Journal articles: 'Adenosine deaminase'

1

Roth, E. Jr, N. Ogasawara, and S. Schulman. "The deamination of adenosine and adenosine monophosphate in Plasmodium falciparum-infected human erythrocytes: in vitro use of 2'deoxycoformycin and AMP deaminase-deficient red cells." Blood 74, no. 3 (August 15, 1989): 1121–25. http://dx.doi.org/10.1182/blood.v74.3.1121.1121.

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Abstract The role of enzymatic deamination of adenosine monophosphate (AMP) and adenosine in the in vitro growth of the malaria parasite Plasmodium falciparum was investigated by means of human red cells deficient in AMP deaminase to which the adenosine deaminase inhibitor 2′- deoxycoformycin was added. Malaria parasites grew normally in red cells lacking one or both of these enzyme activities. As a further probe of adenosine triphosphate (ATP) catabolism, both infected and uninfected RBCs were incubated with NaF (with and without 2′-deoxycoformycin) and the purine nucleotide/nucleoside content was analyzed by high- performance liquid chromatography (HPLC). Uninfected RBCs lacking either AMP or adenosine deaminase were able to bypass the enzyme block and degrade ATP to hypoxanthine. Uninfected RBCs with both deaminases blocked were unable to produce significant quantities of hypoxanthine. On the other hand, infected RBCs were able to bypass blockade of both deaminases and produce hypoxanthine and adenosine. These findings establish that deamination of adenosine and/or AMP are not essential for plasmodial growth. However, further work will be required to elucidate the pathways that permit the parasites to bypass these catabolic steps.

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Roth, E. Jr, N. Ogasawara, and S. Schulman. "The deamination of adenosine and adenosine monophosphate in Plasmodium falciparum-infected human erythrocytes: in vitro use of 2'deoxycoformycin and AMP deaminase-deficient red cells." Blood 74, no. 3 (August 15, 1989): 1121–25. http://dx.doi.org/10.1182/blood.v74.3.1121.bloodjournal7431121.

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The role of enzymatic deamination of adenosine monophosphate (AMP) and adenosine in the in vitro growth of the malaria parasite Plasmodium falciparum was investigated by means of human red cells deficient in AMP deaminase to which the adenosine deaminase inhibitor 2′- deoxycoformycin was added. Malaria parasites grew normally in red cells lacking one or both of these enzyme activities. As a further probe of adenosine triphosphate (ATP) catabolism, both infected and uninfected RBCs were incubated with NaF (with and without 2′-deoxycoformycin) and the purine nucleotide/nucleoside content was analyzed by high- performance liquid chromatography (HPLC). Uninfected RBCs lacking either AMP or adenosine deaminase were able to bypass the enzyme block and degrade ATP to hypoxanthine. Uninfected RBCs with both deaminases blocked were unable to produce significant quantities of hypoxanthine. On the other hand, infected RBCs were able to bypass blockade of both deaminases and produce hypoxanthine and adenosine. These findings establish that deamination of adenosine and/or AMP are not essential for plasmodial growth. However, further work will be required to elucidate the pathways that permit the parasites to bypass these catabolic steps.

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Keegan, Liam P., André P. Gerber, Jim Brindle, Ronny Leemans, Angela Gallo, Walter Keller, and Mary A. O'Connell. "The Properties of a tRNA-Specific Adenosine Deaminase from Drosophila melanogaster Support an Evolutionary Link between Pre-mRNA Editing and tRNA Modification." Molecular and Cellular Biology 20, no. 3 (February 1, 2000): 825–33. http://dx.doi.org/10.1128/mcb.20.3.825-833.2000.

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ABSTRACT Pre-mRNA editing involving the conversion of adenosine to inosine is mediated by adenosine deaminases that act on RNA (ADAR1 and ADAR2). ADARs contain multiple double-stranded RNA(dsRNA)-binding domains in addition to an adenosine deaminase domain. An adenosine deaminase acting on tRNAs, scTad1p (also known as scADAT1), cloned fromSaccharomyces cerevisiae has a deaminase domain related to the ADARs but lacks dsRNA-binding domains. We have identified a gene homologous to scADAT1 in the region of Drosophila melanogaster Adh chromosome II. Recombinant Drosophila ADAT1 (dADAT1) has been expressed in the yeast Pichia pastorisand purified. The enzyme has no activity on dsRNA substrates but is a tRNA deaminase with specificity for adenosine 37 of insect alanine tRNA. dADAT1 shows greater similarity to vertebrate ADARs than to yeast Tad1p, supporting the hypothesis of a common evolutionary origin for ADARs and ADATs. dAdat1 transcripts are maternally supplied in the egg. Zygotic expression is widespread initially and later concentrates in the central nervous system.

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Zhu, Q., G. P. Matherne, R. R. Curnish, C. G. Tribble, and R. M. Berne. "Effect of adenosine deaminase on cardiac interstitial adenosine." American Journal of Physiology-Heart and Circulatory Physiology 263, no. 4 (October 1, 1992): H1322—H1326. http://dx.doi.org/10.1152/ajpheart.1992.263.4.h1322.

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Adenosine deaminase was infused into isolated perfused guinea pig hearts to determine its effect on myocardial adenosine levels. The enzyme was administered during constant coronary flow perfusion at 6.11 +/- 0.36 ml.min-1.g-1. Venous adenosine was measured in samples of pulmonary artery effluent; epicardial and endocardial adenosine were measured with the porous nylon disk technique. Infusion of adenosine deaminase at 2.4 and 4.8 U/ml produced adenosine deaminase activity of 0.92 +/- 0.09 and 2.33 +/- 0.15 U/ml, respectively, in epicardial fluid and 1.93 +/- 0.28 and 4.84 +/- 0.47 U/ml, respectively, in endocardial fluid. Aortic pressure was unchanged by infusion of adenosine deaminase at both infusion rates. Adenosine deaminase (data from both infusion rates pooled) reduced epicardial adenosine from 0.327 +/- 0.028 to 0.139 +/- 0.022 microM, endocardial adenosine from 4.61 +/- 0.42 to 1.64 +/- 0.20 microM, and venous adenosine from 0.017 +/- 0.02 to 0.003 +/- 0.001 microM. The data indicate that infused adenosine deaminase reaches the epicardial and endocardial interstitial fluid (ISF) compartments. The absence of any effect on coronary pressure suggests that adenosine may not be involved in resting basal coronary tone. The presence of significant residual adenosine despite adenosine deaminase infusion indicates that adenosine production in the unstressed isolated guinea pig heart exceeds the degradative capacity of infused adenosine deaminase. Previous studies in which it was assumed that almost all of the endogenous adenosine is inactivated by the infusion of adenosine deaminase should be reevaluated in light of these observations.

