Relevant bibliographies by topics / Adenosine deaminases

Academic literature on the topic 'Adenosine deaminases'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Adenosine deaminases"

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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.v74.3.1121.1121.

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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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LIU, Chengqian, Yulia Mukienko, Chengxiang Wu, and Andrey Zavialov. "Human adenosine deaminases control the immune cell responses to activation signals by reducing extracellular adenosine concentration." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 124.63. http://dx.doi.org/10.4049/jimmunol.196.supp.124.63.

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Abstract Adenosine rapidly accumulates in the sites of inflammation and tumor growth. It binds to adenosine receptors expressed on the cell surface of immune cells and induces either suppression or activation of inflammatory responses to pathogens. In humans the level of extracellular adenosine is regulated by two adenosine deaminases ADA1 and ADA2. Decrease in ADAs concentration due to genetic defects in the ADA genes leads to serious perturbation in the immune system function while increase in ADA activity associates with numerous immune diseases and cancers. The immune responses to extracellular adenosine have largely been studied using pharmacological approach where non-hydrolysable adenosine receptors agonists substitute adenosine to form the activated state of adenosine receptors. On contrary, adenosine receptors bound to adenosine receptor antagonists mimic inactivated state of adenosine receptors. Here, the effect of adenosine receptor agonists and antagonists on the monocytes function as well as and T helper cell proliferation and differentiation was compared with the effect of adenosine and adenosine deaminases. It was demonstrated that adenosine deaminases control the immune cells responses to activation signals by reducing the concentration of extracellular adenosine and that the cells sensitivity to adenosine greatly depends on the type of the cell activation. Therefore, our data suggests that ADAs could be considered as new drug candidates for the treatment of immune disorders and cancers.
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Polson, Andrew G., Herbert L. Ley, Brenda L. Bass, and John L. Casey. "Hepatitis Delta Virus RNA Editing Is Highly Specific for the Amber/W Site and Is Suppressed by Hepatitis Delta Antigen." Molecular and Cellular Biology 18, no. 4 (April 1, 1998): 1919–26. http://dx.doi.org/10.1128/mcb.18.4.1919.

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ABSTRACT RNA editing at adenosine 1012 (amber/W site) in the antigenomic RNA of hepatitis delta virus (HDV) allows two essential forms of the viral protein, hepatitis delta antigen (HDAg), to be synthesized from a single open reading frame. Editing at the amber/W site is thought to be catalyzed by one of the cellular enzymes known as adenosine deaminases that act on RNA (ADARs). In vitro, the enzymes ADAR1 and ADAR2 deaminate adenosines within many different sequences of base-paired RNA. Since promiscuous deamination could compromise the viability of HDV, we wondered if additional deamination events occurred within the highly base paired HDV RNA. By sequencing cDNAs derived from HDV RNA from transfected Huh-7 cells, we determined that the RNA was not extensively modified at other adenosines. Approximately 0.16 to 0.32 adenosines were modified per antigenome during 6 to 13 days posttransfection. Interestingly, all observed non-amber/W adenosine modifications, which occurred mostly at positions that are highly conserved among naturally occurring HDV isolates, were found in RNAs that were also modified at the amber/W site. Such coordinate modification likely limits potential deleterious effects of promiscuous editing. Neither viral replication nor HDAg was required for the highly specific editing observed in cells. However, HDAg was found to suppress editing at the amber/W site when expressed at levels similar to those found during HDV replication. These data suggest HDAg may regulate amber/W site editing during virus replication.
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Bhakta, Sonali, and Toshifumi Tsukahara. "Artificial RNA Editing with ADAR for Gene Therapy." Current Gene Therapy 20, no. 1 (June 24, 2020): 44–54. http://dx.doi.org/10.2174/1566523220666200516170137.

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Editing mutated genes is a potential way for the treatment of genetic diseases. G-to-A mutations are common in mammals and can be treated by adenosine-to-inosine (A-to-I) editing, a type of substitutional RNA editing. The molecular mechanism of A-to-I editing involves the hydrolytic deamination of adenosine to an inosine base; this reaction is mediated by RNA-specific deaminases, adenosine deaminases acting on RNA (ADARs), family protein. Here, we review recent findings regarding the application of ADARs to restoring the genetic code along with different approaches involved in the process of artificial RNA editing by ADAR. We have also addressed comparative studies of various isoforms of ADARs. Therefore, we will try to provide a detailed overview of the artificial RNA editing and the role of ADAR with a focus on the enzymatic site directed A-to-I editing.
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Dolezelova, Eva, Michal Zurovec, Tomas Dolezal, Petr Simek, and Peter J. Bryant. "The emerging role of adenosine deaminases in insects." Insect Biochemistry and Molecular Biology 35, no. 5 (May 2005): 381–89. http://dx.doi.org/10.1016/j.ibmb.2004.12.009.

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Bavelloni, Alberto, Enrico Focaccia, Manuela Piazzi, Mirco Raffini, Valeriana Cesarini, Sara Tomaselli, Arianna Orsini, et al. "AKT‐dependent phosphorylation of the adenosine deaminases ADAR‐1 and ‐2 inhibits deaminase activity." FASEB Journal 33, no. 8 (May 16, 2019): 9044–61. http://dx.doi.org/10.1096/fj.201800490rr.

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Thuy-Boun, Alexander S., Justin M. Thomas, Herra L. Grajo, Cody M. Palumbo, SeHee Park, Luan T. Nguyen, Andrew J. Fisher, and Peter A. Beal. "Asymmetric dimerization of adenosine deaminase acting on RNA facilitates substrate recognition." Nucleic Acids Research 48, no. 14 (June 29, 2020): 7958–72. http://dx.doi.org/10.1093/nar/gkaa532.

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Abstract Adenosine deaminases acting on RNA (ADARs) are enzymes that convert adenosine to inosine in duplex RNA, a modification that exhibits a multitude of effects on RNA structure and function. Recent studies have identified ADAR1 as a potential cancer therapeutic target. ADARs are also important in the development of directed RNA editing therapeutics. A comprehensive understanding of the molecular mechanism of the ADAR reaction will advance efforts to develop ADAR inhibitors and new tools for directed RNA editing. Here we report the X-ray crystal structure of a fragment of human ADAR2 comprising its deaminase domain and double stranded RNA binding domain 2 (dsRBD2) bound to an RNA duplex as an asymmetric homodimer. We identified a highly conserved ADAR dimerization interface and validated the importance of these sequence elements on dimer formation via gel mobility shift assays and size exclusion chromatography. We also show that mutation in the dimerization interface inhibits editing in an RNA substrate-dependent manner for both ADAR1 and ADAR2.
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Kopff, M., I. Zakrzewska, J. Klem, J. Kalinowska-Fuchs, and M. Strzelczyk. "Adenosine deaminase activity in blood of patients with stable angina pectoris." Acta Biochimica Polonica 44, no. 2 (June 30, 1997): 359–61. http://dx.doi.org/10.18388/abp.1997_4432.

