferation. The CXCL12/CXCR4 pathway, instead, was involved in the pro-angiogenic effects of A2BR agonist, but not in its immunosuppressive effects. These effects were significantly blocked by the A2BR antagonists PSB1115. Taken together, these data elucidate the pivotal role of A2BR in establishing a positive cross-talk between tumor-infiltrating immune cells, fibroblasts and endothelial cells that sustain tumor growth, reinforcing the therapeutic potential of A2BR blockers for cancer therapy. ... [edited by Author]
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Hamil, Nicola Elizabeth. « The neuromodulatory role of adenosine A1 receptors in status epilepticus ». Thesis, St George's, University of London, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.526032.

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Wu, Weiping. « The role of adenosine and its receptor subtypes in nociception and neuropathic pain / ». Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-298-5/.

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Finlayson, Keith. « Pharmacology and modulation of adenosine A1 receptors in the mammalian central nervous system ». Thesis, University of Edinburgh, 1998. http://hdl.handle.net/1842/21241.

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Adenosine receptors are members of the G protein coupled receptor (GPCR) superfamily. Neurochemical and electrophysiological experiments point to a neuromodulatory role for adenosine. Adenosine inhibits the release of several neurotransmitters in brain by pre- and postsynaptic actions at adenosine A1 receptors. In this thesis the pharmacology and modulation of adenosine A1 receptors in the central nervous system (CNS) of different species was characterised. Rat renal adenosine A1 receptors were also studied. In addition the central penetration by adenosine A1 receptor antagonists following peripheral administration was investigated. An in vitro [3H]DPCPX ligand binding assay utilising a range of receptor agonists and antagonists, were used to compare the pharmacology of rat, mouse, guinea pig and human adenosine A1 receptors. Standard xanthine-based adenosine antagonists had 10-fold lower affinity in human and guinea pig in comparison with rat and mouse. Several novel nonxanthine A1 antagonists from the Fujisawa Pharmaceutical Co. Ltd., retained high affinity for adenosine A1 receptors in all species, including human. Modulation of ligand binding to adenosine A1 and A2a receptors by Gpp(NH)p and magnesium was examined. In common with other GPCRs, agonists bind to high and low affinity states, with the equilibrium modified by GTP analogues and magnesium, whereas effects on antagonist affinity are minimal. Agonist radioligands under the conditions used labelled predominantly the high affinity state of adenosine A1 and A2a receptors. Gpp(NH)p and magnesium have essentially inverse effects on radioligand (agonists and antagonists) binding to both adenosine A1 and A2a receptors. In addition their effects on [3H]agonist and [3H]antagonist binding are generally opposite, which is consistent with effects observed for other GPCRs. To act centrally, compounds must cross the blood brain barrier (BBB). A modified radioreceptor assay, involving a denaturation step to overcome the lipophilic nature of adenosine A1 receptor antagonists was developed. This assay accurately measures the central penetration of adenosine A1 receptor antagonists. Adenosine A1 antagonists administered peripherally at equipotent behavioural doses, were found to be present in brain, at concentrations between 50-500 fold greater than in vitro Ki values for adenosine A1 receptors. In addition, there was an excellent association between antagonist affinity in vitro and antagonist brain concentrations at the equipotent behavioural dose. Adenosine and its receptors are widely distributed throughout the body. It is important to determine if peripheral adenosine A1 receptors are identical to those in the CNS. Renal adenosine A1 receptors were examined using radioligand binding, in vitro autoradiography and in situ hybridisation. Even using this combined approach, identification of adenosine A1 receptors in rat kidney was not possible. Alzheimer's disease involves a myriad of neurochemical changes and neurotransmitter deficits. By antagonising the actions of endogenous adenosine, A1 receptor antagonists could compensate for some of these deficits, by enhancing synaptic facilitation and increasing neurotransmitter release. Analogues of FK453, a non-xanthine adenosine A1 antagonist, which are BBB permeable and potent and selective for human adenosine A1 receptors, could prove to be clinically useful compounds, by enhancing cognition, in conditions such as Alzheimer's disease.
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Murphy, Cody. « Transregulation of Cardiac Ischaemic Tolerance and Stress Kinase Signalling by A1 Adenosine and ¿-Opioid Receptors ». Thesis, Griffith University, 2018. http://hdl.handle.net/10072/382690.