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Kroll, K., and E. O. Feigl. "Adenosine is unimportant in controlling coronary blood flow in unstressed dog hearts." American Journal of Physiology-Heart and Circulatory Physiology 249, no. 6 (December 1, 1985): H1176—H1187. http://dx.doi.org/10.1152/ajpheart.1985.249.6.h1176.

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The adenosine hypothesis of local metabolic control of coronary blood flow was tested in the unstressed heart with adenosine deaminase, which converts adenosine to nonvasoactive inosine. If adenosine is normally an important physiological regulator, then adenosine deaminase should lower coronary blood flow. The left main coronary artery was perfused at constant pressure in anesthetized, closed-chest dogs. Adenosine deaminase was deposited in one region of the left ventricle by selective infusion into a branch of the left coronary artery. Coronary blood flow measured with radioactive microspheres was not lower in the region treated with adenosine deaminase than flow measured simultaneously in an untreated control region of the same heart. This finding is contrary to the prediction of the adenosine hypothesis. Coronary vasodilation elicited by intracoronary adenosine infusion was inhibited in the adenosine deaminase-treated region compared with the control region, indicating that adenosine deaminase lowered adenosine concentration at the vascular adenosine receptor. Inhibition of exogenous adenosine vasodilation was fully reversed by intracoronary infusion of a specific inhibitor of adenosine deaminase. Measurement of adenosine deaminase activity in cardiac lymph provided evidence that adenosine deaminase reached the myocardial interstitial space. These results demonstrate that introducing adenosine deaminase into the interstitial space of the unstressed heart did not lower coronary blood flow. This finding indicates that adenosine is normally below the vasoactive threshold and therefore is not important in mediating local metabolic control of blood flow in the unstressed heart.

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6

Hirschhorn, Rochelle. "Adenosine Deaminase Deficiency." Hospital Practice 22, no. 6 (June 15, 1987): 149–56. http://dx.doi.org/10.1080/21548331.1987.11703253.

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Bagheri, S., A. A. Saboury, and T. Haertlé. "Adenosine deaminase inhibition." International Journal of Biological Macromolecules 141 (December 2019): 1246–57. http://dx.doi.org/10.1016/j.ijbiomac.2019.09.078.

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8

Martin, Margarita, Josep M. Aran, Dolors Colomer, Joan Huguet, Josep Joan Centelles, Joan Lluis Vives-Corrons, and Rafael Franco. "Surface adenosine deaminase." Human Immunology 42, no. 3 (March 1995): 265–73. http://dx.doi.org/10.1016/0198-8859(94)00097-a.

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9

Schrader, W. P., C. A. West, and N. L. Strominger. "Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit brain." Journal of Histochemistry & Cytochemistry 35, no. 4 (April 1987): 443–51. http://dx.doi.org/10.1177/35.4.3546489.

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Adenosine deaminase and adenosine deaminase complexing protein have been localized in rabbit brain. Brains fixed in paraformaldehyde or in Clarke's solution were blocked coronally. Blocks from brains fixed in paraformaldehyde were either frozen in liquid nitrogen or embedded in paraffin. Tissue fixed in Clarke's solution was embedded in paraffin. Sections from each block were stained by the peroxidase-antiperoxidase method for adenosine deaminase or complexing protein using affinity-purified goat antibodies. Adenosine deaminase and complexing protein did not co-localize. Adenosine deaminase was detected in oligodendroglia and in endothelial cells lining blood vessels, whereas complexing protein was concentrated in neurons. The subcellular location and appearance of the peroxidase reaction product associated with individual cells was also quite distinctive. The cell bodies of adenosine deaminase-positive oligodendroglia were filled with intense deposits of peroxidase reaction product. In contrast to oligodendroglia, the reaction product associated with most neurons stained for complexing protein was concentrated in granular-appearing cytoplasmic deposits. In some instances, these deposits were clustered about the nuclear membrane. Staining of neurons in the granular layer of cerebellum was an exception. Granule cells were lightly outlined by peroxidase reaction product. Cerebellar islands, also referred to as glomeruli, were stained an intense uniform brown. These results raise the possibility that oligodendroglia and blood vessel endothelia, through the action of adenosine deaminase, might play a role in controlling the concentration of extracellular adenosine in brain. They do not, however, support the suggestion that complexing protein aids in adenosine metabolism by positioning adenosine deaminase on the plasma membrane.

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Hashikawa, T., M. Takedachi, M. Terakura, S. Yamada, L. F. Thompson, Y. Shimabukuro, and S. Murakami. "Activation of Adenosine Receptor on Gingival Fibroblasts." Journal of Dental Research 85, no. 8 (August 2006): 739–44. http://dx.doi.org/10.1177/154405910608500810.

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CD73 (ecto-5′-nucleotidase) on human gingival fibroblasts plays a role in the regulation of intracellular cAMP levels through the generation of adenosine, which subsequently activates adenosine receptors. In this study, we examined the involvement of ecto-adenosine deaminase, which can be anchored to CD26 on human gingival fibroblasts, in metabolizing adenosine generated by CD73, and thus attenuating adenosine receptor activation. Ecto-adenosine deaminase expression on fibroblasts could be increased by pre-treatment with a lysate of Jurkat cells, a cell line rich in cytoplasmic adenosine deaminase. Interestingly, the cAMP response to adenosine generated from 5′-AMP via CD73 and the ability of 5′-AMP to induce hyaluronan synthase 1 mRNA were significantly decreased by the pre-treatment of fibroblasts with Jurkat cell lysate. This inhibitory effect was reversed by the specific adenosine deaminase inhibitor. These results suggest that ecto-adenosine deaminase metabolizes CD73-generated adenosine and regulates adenosine receptor activation.