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The activity of adenosine deaminases (EC.3.5.4.4) in granulocytes and lymphocytes of patients with stable angina pectoris was lower by about 27% and 24%, respectively as compared with control group, whereas these values in erythrocytes and blood plasma were at the normal level.
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Dissertations / Theses on the topic "Adenosine deaminases"

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Li, Xianghua. "Physiological roles of Drosophila ADAR and modifiers." Thesis, University of Edinburgh, 2013. http://hdl.handle.net/1842/12225.

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ADAR (Adenosine Deaminases acting on RNA) family proteins are double-strand RNA binding proteins that deaminate specific adenosines into inosines. This A-to-I conversion is called A-to-I RNA editing and is well conserved in the animal kingdom from nematodes to humans. RNA editing is a pre-splicing event on nascent RNA that may affect alternative splicing when the editing occurs in the exon-intron junction or in the intron. Also, editing may change biological function of small RNAs by editing the premicroRNAs or other noncoding RNAs. Editing also alters protein amino acid sequences because inosine in the mRNA base pairs with cytosine and is therefore read as guanosine. In mammals, there are three ADAR family proteins, ADAR1, ADAR2, and ADAR3, encoded by three different genes. So far, no enzymatic activity of ADAR3 is detected. The most frequently edited targets of ADAR1 and ADAR2 are regions covering copies of Alu transposable elements in primates. In addition, loss of some specific editing events leads to profound phenotypes when the editing does not occur correctly. For example, some human neural disorders – such as epilepsy, forebrain ischemia, and Amyotrophic Lateral Sclerosis – are known to be associated with abnormally edited ion channel transcripts. Drosophila has a single ADAR protein (encoded by the Adar gene) that is highly conserved with human ADAR2 (encoded by the ADARB1 gene). To date, 972 editing sites have been identified in 597 transcripts in Drosophila, and approximately 20% of AGO2-associated esiRNAs are edited. Similar to mammals, many ion channel-encoding mRNA transcripts undergo ADAR-mediated A-to-I editing in Drosophila. While Adar1 null mice die at the embryonic stage and Adar2 null mice die shortly after birth due to seizures, Adar null flies are morphologically normal and have normal life span under ideal conditions. However, Adar null flies exhibit severe neurodegeneration and locomotion defects from eclosion, whilst Adar overexpression (OE) is lethal. To better understand the physiological role of RNA editing and ADAR, and to shed light on ADAR-related human disease, I used Drosophila Adar mutant flies as a model organism to investigate phenotypes, and to find chromosomal deletions and specific mutations that rescue the neural-behavioural phenotype of the Adar null mutant flies. Using the publicly available chromosomal deletions collectively covering more than 80% of the euchromatic genome of Chromsome III, I performed a genetic screen to find rescuers of the lethality caused by Adar overexpression. I confirmed that mutation in Rdl (Resistant to dieldrin, the gene encoding GABAA receptor main subunit) rescues. This rescue was not likely caused by effects on Adar expression level or activity. Driven by the hypothesis that the rescue may be due to reduction in GABAergic input to neurons, I recorded spontaneous firing activity of Drosophila larval aCC motor neurons using in vivo extracellular current recording technique. As expected, the neurons overexpressing Adar had much less activities compared with wild type neurons. Also, I found that Adar null fly neurons fired much more and showed epilepsy-like increased excitability. Although feeding PTX (Picrotoxin), a GABAA receptor antagonist, failed to rescue the lethality, reducing the expression of GAD1 to reduce synthesis of GABA was able to rescue the ADAR overexpression lethality. These results suggest that ADAR may finetune neuron activity synergistically with the GABAergic inhibitory signal pathway. I used MARCM (mosaic analysis using a repressible cell marker) to detect cellautonomous phenotypes in Adar null cells in otherwise wild type flies. Although neurodegeneration, observed as enlarged vacuoles formation in neurophils, was detected both in histological staining and EM images, the Adar null neurons marked with GFP from early developmental stages were not lost with age. Nevertheless, swelling in the axons or fragmentation of the axon branches of Adar null neurons was sometimes observed in the midbrain. By comparing the Poly-A RNA sequencing data from Adar null and wild type fly heads, we detected significant upregulation of innate immune genes. I confirmed this by qRT PCR and found that inactive ADAR reduces the innate immune gene transcript levels almost as much as active ADAR does. Further, using the locomotion assay, I confirmed that reintroducing inactive ADAR into Adar null flies can improve the flies’ climbing ability. Based on the Adar null flies having comparatively low viability, I performed a second deficiency screen to find rescuers of Adar null low viability using the same set of deficiencies as in the lethality rescue screen described above. I found seven deletions removing 1 to 37 genes that significantly increased the relative viability of the Adar null flies. However, not all the rescuing deficiencies also improved the Adar null locomotion. One rescuing gene, CG11357 was mapped from one of the rescuing deficiencies, and some mutant alleles of cry, JIL-1 and Gem3 also showed significant effects on the Adar null fly viability. The single gene viability rescuers were also not necessarily locomotion or neurodegeneration rescuers. Although the initial aim was to find neural-behavioural rescuing genes from the viability screen, the viability rescuers found in the screen are more likely to play a role in different aspects of stress response for survival.
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Silva, Aleksandro Schafer da. "Atividade da adenosina desaminase, concentração de nucleotideos e nucleosideo de adenina em ratos Infectados com Trypanosoma evansi." Universidade Federal de Santa Maria, 2011. http://repositorio.ufsm.br/handle/1/4058.