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Protecting hearts from damage sustained during myocardial ischaemia and reperfusion remains an ongoing challenge. Despite successful findings with animal models, the task of trialling and effectively translating experimental findings from laboratory to patients has proven difficult, therefore treatments and clinical therapies are still urgently needed to protect the heart and improve cardiac functional outcome. Previous research has implicated adenosine and opioid receptor participation in the protective response preceding or following myocardial infarction, with evidence of potential cross-talk between receptors. This project aimed to investigate whether A1 adenosine (A1AR) and δ-opioid receptor (δ-OR) dependent cytoprotection and prosurvival kinase activation in murine hearts share common dependencies on „cross-talk‟ between both G-protein coupled receptor (GPCR) sub-types and whether these responses involve a common Matrix Metalloproteinase (MMP) and Epidermal Growth Factor Receptor (EGFR) dependent signalling pathway. This was achieved via four inter-related in vitro studies. Study 1: Healthy mouse hearts were cannulated in a Langendorff mode enabling the coronary circulation to be perfused. Hearts were subjected to 25 minutes of global (zero-flow) ischaemia followed by 45 minutes of aerobic reperfusion. The groups investigated included untreated control hearts, hearts receiving the selective A1AR agonist CCPA (± DPCPX, a selective A1AR antagonist, or BNTX, a selective δ-OR antagonist) and hearts receiving the selective δ-OR agonist BW373U86 (± DPCPX, a selective A1AR antagonist, or BNTX, a selective δ-OR antagonist). Agonists were applied 5 minutes pre-ischaemia and the antagonists were administered 10 minutes prior to agonist treatment. Cardiac functional outcomes were assessed via changes in coronary flow, left ventricular (LV) end diastolic pressure and pressure development, and ±dP/dt (± differentials of pressure change with time – indexing lusitropic and inotropic state). Cell death outcomes were also assessed via lactate dehydrogenase (LDH) release. Treatment with either the selective A1AR agonist CCPA, or the selective δ-OR agonist BW373U86, significantly reduced (p≤0.0001 vs. CTRL) LV end-diastolic pressure following ischaemia/reperfusion. Recovery of LV developed pressure (LVDP) was significantly increased following A1AR activation via CCPA (p≤0.0001 vs. CTRL) or δ-OR activation via BW373U86 (p≤0.001 vs. CTRL). Ventricular contractility (+dP/dt) and relaxation (-dP/dt) were also significantly improved with both CCPA (p≤0.0001 vs. CTRL, p≤0.01 vs. CTRL) and BW373U86 (p≤0.001 vs. CTRL, p≤0.001 vs. CTRL). Treatment with CCPA, but not BW373U86, significantly improved the recovery of coronary flow rate at the termination of reperfusion (p≤0.01 vs. CTRL). LDH release (corresponding to cell death) was significantly reduced by both CCPA and BW373U86 (p<0.05 vs. CTRL, p<0.05 vs. CTRL). A1AR or δ-OR inhibition, via the selective antagonists DPCPX and BNTX respectively (applied alone), did not significantly affect the recovery of functional outcomes or cell death relative to control. These results show that cardioprotection against ischaemic injury is induced with activation of A1ARs and δ-ORs, and that endogenous levels of receptor agonists may not be sufficient to induce this response. Protection with CCPA was abolished via cotreatment with either the selective A1AR antagonist DPCPX or the selective δ-OR antagonist BNTX. Conversely protection with BW373U86 administration was negated by co-treatment with either BNTX or DPCPX. This reveals that A1AR dependent cardioprotection is reliant on the activation of δ-ORs, and δ-OR mediated protection is dependent on A1AR activity, confirming essential cross-talk. Study 2: Perfused hearts from study 1 were snap-frozen in liquid nitrogen following the termination of reperfusion. Hearts were homogenised and fractioned to yield cytosolic proteins. Total and phosphorylated levels of Erk1/2 and Akt were subsequently assessed via western immunoblot. Both A1AR and δ-OR stimulation via CCPA and BW373U86 (respectively) did not significantly influence Erk1/2 phosphorylation. Akt phosphorylation, on the other hand, was increased by both CCPA and BW373U86; although only