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11

Wei, H. M., Y. H. Kang, and G. F. Merrill. "Coronary vasodilation during global myocardial hypoxia: effects of adenosine deaminase." American Journal of Physiology-Heart and Circulatory Physiology 254, no. 5 (May 1, 1988): H1004—H1009. http://dx.doi.org/10.1152/ajpheart.1988.254.5.h1004.

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Isolated, perfused guinea pig hearts were infused with intracoronary adenosine deaminase to investigate the contribution of endogenous adenosine to the coronary vasodilation of global myocardial hypoxia. Coronary perfusate pressure was held constant at 70 cmH2O throughout the experiment. We measured retrograde aortic inflow (assumed to equal total antegrade coronary flow) for 3-5 min of hypoxia before and 4 min after initiation of intracoronary adenosine deaminase infusion (4 U.g-1.min-1). In the absence of adenosine deaminase mild global hypoxia increased coronary perfusate flow 60%. In the presence of adenosine deaminase the response was limited to a 5% increment. Myocardial O2 consumption was significantly reduced during hypoxia in the presence of adenosine deaminase. In a second group of hearts, moderate global hypoxia increased coronary perfusate flow 125%. This was limited to a 53% increment in the presence of adenosine deaminase. Adenosine deaminase vehicle had no measurable effect on coronary perfusate flow responses to repeat mild hypoxia in a third group of hearts. We conclude that endogenous adenosine is singularly important in the coronary vasodilation of mild global myocardial hypoxia, but that other regulatory mechanisms might also contribute during moderate hypoxia.

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12

Kuratani, Mitsuo, Ryohei Ishii, Yoshitaka Bessho, Ryuya Fukunaga, Toru Sengoku, Mikako Shirouzu, Shun-ichi Sekine, and Shigeyuki Yokoyama. "Crystal Structure of tRNA Adenosine Deaminase (TadA) fromAquifex aeolicus." Journal of Biological Chemistry 280, no. 16 (January 26, 2005): 16002–8. http://dx.doi.org/10.1074/jbc.m414541200.

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The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNAArg-2. This modification is essential for the decoding system. In this study, we determined the crystal structure ofAquifex aeolicusTadA at a 1.8-Å resolution. This is the first structure of a deaminase acting on tRNA.A. aeolicusTadA has an α/β/α three-layered fold and forms a homodimer. TheA. aeolicusTadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in theA. aeolicusTadA structure, the shapes of the C-terminal helix and the regions between the β4 and β5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.

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Schrader, W. P., C. A. West, A. D. Miczek, and E. K. Norton. "Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction." Journal of Biological Chemistry 265, no. 31 (November 1990): 19312–18. http://dx.doi.org/10.1016/s0021-9258(17)30659-2.

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14

Hershfield, Michael S., Rebecca H. Buckley, Michael L. Greenberg, Alton L. Melton, Richard Schiff, Christine Hatem, Joanne Kurtzberg, et al. "Treatment of Adenosine Deaminase Deficiency with Polyethylene Glycol–Modified Adenosine Deaminase." New England Journal of Medicine 316, no. 10 (March 5, 1987): 589–96. http://dx.doi.org/10.1056/nejm198703053161005.

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15

Tamura, Risa, Hiroyuki Ohta, Yasushi Satoh, Shigeaki Nonoyama, Yasuhiro Nishida, and Masashi Nibuya. "Neuroprotective effects of adenosine deaminase in the striatum." Journal of Cerebral Blood Flow & Metabolism 36, no. 4 (January 8, 2016): 709–20. http://dx.doi.org/10.1177/0271678x15625077.

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Adenosine deaminase (ADA) is a ubiquitous enzyme that catabolizes adenosine and deoxyadenosine. During cerebral ischemia, extracellular adenosine levels increase acutely and adenosine deaminase catabolizes the increased levels of adenosine. Since adenosine is a known neuroprotective agent, adenosine deaminase was thought to have a negative effect during ischemia. In this study, however, we demonstrate that adenosine deaminase has substantial neuroprotective effects in the striatum, which is especially vulnerable during cerebral ischemia. We used temporary oxygen/glucose deprivation (OGD) to simulate ischemia in rat corticostriatal brain slices. We used field potentials as the primary measure of neuronal damage. For stable and efficient electrophysiological assessment, we used transgenic rats expressing channelrhodopsin-2, which depolarizes neurons in response to blue light. Time courses of electrically evoked striatal field potential (eFP) and optogenetically evoked striatal field potential (optFP) were recorded during and after oxygen/glucose deprivation. The levels of both eFP and optFP decreased after 10 min of oxygen/glucose deprivation. Bath-application of 10 µg/ml adenosine deaminase during oxygen/glucose deprivation significantly attenuated the oxygen/glucose deprivation-induced reduction in levels of eFP and optFP. The number of injured cells decreased significantly, and western blot analysis indicated a significant decrease of autophagic signaling in the adenosine deaminase-treated oxygen/glucose deprivation slices. These results indicate that adenosine deaminase has protective effects in the striatum.

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Chinsky, J. M., M. C. Maa, V. Ramamurthy, and R. E. Kellems. "Adenosine Deaminase Gene Expression." Journal of Biological Chemistry 264, no. 24 (August 1989): 14561–65. http://dx.doi.org/10.1016/s0021-9258(18)71715-8.

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17

Yu, Ming, Hanyun Zhou, Qingan Li, Juan Ding, Hongxia Shuai, and Ji Zhang. "Serum Adenosine Deaminase as a Useful Marker to Estimate Coronary Artery Calcification in Type 2 Diabetes Mellitus Patients." Clinical and Applied Thrombosis/Hemostasis 27 (January 1, 2021): 107602962199972. http://dx.doi.org/10.1177/1076029621999722.

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We investigated the association between serum adenosine deaminase and coronary artery calcification (CAC) in type 2 diabetes mellitus (T2DM) patients. The cross-sectional study included 459 patients with T2DM, the clinical and laboratory tests were performed, and all T2DM patients were separated into the 3 groups based on the tertile of serum adenosine deaminase levels. In the baseline data, the CAC score had statistically significant differences between the 3 groups (p < 0.001). Serum adenosine deaminase levels were positively correlated with CAC score in T2DM patients (r = 0.355, p < 0.001). The results of multiple linear regression analysis showed that serum adenosine deaminase was independent positively correlated with CAC score in T2DM patients (r = 0.255, p < 0.001). Receiver-operating characteristic curve analysis showed that area under curve was 0.750 to identify T2DM patients with CAC. Serum adenosine deaminase levels are correlated with CAC scores in T2DM patients, clinically, serum adenosine deaminase should be considered as an underlying marker to determine the severity of atherosclerosis in T2DM patients.