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The purinergic system is known to be an important signaling pathway in different tissues. Among the components of this system have adenosine, a modulator of central nervous, circulatory and immune systems. The concentration of adenosine in the host is controlled by the enzyme adenosine deaminase (ADA), present in tissues, cells and fluids. As a result, the objectives of this study were (1) to determine the ADA activity in Trypanosoma evansi, (2) evaluate the activity of ADA in serum, erythrocytes, lymphocytes and brain of infected rats, and (3) determine the concentration of nucleotides and nucleosides in serum and cerebral cortex of rats infected with T. evansi. In the first study two mice were infected with T. evansi. When these animals showed high parasitemia (±108 parasites/uL) was performed with blood collection and separation of trypomastigotes by DEAE-cellulose column for performing the assays. Spectrometry was performed by the biochemical detection of ADA in the form trypomastigotes of T. evansi. In a second study, we used 39 rats divided into three groups: group A and B (infected) and group C (C1 and C2 control group) Samples of blood and brain samples were collected on day 4 PI (A and C1) and 20 PI (B and C2). From the blood (with anticoagulant) were separated lymphocytes and erythrocytes for measurement of ADA activity, since the serum was obtained from blood samples stored in tubes without anticoagulant. The brain was separated into cerebellum, cerebral cortex, hippocampus and striatum to evaluate the ADA activity in each structure. Decrease of ADA activity in serum and erythrocytes in rats infected with T. evansi when compared not-infected (P<0.05). ADA activity in lymphocytes was decreased at day 4 PI and increased in day 20 PI. There was no difference in ADA activity in the cerebellum. In the cerebral cortex caused a reduction of ADA activity on days 4 and 20 PI. Decrease of ADA activity in hippocampus and striatum in the day 4 and day 20 PI, respectively. In a third study, 24 rats were used, 12 used as a negative control and 12 infected with T. evansi. On day 4 (n = 6 per group) and 20 PI (n = 6 per group) were performed to obtain blood samples of serum and cerebral cortex for analysis. The samples were prepared for quantification of ATP, ADP, AMP and adenosine. This study found increased concentrations of ATP, AMP and adenosine in the brain and serum of rats infected with T. evansi in both periods, except that the levels of adenosine decreased on day 4 PI. The ADP concentration did not change in this study. Therefore, the infection by T. evansi purinergic system components can be changed, may be involved in immune response, in anemia and neurological signs.
O sistema purinérgico é conhecido por ser uma via de sinalização importante em diversos tecidos. Entre os componentes desse sistema destacamos a adenosina, um modulador do sistema nervoso central, circulatório e imunológico. A concentração de adenosina no hospedeiro é controlada pela enzima adenosina deaminase (ADA), presentes em tecidos, células e fluidos. Em virtude disso, os objetivos deste estudo foram (1) determinar a atividade da ADA no Trypanosoma evansi; (2) avaliar a atividade da ADA no soro, eritrócitos, linfócitos e encéfalo e (3) determinar a concentração de nucleotídeos e nucleosideos no soro e córtex cerebral de ratos infectados com T. evansi. Para um primeiro estudo foram infectados dois camundongos com T. evansi. Quando estes animais apresentavam elevada parasitemia (±108 parasito/μL) foi realizada a coleta de sangue e separação dos flagelados por coluna de DEAE-celulose, a fim realização dos ensaios enzimáticos no parasito. Atividade da ADA nas formas trypomastigotas de T. evansi foi determinada por espectofotometria. Em um segundo estudo foi utilizado 39 ratos, divididos em três grupos: grupo A e B (infectado) e grupo C (C1 e C2/controle). Amostras de sangue e encéfalo foram colhidas nos dias 4 pós-infecção (PI) (grupos A e C1) e 20 PI (grupos B e C2). A partir do sangue total colhido com anticoagulante foram separados os linfócitos e eritrócitos para mensuração da atividade da ADA, já o soro foi obtido de amostras de sangue armazenadas em tubos sem anticoagulante. O encéfalo foi separado em cerebelo, córtex cerebral, hipocampo e estriado para avaliar a atividade da ADA em cada estrutura. Então, observou-se redução da atividade de ADA no soro e eritrócitos em ratos infectados com T. evansi em comparação com não-infectados (P <0,05). A atividade de ADA em linfócitos estava diminuída no dia 4 PI e aumentou no dia 20 PI. Não houve diferença da ADA no cerebelo. No córtex cerebral, no hipocampo e estriado ocorreu redução da atividade da ADA nos dia 4 e 20 PI, respectivamente. Em todas as estruturas do encéfalo foi detectada a presença do parasito por PCR. Em um terceiro estudo foram utilizados 24 ratos, sendo 12 controles negativos e outros 12 infectados com T. evansi. Nos dias 4 (n=6 por grupo) e 20 (n=6 por grupo) foram realizadas as coletas de sangue para obtenção do soro e amostras do córtex cerebral para mensuração dos níveis de ATP, ADP, AMP e adenosina. Neste estudo, foi constatado aumento das concentrações de ATP, AMP e adenosina no encéfalo e soro de ratos infectados com T. evansi nos dois períodos avaliados, com exceção dos níveis de adenosina que reduziram no dia 4 PI. Não houve alteração na concentração de ADP. Portanto, na infecção por T. evansi os componentes do sistema purinérgico pode ser alterados, podendo estar envolvido na resposta imunológica, na anemia e nos sinais neurológicos.
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Carlos, Carolina Dias. "Polimorfismos nos Receptores de Adenosina, suas Associações com Características Fisiopatológicas e Avaliação de Componentes na Biossíntese da Adenosina em Pacientes com Doença Falciforme." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/17/17135/tde-12062013-074600/.