the latter effect achieved statistical significance (p<0.01 vs. CTRL). The A1AR antagonist DPCPX had minimal effect on Erk1/2 and Akt phosphorylation when applied alone. Alternatively inhibition of the δ-OR via BNTX, applied alone, was found to increase both Akt and Erk1/2 phosphorylation, a response in conflict with the existing literature. Co-treatment with the A1AR antagonist DPCPX or the δ-OR antagonist BNTX did not significantly influence Erk1/2 signalling compared to controls. Alternatively Akt phosphorylation was reduced by ~50% relative to control when hearts were co-treated with DPCPX or BNTX applied in conjunction with either the A1AR agonist CCPA or the δ-OR agonist BW373U86. These results imply that both A1ARs and δ-ORs together are necessary to induce protective Akt signalling during ischaemia/reperfusion with either receptor agonist. Study 3: To assess the roles of EGFRs and MMPs in A1AR and δ-OR responses, agonist studies with CCPA and BW373U86 were repeated with co-treatment with the EGFR antagonist AG1478 or the MMP inhibitor GM6001. Functional and cytoprotective outcomes were assessed in perfused hearts subjected to ischaemiareperfusion. The protective response observed with either A1AR and δ-OR stimulation was negated via co-treatment with either AG1478 or GM6001. A1AR and δ-OR dependent recovery of end diastolic pressure, LV developed pressure, +dP/dt and -dP/dt were all repressed via EGFR or MMP inhibition. Moreover, the cytoprotective response conferred by δ-OR activation was completely abolished via co-treatment with AG1478 or GM6001, providing evidence that adenosinergic and opioidergic protection within the myocardium involves an EGFR and MMP dependent pathway. Study 4: Western blot analysis was used to assess changes in Erk1/2 and Akt expression and phospho-regulation in hearts treated with CCPA or BW373U86 in the presence of AG1478 or GM6001. Due to time constraints, data collected previously in our lab was used in this research; therefore the effect of EGFR and MMP inhibition on A1AR dependent Erk1/2 and Akt signalling was assessed in whole heart rather than cytosolic fractions. In these hearts, administration of CCPA significantly elevated both Erk1/2 and Akt phosphorylation, a response negated via co-treatment with either AG1478 or GM6001 (p≤ 0.05 vs. CCPA). Infusion of the selective δ-OR agonist BW373U86 did not significantly alter Erk/1/2 expression or phosphorylation in cytosolic fractions. Despite this, co-treatment with AG1478 reduced Erk1/2 phosphorylation by ~50% compared to the agonist alone (p ≤ 0.05 vs. BW373U86), suggesting an EGFR dependent mechanism. Surprisingly co-treatment with GM6001 did not significantly influence δ-OR mediated Erk1/2 activity. Akt phosphorylation was increased by more than 60% with BW373U86 (p≤0.05 vs. CTRL) and this response was abolished via treatment with the selective EGFR antagonist AG1478 or the selective MMP inhibitor GM6001. This provides further evidence that adenosinergic and opioidergic protective signalling during ischaemia-reperfusion requires the activity of EGFRs and MMPs. Conclusions: As a whole, the present study confirms an essential interaction between ARs and ORs in the heart, with kinase signalling and tissue protection via either A1ARs or -ORs exhibiting common and essential dependencies on activity of both receptors. The basis of this intriguing response remains unclear, although we show that both receptors engage distal kinases (and cardioprotection) in an MMP/EGFR dependent manner, adding an additional level to this novel cross-talk. This research provides further insight into cardioprotective receptor interactions in the heart, potentially leading to the development of new pharmacotherapeutics and improved outcomes for cardiovascular disease patients. Further research is needed to clarify the mechanism behind adenosinergic and opioidergic cross-talk and cardioprotection, potentially exploring membrane signalling, temporal expression of kinases, existence of A1AR/δ-OR dimers/oligomers, and concepts such as dual agonism and potential signalling thresholds for protection.
Thesis (Masters)
Master of Medical Research (MMedRes)
School of Medical Science
Griffith Health
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Livres sur le sujet "Adenosine receptors, A1, A2B"