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Friedrichs, G. S., and G. F. Merrill. "Adenosine deaminase and adenosine attenuate ventricular arrhythmias caused by norepinephrine." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 3 (March 1, 1991): H979—H984. http://dx.doi.org/10.1152/ajpheart.1991.260.3.h979.

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Twenty-five beagles weighing 9.1 +/- 0.4 kg were used to investigate the arrhythmogenic effects of divided doses of intracoronary norepinephrine (50-200 ng.kg-1.min-1) in the absence and the presence of adenosine deaminase (5 U.kg-1.min-1). A dose of norepinephrine (100 ng.kg-1.min-1) that caused 66 +/- 17% ectopy in the absence of adenosine deaminase caused only 16 +/- 14% ectopy (P less than 0.05) in the presence of the enzyme. Ventricular tachycardia caused by 200 ng.kg-1.min-1 norepinephrine was reduced from 1.2 +/- 0.3 to 0.1 +/- 0.1 bouts/10 cardiac cycles (P less than 0.05) by adenosine deaminase. In five additional dogs, intracoronary adenosine (0.11 mumol/min) terminated sustained norepinephrine-induced (200 ng.kg-1.min-1) ventricular tachycardia within 23 +/- 9 s (P less than 0.05). As long as the adenosine infusion was maintained, a normal sinus rhythm was observed. We conclude that both adenosine and adenosine deaminase significantly attenuate norepinephrine-induced ventricular arrhythmias. A common element beyond the deamination of adenosine, quite possibly ammonia, appears to account for these results.

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Tarigan, Lupita Yessica, and Deddy Iskandar. "Pemeriksaan Adenosine Deaminase (ADA) sebagai Alternatif Diagnosis TB pada Anak." Cermin Dunia Kedokteran 49, no. 7 (July 5, 2022): 382. http://dx.doi.org/10.55175/cdk.v49i7.1935.

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Pendahuluan. Diagnostik tuberkulosis (TB) pada anak merupakan masalah tersendiri karena manifestasi klinis yang beragam dan tidak tersedianya standar baku penegakan diagnosis. Kasus. Anak perempuan usia 6 tahun, dengan klinis demam, batuk, dan sesak nafas. Pada pemeriksaan fisik didapatkan penurunan suara napas di rongga dada kanan. Hasil pemeriksaan radiologis didukung ultrasonografi tampak gambaran efusi pleura kanan yang sebagian sudah terorganisasi. Hasil uji laboratorium didapatkan leukositosis dan hasil tes IGRA negatif. Analisis cairan pleura menunjukkan peningkatan kadar adenosin deaminase. Pengobatan TB menghasilkan perbaikan klinis dan radiologis bermakna. Simpulan. Pemeriksaan adenosin deaminase dapat dipertimbangkan untuk alternatif diagnosis TB pada anak.Diagnosis of tuberculosis (TB) in children is still problematic because of various clinical manifestations and the unavailability of diagnostic standard. Case. A 6-year old girl with fever, cough and shortness of breath. On physical examination, there was a decrease breath sounds in the right chest. Radiology examination showed a partially organized right pleural effusion, supported with ultrasound finding. Lab test found leucocytosis and IGRA test was negative. Pleural fluid analysis showed increased adenosine deaminase level. TB treatment resulted in significant clinical and radiological improvement. Conclusion. Adenosine deaminase test can be considered as an alternative for TB diagnosis in children.

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O'Connell, M. A., S. Krause, M. Higuchi, J. J. Hsuan, N. F. Totty, A. Jenny, and W. Keller. "Cloning of cDNAs encoding mammalian double-stranded RNA-specific adenosine deaminase." Molecular and Cellular Biology 15, no. 3 (March 1995): 1389–97. http://dx.doi.org/10.1128/mcb.15.3.1389.

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Double-stranded RNA (dsRNA)-specific adenosine deaminase converts adenosine to inosine in dsRNA. The protein has been purified from calf thymus, and here we describe the cloning of cDNAs encoding both the human and rat proteins as well as a partial bovine clone. The human and rat clones are very similar at the amino acid level except at their N termini and contain three dsRNA binding motifs, a putative nuclear targeting signal, and a possible deaminase motif. Antibodies raised against the protein encoded by the partial bovine clone specifically recognize the calf thymus dsRNA adenosine deaminase. Furthermore, the antibodies can immunodeplete a calf thymus extract of dsRNA adenosine deaminase activity, and the activity can be restored by addition of pure bovine deaminase. Staining of HeLa cells confirms the nuclear localization of the dsRNA-specific adenosine deaminase. In situ hybridization in rat brain slices indicates a widespread distribution of the enzyme in the brain.

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Doyle, Michael, and Michael F. Jantsch. "Distinct in vivo roles for double-stranded RNA-binding domains of the Xenopus RNA-editing enzyme ADAR1 in chromosomal targeting." Journal of Cell Biology 161, no. 2 (April 28, 2003): 309–19. http://dx.doi.org/10.1083/jcb.200301034.

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The RNA-editing enzyme adenosine deaminase that acts on RNA (ADAR1) deaminates adenosines to inosines in double-stranded RNA substrates. Currently, it is not clear how the enzyme targets and discriminates different substrates in vivo. However, it has been shown that the deaminase domain plays an important role in distinguishing various adenosines within a given substrate RNA in vitro. Previously, we could show that Xenopus ADAR1 is associated with nascent transcripts on transcriptionally active lampbrush chromosomes, indicating that initial substrate binding and possibly editing itself occurs cotranscriptionally. Here, we demonstrate that chromosomal association depends solely on the three double-stranded RNA-binding domains (dsRBDs) found in the central part of ADAR1, but not on the Z-DNA–binding domain in the NH2 terminus nor the catalytic deaminase domain in the COOH terminus of the protein. Most importantly, we show that individual dsRBDs are capable of recognizing different chromosomal sites in an apparently specific manner. Thus, our results not only prove the requirement of dsRBDs for chromosomal targeting, but also show that individual dsRBDs have distinct in vivo localization capabilities that may be important for initial substrate recognition and subsequent editing specificity.