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Na Anemia Falciforme em situações de baixa tensão de oxigênio, a hemoglobina mutante S (HbS) sofre polimerização promovendo a falcização das hemácias, que podem aderir ao endotélio vascular, causando a oclusão de vasos (VO) e isquemia tecidual (crises dolorosas) que caracterizam o quadro clínico da doença. Além disso, os pacientes falciformes apresentam outras manifestações clínicas como o priapismo, alterações ósseas, certas complicações pulmonares entre outros. Além das células eritróides, células endoteliais, leucócitos e plaquetas também desempenham um papel fundamental na fisiopatologia da anemia falciforme. A hidroxiuréia (HU), na anemia falciforme, aumenta a produção de hemoglobina fetal (HbF) em células eritróides, reduzindo a polimerização da HbS, diminuindo os sintomas clínicos dos pacientes. O aumento da HbF, no entanto, não implica necessariamente na melhora clínica, indicando desta forma a potencial ação da HU sobre outros processos. Estudos recentes vêm relacionando priapismo e asma com elevados níveis de adenosina. Devido a esta importância da adenosina relacionada a patologias comuns a AF, tivemos como objetivo identificar polimorfismos em genes de receptores de adenosina e na adenosina deaminase e verificar a possível associação entre as manifestações clínicas, além de investigar o papel da HU na modulação de marcadores envolvido na síntese e degradação da adenosina. Foram analisados diversos sítios polimórficos nos genes que codificam ADORA1, ADORA 2b, ADORA 3 e ADA, seguindo com a genotipagem em pacientes com AF, comparando afetados e não afetados. Em adição foi avaliada a expressão diferencial de mRNA de ADA pela HU em monócitos destes pacientes, comparando tratados e não tratados e também avaliamos por citometria de fluxo a modulação de marcadores de superfície CD39, CD73 e CD26, pela HU. As análises estatísticas foram realizadas utilizando os softwares GenePop 3.4 para análises de associação, cálculo do HWE, GraphPad Prism 5, Arlequin para identificação de desequilíbrio de ligação, haplótipos, heterozigozidade e SAS 9.13 para associação dos haplótipos as características. Os resultados mostraram que os pacientes sob tratamento com HU apresentaram um aumento da expressão de mRNA de ADA, aumento da expressão de CD26 em monócitos e diminuição de CD39 em linfócitos. Sem alterações significativas em relação a CD73. Encontramos também um aumento da freqüência do alelo T do SNP (rs1685103) presente no gene de ADORA 1 associado com pacientes afetados com síndrome torácica aguda. Apesar de não ter sido estatisticamente significante, concorda com dados da literatura. No gene ADORA 2B, verificamos associação do SNP 1007 C>T no desenvolvimento de STA indicando o alelo T como fator de risco e o alelo C para alterações ósseas. Para o SNP 968 G>T houve associação com alterações ósseas. Na análise haplotípica entre os SNPs 968 G>T e 1007 C>T encontramos associação dos haplótipos ht2 e ht3 com STA, como fator de risco, ht2 para hipertensão pulmonar. ht1 para priapismo, alterações ósseas e estenose/AVC. Os haplótipos formados pelos três SNPs 968 G>T, 1007 C>T e rs16851030, encontramos associação entre ht1, ht3 e ht4 entre os afetados com priapismo, caracterizando-o como haplótipo de risco e também ht1 e ht6 associados à estenose/AVC. Concluímos, que a hidroxiuréia participa na modulação da expressão da adenosina deaminase, de CD26 em monócitos e CD39 em linfócitos. Além disso, mostrou-se a importância de sítios polimórfico presente no gene ADORA 2B e ADORA1 envolvido na fisiopatologia das manifestações clínicas da doença falciforme. Associações dos SNPs em ADORA 1 e ADA, devem ser melhor estudados em um número maior de pacientes. A determinação destes polimorfismos associados com diferentes características clínicas pode levar a um melhor entendimento dos processos fisiopatológicos da anemia falciforme, levando à identificação de pacientes de risco, possibilitando um manejamento racional dos mesmos, em termos de cuidados específicos, ou mesmo à determinação de alvos para o desenvolvimento de terapias alternativas.
In sickle cell disease in low oxygen tension, mutant hemoglobin S (HbS) undergoes polymerization promoting sickling of red blood cells that can adhere to vascular endothelium, causing vessel occlusion (VO) and tissue ischemia (painful crises) that characterize the clinical disease. In addition, sickle cell patients have other clinical manifestations such as priapism, bone disorders, certain pulmonary complications among others. In addition to the erythroid cells, endothelial cells, white cells and platelets also play a key role in the pathophysiology of sickle cell anemia. Hydroxyurea (HU) in sickle cell anemia, increases the production of fetal hemoglobin (HbF) in erythroid cells, reducing the HbS polymerization, reducing the clinical symptoms of patients. The increase in HbF, however, does not necessarily imply clinical improvement, thus indicating the potential effects of HU on other processes. Recent studies relating asthma and priapism with high levels of adenosine. Due to this importance of adenosine-related pathologies common to AF, we aimed to identify gene polymorphisms in adenosine receptors and adenosine deaminase and verify the possible association between clinical manifestations, and to investigate the role of HU in the modulation of markers involved synthesis and degradation of adenosine. We analyzed several polymorphic sites in genes that encode ADORA1, ADORA 2b, 3 and ADORA ADA, according to the genotype in patients with AF, comparing affected and unaffected. In addition we assessed the differential expression of ADA mRNA by HU in monocytes of these patients, comparing treated and untreated, and also evaluated by flow cytometry modulation of surface markers CD39, CD73 and CD26 by HU. Statistical analysis was performed using the software GenePop 3.4 for association analysis, calculation of HWE, GraphPad Prism 5, Arlequin for identification of linkage disequilibrium, haplotypes, heterozygosity and SAS 9.13 for association of haplotypes features. The results showed that patients treated with HU showed an increase in mRNA expression of ADA, increased expression of CD26 on monocytes and decreased CD39 on lymphocytes. No significant changes in relation to CD73. We also found an increased frequency of allele T (SNP rs1685103) present in a gene associated with ADORA affected patients with acute chest syndrome. Although not statistically significant, agrees with literature data. ADORA 2B gene, we found association of the SNP 1007 C> T in the development of STA indicating the T allele as a risk factor for the C allele and bone changes. For the SNP 968 G> T was associated with bone disorders. In haplotype analysis between SNPs 968 G> T and 1007 C> T found association of haplotypes ht2 and HT3 with STA as a risk factor for pulmonary hypertension ht2. ht1 for priapism, stenosis and bone disorders / stroke. The three haplotypes formed by SNPs 968 G> T, 1007 C> T and rs16851030, we found association between ht1, HT3 and HT4 among those affected with priapism, characterizing it as a risk haplotype and also ht1 ht6 associated with renal and / AVC. We conclude that hydroxyurea participates in modulating the expression of adenosine deaminase of CD26 on monocytes and CD39 on lymphocytes. Moreover, he showed the importance of polymorphic sites in this gene and ADORA 2B ADORA1 involved in the pathophysiology of clinical manifestations of sickle cell disease. Associations of SNPs in ADORA 1 and ADA should be better studied in a larger number of patients. The determination of these polymorphisms associated with different clinical characteristics can lead to a better understanding of the pathophysiological processes of sickle cell anemia, leading to the identification of patients at risk, enabling a rational handling of the same in terms of specific care, or even the determination of targets for the development of alternative therapies.
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4

Abbott, C. M. "Adenosine deaminase in the wasted mouse." Thesis, University of Reading, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.374695.

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5

Molaudzi, Mulalo. "The usefulness of the adenosine deaminase assay for diagnosing tuberculosis pleuritis in immunocompromised patients at Dr George Mukhari tertiary laboratory, Pretoria." Thesis, University of Limpopo (Medunsa Campus), 2012. http://hdl.handle.net/10386/671.