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Blythe, Louise Jane. Analysis of presynaptic metabotropic glutamate and adenosine A1 receptors. Ottawa : National Library of Canada, 1998.

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Chapitres de livres sur le sujet "Adenosine receptors, A1, A2B"

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IJzerman, Ad P., Nora M. van der Wenden, Philip J. M. van Galen et Ken A. Jacobson. « Molecular Modeling of Adenosine A1 and A2a Receptors ». Dans Adenosine and Adenine Nucleotides : From Molecular Biology to Integrative Physiology, 27–37. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2011-5_4.

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Müller, Christa E., Younis Baqi, Sonja Hinz et Vigneshwaran Namasivayam. « Medicinal Chemistry of A2B Adenosine Receptors ». Dans The Adenosine Receptors, 137–68. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-90808-3_6.

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Scherrmann, Jean-Michel, Kim Wolff, Christine A. Franco, Marc N. Potenza, Tayfun Uzbay, Lisiane Bizarro, David C. S. Roberts et al. « Adenosine A1 Receptors ». Dans Encyclopedia of Psychopharmacology, 28–29. Berlin, Heidelberg : Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-68706-1_1102.

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Trivedi, Bharat K., Alexander J. Bridges et Robert F. Bruns. « Structure-Activity Relationships of Adenosine A1 and A2 Receptors ». Dans Adenosine and Adenosine Receptors, 57–103. Totowa, NJ : Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-4504-9_3.

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Kalla, Rao V., Jeff Zablocki, Mojgan Aghazadeh Tabrizi et Pier Giovanni Baraldi. « Recent Developments in A2B Adenosine Receptor Ligands ». Dans Adenosine Receptors in Health and Disease, 99–122. Berlin, Heidelberg : Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-89615-9_4.

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Gao, Zhan-Guo, Dilip K. Tosh, Shanu Jain, Jinha Yu, Rama R. Suresh et Kenneth A. Jacobson. « A1 Adenosine Receptor Agonists, Antagonists, and Allosteric Modulators ». Dans The Adenosine Receptors, 59–89. Cham : Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-90808-3_4.

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Hoppe, Edmund, et Martin J. Lohse. « Desensitization of A1 Adenosine Receptors ». Dans Adenosine and Adenine Nucleotides : From Molecular Biology to Integrative Physiology, 133–38. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2011-5_16.

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Martini, C., L. Trincavelli, M. Fiorini, F. Salvetti, U. Montali, A. Falleni, V. Gremigni et A. Lucacchini. « A1 Adenosine Receptors in Human Neutrophils ». Dans Advances in Experimental Medicine and Biology, 107–11. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5381-6_21.

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Kiesman, William F., Elfatih Elzein et Jeff Zablocki. « A1 Adenosine Receptor Antagonists, Agonists, and Allosteric Enhancers ». Dans Adenosine Receptors in Health and Disease, 25–58. Berlin, Heidelberg : Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-89615-9_2.

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Dhalla, Arvinder K., Jeffrey W. Chisholm, Gerald M. Reaven et Luiz Belardinelli. « A1 Adenosine Receptor : Role in Diabetes and Obesity ». Dans Adenosine Receptors in Health and Disease, 271–95. Berlin, Heidelberg : Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-89615-9_9.

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Actes de conférences sur le sujet "Adenosine receptors, A1, A2B"

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Lin, Juqiang, Yating Lin, Yiming Huang, Zhiwei Wu, Jianshu Xu, Ya Hu et Shusen Xie. « Quantitative FRET measurement of the interaction of A1 adenosine receptors and A2A adenosine receptors in living cell ». Dans Optics in Health Care and Biomedical Optics VIII, sous la direction de Qingming Luo, Xingde Li, Yuguo Tang et Ying Gu. SPIE, 2018. http://dx.doi.org/10.1117/12.2500692.

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Jang, Sunyoung, Seunah Jun, Hosun Lee, Yongtaek Lee, Joo-Yun Byun, Junghwa Park, Yu-Yon Kim, Young Gil Ahn, YoungHoon Kim et Kwee Hyun Suh. « Abstract 1704 : Discovery and characterization of a novel triple A1/A2a/A2b adenosine receptor antagonist for cancer immunotherapy ». Dans Proceedings : AACR Annual Meeting 2021 ; April 10-15, 2021 and May 17-21, 2021 ; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1704.

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Umapathy, Nagavedi S., Elzbieta Kaczmarek, Rudolf Lucas, Kurt Stenmark, Alexander D. Verin et Evgenia Gerasimovskaya. « Adenosine A1 Receptors Mediated Enhancement Of Barrier Function In Vasa Vasorum Endothelial Cells ». Dans American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1872.

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Gerasimovskaya, E. V., V. Karoor, D. Strassheim, R. Batori, A. Kovacs-Kasa, T. Sullivan, R. Moldovan, D. Klemm, A. Verin et K. R. Stenmark. « HDAC Inhibitor Butyrate Cooperates with A1 and A2B Receptors to Attenuate Pulmonary Artery Vasa Vasorum Dysfunction in Hypoxia ». Dans American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6365.

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Abd. Aziz, N. A. W., R. Agarwal, A. Abd Latiff et N. M. Ismail. « RESVERATROL AS A POTENTIAL AGENT FOR NEUROPROTECTION AGAINST INTRACEREBRAL HEMORRHAGE : INSIGHT ON THE ROLE OF ADENOSINE A1 RECEPTORS ». Dans MedChem-Russia 2021. 5-я Российская конференция по медицинской химии с международным участием «МедХим-Россия 2021». Издательство Волгоградского государственного медицинского университета, 2021. http://dx.doi.org/10.19163/medchemrussia2021-2021-88.

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