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Centelles, J. J., and R. Franco. "Is adenosine deaminase involved in adenosine transport?" Medical Hypotheses 33, no. 4 (December 1990): 245–50. http://dx.doi.org/10.1016/0306-9877(90)90136-3.

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23

Kirkeboen, K. A., G. Aksnes, K. Lande, and A. Ilebekk. "Role of adenosine for reactive hyperemia in normal and stunned porcine myocardium." American Journal of Physiology-Heart and Circulatory Physiology 263, no. 4 (October 1, 1992): H1119—H1127. http://dx.doi.org/10.1152/ajpheart.1992.263.4.h1119.

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The role of adenosine for reactive hyperemia in normal and stunned myocardium was examined in 16 open-chest barbiturate-anesthetized pigs. Interstitial adenosine concentration was reduced or enhanced by intracoronary infusion of adenosine deaminase or the nucleoside transport inhibitor R 75231, respectively. In normal myocardium, adenosine deaminase reduced volume of hyperemia (Doppler flowmetry) after a 30-s left anterior descending coronary artery (LAD) occlusion by 20% (6-34%; P < 0.05), whereas R 75231 increased volume of hyperemia by 15% (2-24%; P < 0.05). Adenosine deaminase reduced volume of hyperemia after a 2-min LAD occlusion by 27% (13-37%; P < 0.001), whereas R 75231 increased volume of hyperemia by 66% (53-159%; P < 0.001). Adenosine deaminase and R 75231 did not affect maximal hyperemia. Volume of hyperemia after a 2-min LAD occlusion was reduced in stunned myocardium (%systolic segment length shortening reduced by approximately 45%, ultrasonic technique) but not further altered by either adenosine deaminase or R 75231. These findings show that adenosine contributes to reactive hyperemia after 30-120 s of ischemia in normal myocardium and indicate that the reduced reactive hyperemia in stunned myocardium is due to reduced accumulation of adenosine during ischemia.

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Saccomanno, L., and B. L. Bass. "The cytoplasm of Xenopus oocytes contains a factor that protects double-stranded RNA from adenosine-to-inosine modification." Molecular and Cellular Biology 14, no. 8 (August 1994): 5425–32. http://dx.doi.org/10.1128/mcb.14.8.5425-5432.1994.

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Here we describe studies of double-stranded RNA (dsRNA) adenosine deaminase in Xenopus laevis, in particular during meiotic maturation, the period during which a stage VI oocyte matures to an egg. We show that dsRNA adenosine deaminase is in the nuclei of stage VI oocytes. Most importantly, we demonstrate that the cytoplasm of stage VI oocytes contains a factor that protects microinjected dsRNA from deamination when dsRNA adenosine deaminase is released from the nucleus during meiotic maturation. Our data suggest that the protection factor is a cytoplasmic dsRNA-binding protein or proteins that bind to dsRNA in a sequence-independent manner to occlude dsRNA from binding to dsRNA adenosine deaminase. The cytoplasmic double-stranded RNA-binding protein(s) does not bind to other nucleic acids and can be titrated at high concentrations of dsRNA. These studies raise the question of whether all dsRNA-binding proteins share endogenous substrates and also suggest potential means of regulating dsRNA adenosine deaminase in vivo.

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Saccomanno, L., and B. L. Bass. "The cytoplasm of Xenopus oocytes contains a factor that protects double-stranded RNA from adenosine-to-inosine modification." Molecular and Cellular Biology 14, no. 8 (August 1994): 5425–32. http://dx.doi.org/10.1128/mcb.14.8.5425.

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Here we describe studies of double-stranded RNA (dsRNA) adenosine deaminase in Xenopus laevis, in particular during meiotic maturation, the period during which a stage VI oocyte matures to an egg. We show that dsRNA adenosine deaminase is in the nuclei of stage VI oocytes. Most importantly, we demonstrate that the cytoplasm of stage VI oocytes contains a factor that protects microinjected dsRNA from deamination when dsRNA adenosine deaminase is released from the nucleus during meiotic maturation. Our data suggest that the protection factor is a cytoplasmic dsRNA-binding protein or proteins that bind to dsRNA in a sequence-independent manner to occlude dsRNA from binding to dsRNA adenosine deaminase. The cytoplasmic double-stranded RNA-binding protein(s) does not bind to other nucleic acids and can be titrated at high concentrations of dsRNA. These studies raise the question of whether all dsRNA-binding proteins share endogenous substrates and also suggest potential means of regulating dsRNA adenosine deaminase in vivo.

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Schrader, W. P., and C. A. West. "Localization of adenosine deaminase and adenosine deaminase complexing protein in rabbit heart. Implications for adenosine metabolism." Circulation Research 66, no. 3 (March 1990): 754–62. http://dx.doi.org/10.1161/01.res.66.3.754.

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Hanley, F. L., M. T. Grattan, M. B. Stevens, and J. I. Hoffman. "Role of adenosine in coronary autoregulation." American Journal of Physiology-Heart and Circulatory Physiology 250, no. 4 (April 1, 1986): H558—H566. http://dx.doi.org/10.1152/ajpheart.1986.250.4.h558.

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The role of cardiac interstitial adenosine as an important metabolite in coronary autoregulation has not been established. We therefore measured steady-state cardiac interstitial adenosine concentration at a high and a low coronary inflow pressure using an epicardial diffusion well in anesthetized dogs. Although coronary resistance for the high and low pressure points showed highly significant differences (P less than 0.001), adenosine averaged 302 +/- 98 and 286 +/- 91 (SD) pmol/ml for the high and low pressure points, respectively (P greater than 0.20). Cardiac interstitial adenosine concentration was then measured with and without an intracoronary infusion of adenosine deaminase catalytic subunit. Adenosine averaged 28 +/- 21 (SD) pmol/ml during the infusion compared with 281 +/- 68 during control conditions (P less than 0.001). Finally, pressure-flow relations were obtained with and without the adenosine deaminase infusion, and there was no loss of autoregulation in the pressure of adenosine deaminase. These findings indicate that intracoronary adenosine deaminase markedly reduces interstitial adenosine concentration, that cardiac interstitial adenosine concentration remains constant during autoregulation, and that the coronary bed autoregulates normally when interstitial adenosine is reduced to levels close to zero. We conclude that cardiac interstitial adenosine concentration is not an important component in coronary autoregulation.