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Thesis (MSc (Med)(Microbiology)) -- University of Limpopo, 2012.
Mycobacterium tuberculosis is the most common cause of death world-wide and its incidence has been steadily increasing, which is more evident when comparing the global tuberculosis (T8) incidence of 9.24 million in 2006 to 9.27 million cases in 2007. African countries are the second most affected by the epidemic and South Africa is among the 22 highest burden countries most affected by T8 with a very high number of cases relative to the total population. The early diagnosis of tuberculosis and screening of contacts is the cornerstone for controlling spread of active T8 infection. T8 diagnosis becomes even more challenging in patients with immunosuppression (for example in human immunodeficiency virus (HIV) infected), in the case of latent infection and extra pulmonary T8 such as pleural T8. The definitive diagnosis of pleural T8 depends on the demonstration of M. tuberculosis in sputum, pleural fluid and pleural biopsy. Although acid fast bacilli (AF8) microscopy is a rapid, inexpensive and relatively simple method, it has low sensitivity. The culture method is more sensitive than AF8 microscopy, detecting 25-37% of all pleural tuberculosis cases however it takes 4 to 8 weeks for a visible growth on a solid medium. Therefore it is important to find a rapid and reliable test for the diagnosis of pleural T8 particularly in developing countries such as South Africa where there is a high T8 incidence and HIV infection rate.
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Oliveira, Camila Belmonte. "Atividade das enzimas ntpdase, 5´-nucleotidase e adenosina deaminase em plaquetas de ratos infectados por Trypanosoma evansi." Universidade Federal de Santa Maria, 2010. http://repositorio.ufsm.br/handle/1/10079.

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
Nucleotide- and nucleoside-degrading enzymes are present in the surface of platelets, blood cells involved in clotting disturbances of Trypanosoma evansi-infected animals. Thus, this study was aimed at evaluating the activity of the enzymes NTPDase, 5 - nucleotidase and adenosine deaminase in platelets of rats experimentally infected by T. evansi. Animals were divided into four groups, according to the degree of parasitemia. Samples were collected at days 3 (group A: at the beginning of parasitemia), 5 (group B: high parasitemia) and 15 (group C: chronic infection). Group D (control group) was composed of non-infected animals. Blood samples with citrate as the anticoagulant were collected and used for platelet separation and enzymatic assays. NTPDase, 5 - nucleotidase and adenosine deaminase (ADA) activities were decreased (p<0.05) in platelets from rats of groups A and B, when compared to the control group. In group C, only NTPDase and 5 -nucleoside activities were decreased (p<0.001), observed by ADP and AMP hydrolysis. The correlation between platelet count and nucleotide and nucleoside hydrolysis was positive and statistically significant (p<0.05) in groups A and B. Platelet aggregation of all infected groups was decreased in comparison to the control group (p<0.05). Based upon the results, it is concluded that the alterations observed in the activity of the enzymes NTPDase, 5 -nucleotidase and adenosine deaminase in platelets of T. evansi-infected animals might be related to thrombocytopenia.
Nucleotide- and nucleoside-degrading enzymes are present in the surface of platelets, blood cells involved in clotting disturbances of Trypanosoma evansi-infected animals. Thus, this study was aimed at evaluating the activity of the enzymes NTPDase, 5 - nucleotidase and adenosine deaminase in platelets of rats experimentally infected by T. evansi. Animals were divided into four groups, according to the degree of parasitemia. Samples were collected at days 3 (group A: at the beginning of parasitemia), 5 (group B: high parasitemia) and 15 (group C: chronic infection). Group D (control group) was composed of non-infected animals. Blood samples with citrate as the anticoagulant were collected and used for platelet separation and enzymatic assays. NTPDase, 5 - nucleotidase and adenosine deaminase (ADA) activities were decreased (p<0.05) in platelets from rats of groups A and B, when compared to the control group. In group C, only NTPDase and 5 -nucleoside activities were decreased (p<0.001), observed by ADP and AMP hydrolysis. The correlation between platelet count and nucleotide and nucleoside hydrolysis was positive and statistically significant (p<0.05) in groups A and B. Platelet aggregation of all infected groups was decreased in comparison to the control group (p<0.05). Based upon the results, it is concluded that the alterations observed in the activity of the enzymes NTPDase, 5 -nucleotidase and adenosine deaminase in platelets of T. evansi-infected animals might be related to thrombocytopenia.
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Barros, Muriel Primon de. "Adenosina deaminase em trichomonas vaginalis : estudo da localização celular e do efeito de nutrientes essenciais." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2013. http://hdl.handle.net/10183/85309.

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Trichomonas vaginalis é o protozoário flagelado que parasita o trato urogenital humano causando a tricomonose, doença sexualmente transmissível (DST) de origem não viral mais comum no mundo. Durante a infecção a aquisição de nutrientes, como nucleotídeos púricos, pirimidínicos e ferro é essencial à sobrevivência do parasito. T. vaginalis não sintetiza de novo purinas e pirimidinas, dependendo de vias de salvação para aquisição destas moléculas. O ferro desempenha um papel crucial na patogenicidade da tricomonose, influenciando a expressão de múltiplos genes envolvidos na virulência. Nucleotídeos extracelulares, especialmente o ATP, são liberados em situações de estresse, anoxia ou injúria, atuando como sinalizadores pró-inflamatórios ao sistema imune. As enzimas NTPDase e ecto-5'-nucleotidase degradam ATP à adenosina, esta com ação anti-inflamatória. A enzima adenosina deaminase (ADA) degrada adenosina à inosina. A presença desta cadeia enzimática em T. vaginalis sugere a modulação das concentrações nucleotídeos/nucleosídeos durante a inflamação. A atividade da ADA foi caracterizada em T. vaginalis, porém há poucos relatos sobre a participação desta enzima na sobrevivência do parasito, bem como, a localização celular e o efeito de nutrientes essenciais na atividade enzimática e na expressão gênica. O estudo da localização da ADA em T. vaginalis foi realizado, indicando a presença da enzima na membrana celular e no citoplasma do trofozoíto. Avaliando-se o perfil da ADA de diferentes isolados de T. vaginalis em uma condição de limitação de soro bovino, o qual representa a fonte de adenosina aos trofozoítos, não se observou diferenças significativas na deaminação da adenosina à inosina. Na avaliação do efeito de diferentes fontes de ferro ou a privação deste cátion na atividade e na expressão gênica da ADA foi possível verificar uma diminuição da atividade e um aumento na expressão gênica após a privação do ferro, reforçando a hipótese que este elemento pode modular a atividade das enzimas envolvidas na sinalização purinérgica. Os resultados obtidos nesta dissertação permitem a avaliação de importantes aspectos da ADA, contribuindo para o melhor entendimento do sistema purinérgico em T. vaginalis e seu papel no estabelecimento e manutenção da infecção e consequente sobrevivência do parasito.
Trichomonas vaginalis is a flagellate protozoan that parasitizes the urogenital human tract causing trichomonosis, the non-viral sexually transmitted disease (STD) most common in the world. During infection the acquisition of nutrients such as purine and pyrimidine nucleotides, and iron is essential to the parasite survival. T. vaginalis lacks de novo purines and pyrimidines synthesis depending on the salvation pathway for the acquisition of these molecules. Iron plays a crucial role in trichomonosis pathogenesis, influencing the expression of multiple genes involved in virulence. Extracellular nucleotides, especially ATP, are released during stress, injury or anoxia, acting as a pro-inflammatory signaling to the immune system. The enzymes NTPDase and ecto-5'-nucleotidase degrade ATP to adenosine with anti-inflammatory action. The adenosine deaminase (ADA) enzyme degrades adenosine to inosine. The presence of this enzymatic chain in T. vaginalis suggests the modulation of nucleotides/nucleosides concentrations during inflammation. The ADA activity was characterized in T. vaginalis, but there are few reports on the participation of this enzyme in the parasite survival, as well as the cellular localization and the effect of essential nutrients on enzyme activity and gene expression. The study of ADA localization in T. vaginalis was performed, indicating the presence of the enzyme on trophozoite cell membrane and cytoplasm. Evaluating the ADA profile in different T. vaginalis isolates in bovine serum limitation condition, which is the source of adenosine for the trophozoites, no significant differences were observed in the deamination of adenosine to inosine. Regarding the effect of different iron sources or iron deprivation in activity and gene expression of ADA, it was observed a decrease in activity and an increase in gene expression after iron deprivation, reinforcing the hypothesis that this element can modulate the activity of enzymes involved in the purinergic signaling. The results obtained in this study allow the assessment of important aspects of ADA, contributing to a better understanding of the purinergic system in T. vaginalis and its role in the establishment and maintenance of infection and consequent survival of the parasite.
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Chielle, Eduardo Ottobelli. "EFEITO DA RUTINA SOBRE A ATIVIDADE DA ADENOSINA DEAMINASE EM RATOS DIABÉTICOS." Universidade Federal de Santa Maria, 2012. http://repositorio.ufsm.br/handle/1/5921.

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Diabetes mellitus (DM) is a metabolic disorder of multiple etiology characterized by chronic hyperglycemia resulting from deficiency of insulin production and/or action. This state of hyperglycemia may cause a variety of cardiovascular, renal, neurological and eye complications. Adenosine deaminase (ADA) is an important enzyme responsible for regulation the levels of adenosine (ado) an important component of the system purinergic nucleoside. Changes in ADA activity has been demonstrated in several diseases, including DM. The Rutin (RT) is an abundant polyphenolic flavonoid found in food that exhibits multiple pharmacological activities including antibacterial, antitumoural, vasodilator and hepatoprotective activities. The objective of this study was to investigate the effect of RT on the activity of ADA in serum, tissues and biochemical parameters in models of diabetes induced by streptozotocin (STZ). Diabetes was induced in rats by an intraperitoneal injection of streptozotocin (STZ). RT (100 mg/kg/day) and glibenclamide (10mg/kg/day) were administered for 30 days, except for control groups (non diabetic and diabetic). Six groups of rats were used in the study and grouped based on fasting blood glucose levels after diabetes induction. The results showed an increase in ADA activity in serum and liver of diabetic rats, like transaminases (AST, ALT), -glutamyltransferase (-GT) and glucose. The RT at a concentration of 100 mg/kg was able to reduce the ADA activity in serum and liver tissue when compared with the diabetic control. The protective effect of RT was also observed increases the activity of enzymes ALT and -GT. Significant reductions were also observed in total cholesterol and LDL-cholesterol as well as in blood glucose levels in the diabetic group treated with RT. The results suggest that RT can improve hyperglycemia and hyperlipidemia, and restoring damaged liver function, as well as prevents the increase in ADA activity in serum and liver tissue on diabetic rats treated with this flavonoid.
O Diabetes mellitus (DM) é uma disfunção metabólica de múltipla etiologia caracterizado por hiperglicemia crônica resultante da deficiência da produção e/ou ação da insulina. Esse estado de hiperglicemia pode provocar uma série de complicações cardiovasculares, renais, neurológicas e oculares. A Adenosina deaminase (ADA) é uma importante enzima responsável por regular os níveis de adenosina (ado), um importante nucleosídeo componente do sistema purinérgico. Alterações na atividade da ADA têm sido demonstradas em várias doenças, incluindo o DM. A rutina (RT) é um flavonoide polifenólico abundante nos alimentos que exibe múltiplas atividades farmacológicas como atividade antibacteriana, antitumoral, vasodilatadora e hepatoprotetora. O objetivo deste estudo foi verificar o efeito da RT sobre a atividade da ADA sérica e tecidual e parâmetros bioquímicos em modelos de diabetes induzidos por estreptozotocina (STZ). O diabetes foi induzido através de injeção única intraperitoneal (i.p.) de 55 mg/kg de STZ. A RT (100 mg / kg / dia) e a glibenclamida (10mg/kg/dia) foram administradas durante 30 dias, com exceção dos grupos controles (não diabéticos e diabéticos). Seis grupos de ratos foram utilizados no estudo e agrupados com base nos níveis de glicose em jejum após a indução de diabetes. Os resultados demonstraram um aumento na atividade da ADA no soro e no fígado de ratos diabéticos, assim como das transaminases (AST, ALT), -glutamiltransferase (-GT) e glicose. A RT na concentração de 100 mg/kg foi capaz de reduzir a atividade sérica e em tecido hepático da ADA quando comparado com o controle. O efeito protetor da RT também foi observado sobe a atividade das enzimas ALT e -GT. Reduções significativas foram observadas no colesterol total e LDL-colesterol, bem como, na concentração sérica de glicose no grupo diabético tratado com RT. Os resultados sugerem que a RT pode melhorar a hiperglicemia e dislipidemia, restabelecer danos à função hepática, bem como é capaz de prevenir o aumento da atividade da ADA no soro e no fígado de ratos diabéticos tratados com este flavonoide.
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Ribeiro, Cristina Alves. "Amplificação, clonagem, expressão e purificação da enzima adenosina deaminase (ADA) de Tripanosoma evansi." Universidade do Estado de Santa Catarina, 2016. http://tede.udesc.br/handle/handle/2366.