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Hu, B., R. A. Altschuld, and C. M. Hohl. "Adenosine stimulation of AMP deaminase activity in adult rat cardiac myocytes." American Journal of Physiology-Cell Physiology 264, no. 1 (January 1, 1993): C48—C53. http://dx.doi.org/10.1152/ajpcell.1993.264.1.c48.

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Using an in situ assay for analyzing AMP deaminase activity in isolated adult rat ventricular myocytes, we have shown that IMP production is stimulated approximately twofold in cardiac cells incubated with 10 microM adenosine. This effect of adenosine was not blocked by the adenosine A1-receptor antagonist 8-cyclophenyl-1,3-dipropylaxanthine (0.01-1 microM) except at a concentration (100 microM) that may inhibit adenosine transport. Similarly, in situ AMP deaminase activity was not enhanced by treatment with the specific adenosine A1-receptor agonists N6-phenylisopropyl adenosine or cyclopentyladenosine, nor was it sensitive to prior treatment of cells with pertussis toxin. The nucleoside transport blockers S-4-nitrobenzyl-6-thioinosine, dipyridamole, and papaverine inhibited adenosine-induced increases in IMP production by 75-85%, suggesting an intracellular site of action. Modulation of enzyme activity via the transmethylation pathway could not be implicated since incubation of cardiac cells under conditions known to elevate intracellular S-adenosyl-L-homocysteine had no demonstrable effect on AMP deaminase. Furthermore, a direct allosteric effect of adenosine on the partially purified rat cardiac enzyme was not observed. The results indicate that intracellular adenosine modulates rat cardiac AMP deaminase by an unknown mechanism.

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Kocic, G., J. Nikolic, T. Jevtovic-Stoimenov, D. Sokolovic, H. Kocic, T. Cvetkovic, D. Pavlovic, A. Cencic, and D. Stojanovic. "L-Arginine Intake Effect on Adenine Nucleotide Metabolism in Rat Parenchymal and Reproductive Tissues." Scientific World Journal 2012 (2012): 1–4. http://dx.doi.org/10.1100/2012/208239.

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L-arginine is conditionally essetcial amino acid, required for normal cell growth, protein synthesis, ammonia detoxification, tissue growth and general performance, proposed in the treatment of men sterility and prevention of male impotence. The aim of the present paper was to estimate the activity of the enzymes of adenine nucleotide metabolism:5′-nucleotidase (5′-NU), adenosine deaminase (ADA), AMP deaminase, and xanthine oxidase (XO), during dietary intake of L-arginine for a period of four weeks of male Wistar rats. Adenosine concentration in tissues is maintained by the relative activities of the adenosine-producing enzyme,5′-NU and the adenosine-degrading enzyme-ADA adenosine deaminase. Dietary L-arginine intake directed adenine nucleotide metabolism in liver, kidney, and testis tissue toward the activation of adenosine production, by increased5′-NU activity and decreased ADA activity. Stimulation of adenosine accumulation could be of importance in mediating arginine antiatherosclerotic, vasoactive, immunomodulatory, and antioxidant effects. Assuming that the XO activity reflects the rate of purine catabolism in the cell, while the activity of AMP deaminase is of importance in ATP regeneration, reduced activity of XO, together with the increased AMP-deaminase activity, may suggest that adenine nucleotides are presumably directed to the ATP regenerating process during dietary L-arginine intake.

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Rosfadilla, Puspa, Widirahardjo Widirahardjo, Fajrinur Syarani, and Erna Mutiara. "Diagnostic Accuracy of Pleural Fluid Adenosine Deaminase Level Test in Tuberculous Pleural Effusion." Jurnal Respirologi Indonesia 37, no. 4 (October 17, 2017): 278–82. http://dx.doi.org/10.36497/jri.v37i4.81.

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Background: Tuberculous pleural effusion is a paucibacillary manifestation of tuberculosis, so isolation of Mycobacterium tuberculosis is difficult, biomarkers being an alternative for diagnosis. Adenosine deaminase has the potential to optimize the diagnostic approach of tuberculous pleural effusion. Methods: This study is a diagnostic test observational (cross-sectional), which included 35 inpatient samples that meet inclusion and exclusion criteria from H. Adam Malik Medan General Hospital. Research began on February 1st until July 31st 2016 to examine 10 cc of pleural fluid specimens for the levels of Adenosine deaminase. Results: There are significant differences in the levels of adenosine deaminase from tuberculous and non-tuberculous pleural effusion (P=0.001). In the cut-off point 36.55 IU/L, level of sensitivity 95.8%, specificity 90.99%, positive predictive value 95.8%, negative predictive value 90.99%, and accuracy 94.2% of pleural fluid adenosine deaminase level test in tuberculous pleural effusion. Conclusion: Adenosine deaminase pleural fluid can be a diagnostic modality that is easy, fast, relatively affordable and applicable in the diagnosis of tuberculous pleural effusion. (J Respir Indo. 2017; 37(4): 278-82)

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Sawmiller, D. R., and C. C. Chou. "Role of adenosine in postprandial and reactive hyperemia in canine jejunum." American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no. 4 (October 1, 1992): G487—G493. http://dx.doi.org/10.1152/ajpgi.1992.263.4.g487.

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The role of adenosine in postprandial jejunal hyperemia was investigated by determining the effect of placement of predigested food into the jejunal lumen on blood flow and oxygen consumption before and during intra-arterial infusion of dipyridamole (1.5 microM arterial concn) or adenosine deaminase (9 U/ml arterial concn) in anesthetized dogs. Neither drug significantly altered resting jejunal blood flow and oxygen consumption. Before dipyridamole or deaminase, food placement increased blood flow by 30-36%, 26-42%, and 21-46%, and oxygen consumption by 13-22%, 21-22%, and 26-29%, during 0- to 3-, 4- to 7-, and 8- to 11-min placement periods, respectively. Adenosine deaminase abolished the entire 11-min hyperemia, whereas dipyridamole significantly enhanced the initial 7-min hyperemia (45-49%). Both drugs abolished the initial 7-min food-induced increase in oxygen consumption. Dipyridamole attenuated (14%), whereas deaminase did not alter (28%), the increased oxygen consumption that occurred at 8-11 min. Adenosine deaminase also prevented the food-induced increase in venoarterial adenosine concentration difference. In separate series of experiments, luminal placement of food significantly increased jejunal lymphatic adenosine concentration and release. Also, reactive hyperemia was accompanied by an increase in venous adenosine concentration and release. This study provides further evidence to support the thesis that adenosine plays a role in postprandial and reactive hyperemia in the canine jejunum.

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Schrader, W. P., C. A. West, U. H. Rudofsky, and W. A. Samsonoff. "Subcellular distribution of adenosine deaminase and adenosine deaminase-complexing protein in rabbit kidney: implications for adenosine metabolism." Journal of Histochemistry & Cytochemistry 42, no. 6 (June 1994): 775–82. http://dx.doi.org/10.1177/42.6.8189039.

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We evaluated the age-related distribution of adenosine deaminase (ADA) and adenosine deaminase-complexing protein (CP) in rabbit kidney by immunohistochemical staining procedures. Paraffin- or resin-embedded tissue from rabbits < 1 week-4 years of age were stained by the peroxidase-anti-peroxidase (PAP) method for ADA and CP. With the exception of neonates, the qualitative staining pattern of each protein remained generally constant with age. In the cortex, distal tubules, blood vessels, histiocytes, and epithelial cells lining Bowman's capsule stained for ADA. Proximal tubules and glomeruli were positive for CP. In contrast to the segregated pattern in the cortex, staining for ADA and CP overlapped in the corticomedullary junction. ADA and CP co-localized on the brush border of tubule cells of the S3 segment. In the cytoplasm of these cells, staining for ADA was characterized by scattered punctuate deposits of peroxidase reaction product. In some instances these punctuate deposits also appeared to be positive for CP. In medulla, epithelial cells of the thin limb were positive for both ADA and CP, whereas papillary collecting ducts stained only for CP. These results document the age-related, tissue-specific expression and localization of ADA in renal tissue, features that probably reflect the crucial role played by the enzyme in adenosine/deoxyadenosine catabolism. In addition, colocalization of ADA and CP on the brush border of cells in the S3 segment of proximal tubules provides support for the hypothesis that one function of CP may be to position ADA on the plasma membrane of specific cell populations, further expanding the enzyme's utility in nucleoside metabolism.

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Zhulai, Galina, Eugenia Oleinik, Mikhail Shibaev, and Kirill Ignatev. "Adenosine-Metabolizing Enzymes, Adenosine Kinase and Adenosine Deaminase, in Cancer." Biomolecules 12, no. 3 (March 8, 2022): 418. http://dx.doi.org/10.3390/biom12030418.

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The immunosuppressive effect of adenosine in the microenvironment of a tumor is well established. Presently, researchers are developing approaches in immune therapy that target inhibition of adenosine or its signaling such as CD39 or CD73 inhibiting antibodies or adenosine A2A receptor antagonists. However, numerous enzymatic pathways that control ATP-adenosine balance, as well as understudied intracellular adenosine regulation, can prevent successful immunotherapy. This review contains the latest data on two adenosine-lowering enzymes: adenosine kinase (ADK) and adenosine deaminase (ADA). ADK deletes adenosine by its phosphorylation into 5′-adenosine monophosphate. Recent studies have revealed an association between a long nuclear ADK isoform and an increase in global DNA methylation, which explains epigenetic receptor-independent role of adenosine. ADA regulates the level of adenosine by converting it to inosine. The changes in the activity of ADA are detected in patients with various cancer types. The article focuses on the biological significance of these enzymes and their roles in the development of cancer. Perspectives of future studies on these enzymes in therapy for cancer are discussed.

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Bindu, T. Hima, and R. Maheshwara Reddy. "Role of cerebrospinal fluid adenosine deaminase activity in the diagnosis of tuberculous meningitis in children." International Journal of Contemporary Pediatrics 4, no. 2 (February 22, 2017): 411. http://dx.doi.org/10.18203/2349-3291.ijcp20170537.

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Background: Early and correct treatment is essential for successful outcome in patients of tuberculous men-ingitis. Adenosine deaminase activity in the cerebrospinal fluid has been found to be a simple and useful investigation in the diagnosis of tuberculous meningitis in children.Methods: It is a cross sectional observational hospital based study conducted at the Department of Paediatrics, Deccan College of Medical Sciences, Kanchanbagh, Hyderabad, India. Children aged 2 months to 12 years were included in the study during April 2016 to October 2016.Results: The mean value of adenosine deaminase activity in the cerebrospinal fluid of tuberculous meningitis cases was 13.3±14.49. The mean cerebrospinal fluid adenosine deaminase levels in tuberculous meningitis patients was significantly higher than non-tuberculous meningitis patients with P <0.01.Conclusions: The mean cerebrospinal fluid adenosine deaminase level was significantly raised in tuberculous meningitis patients.

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35

Dobson, J. G., R. W. Ordway, and R. A. Fenton. "Endogenous adenosine inhibits catecholamine contractile responses in normoxic hearts." American Journal of Physiology-Heart and Circulatory Physiology 251, no. 2 (August 1, 1986): H455—H462. http://dx.doi.org/10.1152/ajpheart.1986.251.2.h455.

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The importance of endogenous myocardial adenosine in attenuating catecholamine-elicited contractile responses was investigated in perfused oxygenated rat hearts. Perfusion of the isolated hearts with adenosine deaminase potentiated the isoproterenol-induced increases of three contractile variables (left ventricular pressure development and rates of both left ventricular pressure development and relaxation). The peak (maximal, within 30 s) and maintained (after 1 min) increases of the contractile variables caused by 10(-8) M isoproterenol were enhanced by 15-22 and 31-43%, respectively. Adenosine deaminase appeared in epicardial surface transudates of similarly perfused hearts, indicating that the enzyme had entered the myocardial interstitial space. Isoproterenol alone elevated the release of adenosine into coronary effluents of isoproterenol-stimulated hearts, and adenosine deaminase prevented the release of the nucleoside. The higher the level of adenosine in the effluent, the greater the reduction of the peak contractile variables. Phenylisopropyladenosine at 10(-8) M prevented the adenosine deaminase potentiation of 10(-9) M isoproterenol-induced contractile responses. The adenosine analogue at 10(-6) M blocked completely the isoproterenol-produced increases in the contractile variables. These results suggest that endogenous adenosine prevents full mechanical responsiveness to beta-adrenoceptor stimulation in the oxygenated myocardium. In addition, the findings support the notion that adenosine serves as an important negative feedback modulator in the oxygenated heart.