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UNIEDU
FUMDES
T. evansi causes a highly pathogenic disease in horses popularly known as "Surra" or "Mal das Cadeiras". The Pantanal (Brazil) outbreaks are recorded due to the large population of horses. To date there are no effective treatment methods causing major damage to livestock. Trypanosomes present themselves vulnerable in relation to the metabolism of purines as these organisms do not have the pathway “De novo” of meeting their requirements through the rescue of preformed bases and demonstrate complete dependence of purines of their hosts. Among the components of this system point out that adenosine has its concentration controlled by the enzyme adenosine deaminase (ADA). The objectives of this study were to amplify, clone and sequence the ADA gene from T. evansi DNA samples and express the recombinant protein ADA. The coding region of the ADA gene was amplified from genomic DNA of T. evansi and yielded a sequence of 1857 bp showed high degree of similarity (95%) ADA T. brucei. This region was cloned into the pGEM-T vector Easy®. After digestion of construct pGEM: ADA fragments were cloned into expression vector pET30. The expression analysis by SDS-PAGE demonstrated that the temperature of 18ºC for 24 hours and 0,05 mM IPTG induction was the most effective indicating molecular mass of approximately 68 kDa. The Western blot analysis detected the ADA enzyme in the protein extract of T. evansi only in the insoluble fraction. The protein was solubilized and purified by affinity chromatography. Through these results the presence of ADA in T. evansi was confirmed. tests will be performed to detect the enzymatic activity of ADA. Their study can contribute to the development of new chemotherapeutic agents and the development of specific inhibitors for the ADA
T. evansi causa uma doença altamente patogênica em equídeos popularmente conhecida como “Surra” ou “Mal das Cadeiras”. No Pantanal (Brasil) surtos são registrados devido à grande população de equinos. Até o presente momento não existem métodos de tratamento eficazes gerando grandes prejuízos à pecuária. Os tripanossomas apresentam-se vulneráveis em relação ao metabolismo das purinas pois estes organismos não contam com a via De novo satisfazendo suas exigências por meio do salvamento das bases pré-formadas e demonstram completa dependência das purinas dos seus hospedeiros. Entre os componentes desse sistema destacamos a adenosina que tem sua concentração controlada pela enzima adenosina deaminase (ADA). Os objetivos deste estudo foram amplificar, clonar e sequenciar o gene ADA a partir de amostras do DNA de T. evansi e expressar a proteína recombinante ADA. A região codificadora do gene da enzima ADA foi amplificada a partir do DNA genômico de T. evansi e originou uma sequência de 1857 bp que apresentou alto grau de similaridade (95%) com a enzima ADA de T. brucei. Essa região foi clonada no vetor pGEM-T Easy®. Após a digestão da construção pGEM:ADA, os fragmentos foram clonados em vetor de expressão pET30. A análise da expressão através do SDS-PAGE demonstrou que a temperatura de 18ºC por 24 horas e indução com IPTG 0.05 mM foi a mais eficiente indicando massa molecular de aproximadamente 68 kDa. A análise Western-Blot detectou a enzima ADA no extrato proteico de T. evansi apenas na fração insolúvel. A proteína foi solubilizada e purificada por meio da cromatografia de afinidade. SDS-PAGE e o Western-blot confirmaram a eficiência destes protocolos. Através desses resultados a presença da enzima ADA em T. evansi foi confirmada. Seu estudo pode contribuir para o desenvolvimento de novos agentes quimioterápicos e o desenvolvimento de agentes inibidores específicos para ADA
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Junqueira, Ana FlÃvia Torquato de AraÃjo. "Estudo do efeito do inibidor da enzima adenosina desaminase, EHNA, sobre a enterite induzida pela toxina a do Clostridium difficile em alÃa ileal isolada de camundongos." Universidade Federal do CearÃ, 2008. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=1305.

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Conselho Nacional de Desenvolvimento CientÃfico e TecnolÃgico
O Clostridium difficile tem como principal fator de virulÃncia a toxina A (TxA), a qual provoca inflamaÃÃo e destruiÃÃo tecidual aguda em intestinos de animais experimentais e de pacientes com a doenÃa induzida por esta bactÃria. Em locais de injÃria tecidual, adenosina à produzida em altas concentraÃÃes, onde exerce uma sÃrie de efeitos antiinflamatÃrios, limitados por sua rÃpida degradaÃÃo pela enzima adenosina desaminase. O objetivo deste trabalho foi investigar o efeito da inibiÃÃo da enzima adenosina desaminase pelo EHNA (eritro-9-(2-hidrÃxi-3-nonil)-adenina) sobre a enterite induzida pela TxA do C. difficile em alÃa ileal de camundongos. Para isto, injetamos EHNA (90 μmol/kg) ou PBS i.p. 30 minutos antes da administraÃÃo de TxA (10 a 100 μg) ou PBS na alÃa ileal isolada. Os animais foram sacrificados 3 horas depois da induÃÃo da enterite e as alÃas foram retiradas para estudo. As razÃes peso/comprimento da alÃa e volume de secreÃÃo/comprimento da alÃa foram calculadas e amostras de tecido foram coletadas para histopatologia, dosagem de atividade de mieloperoxidase (MPO), dosagem de TNF-α, IL-1β e IL-10 por ELISA, imunohistoquÃmica para TNF-α, IL-1β, NOS induzÃvel e PTX3, e PCR para TNF-α, IL-1β e PTX3. A injeÃÃo de TxA (10 a 100 μg) nas alÃas ileais aumentou significativamente (p<0,05) as razÃes peso/comprimento da alÃa e volume de secreÃÃo/comprimento da alÃa com resultados consistentes a partir de 50 μg. A TxA promoveu significativa (p<0,05) destruiÃÃo tecidual, edema, infiltraÃÃo de cÃlulas inflamatÃrias, aumento das citocinas TNF-α e IL-1β, e elevaÃÃo de iNOS e PTX3. Todos esses parÃmetros foram significativamente revertidos com o uso do EHNA (p<0,05). Em adiÃÃo, a TxA nÃo alterou os nÃveis de IL-10 em relaÃÃo ao controle, mas o prÃ-tratamento com EHNA promoveu uma elevaÃÃo nos nÃveis desta citocina. Assim, concluÃmos que na enterite induzida pela TxA em camundongos o EHNA demonstrou um potente efeito antiinflamatÃrio, reduzindo consideravelmente a lesÃo tecidual, a migraÃÃo neutrofÃlica, a expressÃo e os nÃveis de citocinas prÃinflamatÃrias (TNF-α, IL-1β) e produzindo um aumento nos nÃveis de IL-10. AlÃm disso, a administraÃÃo de TxA induziu um aumento na expressÃo da proteÃna PTX3 e no nÃmero de cÃlulas imunomarcadas para iNOS no tecido ileal, ambos revertidos pelo EHNA
The main factor of virulence in Clostridium difficile is toxin A (TxA), which can induce inflammation and acute tissue injury in the bowels of animals and humans affected by this organism. The high concentration of adenosine generated upon injury produces a number of antiinflammatory effects limited by rapid degradation by adenosine deaminase. The objective of this study was to determine the effect of EHNA (erythro-9-(2-hydroxy-3-nonyl)-adenine) inhibition of adenosine deaminase upon TxA-induced ileal loop enteritis in mice. EHNA (90 μmol/kg) or PBS was injected i.p. 30 minutes prior to TxA (10-100 μg) or PBS instillation into the ligated ileal loop. The animals were euthanized 3 hours after enteritis induction and the ileal loops were retrieved for analysis. The weight/length ratio and the secretion volume/length ratio were calculated and tissue samples were submitted to histopathological study, myeloperoxidase assay (MPO), measurement of TNF-α, IL-1β and IL-10 levels with ELISA, immunohistochemical tests for TNF-α, IL-1β, inducible NOS and PTX3, and PCR assay for TNF-α, IL-1β and PTX3. The instillation of TxA (10-100 μg) into the ileal loop significantly increased (p<0.05) the weight/length ratio and the secretion volume/length ratio with consistent results above 50 μg. TxA induced a significant amount (p<0.05) of histological damage, edema and inflammatory cell infiltration and increased the production of TNF-α, IL-1β, iNOS and PTX3. All changes were significantly reverted by treatment with EHNA (p<0.05). Moreover, IL-10 levels remained unchanged in animals treated with TxA, but increased in animals receiving EHNA. In conclusion, in mice with TxA-induced enteritis EHNA produced considerable antiinflammatory effects, reducing tissue injury, neutrophil migration, the expression and levels of proinflammatory cytokines (TNF-α and IL-1β) and producing an increase in IL-10 levels. In addition, TxA instillation increased PTX3 expression and the number of cells immunolabeled for iNOS in the ileal tissue, both of which were reverted by EHNA
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Books on the topic "Adenosine deaminases"