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36

Bothamley, G. H. "Tuberculous pleurisy and adenosine deaminase." Thorax 50, no. 6 (June 1, 1995): 593–94. http://dx.doi.org/10.1136/thx.50.6.593.

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37

Ungerer, J. P., and S. H. Bissbort. "Adenosine deaminase in pleural effusions." Clinical Chemistry 42, no. 11 (November 1, 1996): 1880. http://dx.doi.org/10.1093/clinchem/42.11.1880.

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38

Fein, Alan M. "Tuberculous Pleurisy and Adenosine Deaminase." Clinical Pulmonary Medicine 3, no. 1 (January 1996): 52. http://dx.doi.org/10.1097/00045413-199601000-00007.

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39

Lupidi, G., C. Colao, F. Marmocchi, and G. Cristalli. "Photoinactivation studies on adenosine deaminase." IUBMB Life 44, no. 5 (April 1998): 1031–43. http://dx.doi.org/10.1080/15216549800202092.

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40

Jaqueti, J., D. Martinez-Hernández, R. Hernández-Garcia, F. Navarro-Gallar, and J. Arenas-Barbero. "Adenosine deaminase in pregnancy serum." Clinical Chemistry 36, no. 12 (December 1, 1990): 2144. http://dx.doi.org/10.1093/clinchem/36.12.2144.

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Ozsahin, Hulya, Francisco X. Arredondo-Vega, Ines Santisteban, Hanspeter Fuhrer, Peter Tuchschmid, Wolfram Jochum, Adriano Aguzzi, et al. "Adenosine Deaminase Deficiency in Adults." Blood 89, no. 8 (April 15, 1997): 2849–55. http://dx.doi.org/10.1182/blood.v89.8.2849.

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Abstract Adenosine deaminase (ADA) deficiency typically causes severe combined immunodeficiency (SCID) in infants. We report metabolic, immunologic, and genetic findings in two ADA-deficient adults with distinct phenotypes. Patient no. 1 (39 years of age) had combined immunodeficiency. She had frequent infections, lymphopenia, and recurrent hepatitis as a child but did relatively well in her second and third decades. Then she developed chronic sinopulmonary infections, including tuberculosis, and hepatobiliary disease; she died of viral leukoencephalopathy at 40 years of age. Patient no. 2, a healthy 28-year-old man with normal immune function, was identified after his niece died of SCID. Both patients lacked erythrocyte ADA activity but had only modestly elevated deoxyadenosine nucleotides. Both were heteroallelic for missense mutations: patient no. 1, G216R and P126Q (novel); patient no. 2, R101Q and A215T. Three of these mutations eliminated ADA activity, but A215T reduced activity by only 85%. Owing to a single nucleotide change in the middle of exon 7, A215T also appeared to induce exon 7 skipping. ADA deficiency is treatable and should be considered in older patients with unexplained lymphopenia and immune deficiency, who may also manifest autoimmunity or unexplained hepatobiliary disease. Metabolic status and genotype may help in assessing prognosis of more mildly affected patients.

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Baganha, Manuel Fontes, Alice Pêgo, Maria A. Lima, Ermelinda V. Gaspar, and Antonio Robalo Cordeiro. "Serum and Pleural Adenosine Deaminase." Chest 97, no. 3 (March 1990): 605–10. http://dx.doi.org/10.1378/chest.97.3.605.

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Baganha, Manuel Fontes, Alice Pego, Maria A. Lima, Ermelinda V. Gaspar, and Antonio Robalo Cordeiro. "Adenosine Deaminase and Lymphocytic Populations." Chest 99, no. 3 (March 1991): 790. http://dx.doi.org/10.1378/chest.99.3.789-b.

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Bovornkitti, Somchai, Rungsun Pushpakom, Nanta Maranetra, Arth Nana, and Suchai Charoenratanakul. "Adenosine Deaminase and Lymphocytic Populations." Chest 99, no. 3 (March 1991): 789–90. http://dx.doi.org/10.1378/chest.99.3.790-a.

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Saio, Fumimasa, Hiroaki Omura, and Koichi Hayano. "Adenosine Deaminase Activity in Soils." Soil Science and Plant Nutrition 32, no. 1 (March 1986): 107–12. http://dx.doi.org/10.1080/00380768.1986.10557485.

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Hoogerbrugge, Peter M., Jack J. H. Bleesing, Jaak M. Vossen, and Dinko Valerio. "Treatment of Adenosine Deaminase Deficiency." BioDrugs 9, no. 2 (1998): 87–93. http://dx.doi.org/10.2165/00063030-199809020-00001.

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Aguado, J. M., F. Pons, D. K. Bhargava, Sandeep Nijhawan, and Manju Gupta. "ADENOSINE DEAMINASE AND TUBERCULOUS PERITONITIS." Lancet 333, no. 8649 (June 1989): 1260–61. http://dx.doi.org/10.1016/s0140-6736(89)92350-7.

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Villena Garrido, V. "Mesothelioma and Pleural Adenosine Deaminase." Archivos de Bronconeumología ((English Edition)) 41, no. 3 (March 2005): 175. http://dx.doi.org/10.1016/s1579-2129(06)60420-5.

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Szabados, Eve, and Richard I. Christopherson. "Adenosine deaminase deficiency in erythrocytes." Biochemical Education 19, no. 2 (April 1991): 90–94. http://dx.doi.org/10.1016/0307-4412(91)90016-2.

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NAGY, J., J. GEIGER, and W. STAINES. "Adenosine deaminase and purinergic neuroregulation." Neurochemistry International 16, no. 3 (1990): 211–21. http://dx.doi.org/10.1016/0197-0186(90)90093-9.

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Journal articles on the topic 'Adenosine deaminase'

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