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Adenosine deaminases acting on RNA (ADARs) and A-to-I editing. Heidelberg: Springer, 2012.

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Samuel, Charles E., ed. Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-22801-8.

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L, Tritsch George, New York Academy of Sciences., and Conference on Adenosine Deaminase in Disorders of Purine Metabolism and in Immune Deficiency (1984 : New York, N.Y.), eds. Adenosine deaminase in disorders of purine metabolism and in immune deficiency. New York, N.Y: New York Academy of Sciences, 1985.

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Chu, Peter Pui Tak. Retroviral-mediated human adenosine deaminase gene transfer into human hematopoietic progenitor and stem cells. Ottawa: National Library of Canada, 1995.

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Samuel, Charles E. Adenosine Deaminases Acting on RNA and A-to-I Editing. Springer, 2011.

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Samuel, Charles E. Adenosine Deaminases Acting on RNA and A-to-I Editing. Springer, 2014.

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Geha, Raif, and FRED Rosen. Case Studies in Immunology: Adenosine Deaminase Deficiency. W.W. Norton & Company, 2010. http://dx.doi.org/10.4324/9780203853566.

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Geha, Raif, and Fred Rosen. Case Studies in Immunology : Adenosine Deaminase Deficiency: A Clinical Companion. Norton & Company, Incorporated, W. W., 2010.

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Geha, Raif, and Fred Rosen. Case Studies in Immunology : Adenosine Deaminase Deficiency: A Clinical Companion. Norton & Company, Incorporated, W. W., 2010.

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Geha, Raif, and Fred Rosen. Case Studies in Immunology : Adenosine Deaminase Deficiency: A Clinical Companion. Norton & Company, Incorporated, W. W., 2010.

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Book chapters on the topic "Adenosine deaminases"

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Carter, Charles W. "Nucleoside Deaminases for Cytidine and Adenosine: Comparison with Deaminases Acting on RNA." In Modification and Editing of RNA, 363–75. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555818296.ch20.

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Frazier, Ronald B., and Pang Fai Ma. "A Study of Adenosine Deaminases in Human Sera." In Purine and Pyrimidine Metabolism in Man V, 267–70. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_43.

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Jantsch, Michael F., and Marie Öhman. "RNA Editing by Adenosine Deaminases that Act on RNA (ADARs)." In Nucleic Acids and Molecular Biology, 51–84. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-73787-2_3.

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Morse, Daniel P. "Identification of Substrates for Adenosine Deaminases That Act on RNA." In RNA Interference, Editing, and Modification, 199–218. Totowa, NJ: Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-775-0:199.

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Schomburg, Dietmar, and Margit Salzmann. "Adenosine deaminase." In Enzyme Handbook 4, 999–1003. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_199.

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Agarwal, Ram P. "Adenosine Deaminase." In Methods Used in Adenosine Research, 109–25. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-4886-3_6.

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Schomburg, Dietmar, and Margit Salzmann. "Adenosine-phosphate deaminase." In Enzyme Handbook 4, 1059–62. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-84437-9_212.

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Scharnagl, Hubert, Winfried März, Markus Böhm, Thomas A. Luger, Federico Fracassi, Alessia Diana, Thomas Frieling, et al. "Adenosine Deaminase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 36–37. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_52.

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Belmont, J. W., J. Henkel-Tigges, K. Wager-Smith, S. M. W. Chang, and C. Th Caskey. "Adenosine Deaminase Gene Transfer." In Human Genetics, 639–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71635-5_88.

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Geiger, Jonathan D., and James I. Nagy. "Adenosine Deaminase and [3H] Nitrobenzylthioinosine as Markers of Adenosine Metabolism and Transport in Central Purinergic Systems." In Adenosine and Adenosine Receptors, 225–88. Totowa, NJ: Humana Press, 1990. http://dx.doi.org/10.1007/978-1-4612-4504-9_7.

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Conference papers on the topic "Adenosine deaminases"

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Pereira, Flávio Ribeiro, Blanca Helena Rios Gomes Bica, Maria Pompeya Olmedo de Lopes de Figueiredo, Rodrigo Lousada, Virginia de Souza Guimarães Merat, Dimona Carvalho Vivas Amado, and Mariana Ferreira Vieira. "Deficiency of Adenosine Deaminase 2: a rare disease." In XXXIX Congresso Brasileiro de Reumatologia. Sociedade Brasileiro de Reumatologia, 2022. http://dx.doi.org/10.47660/cbr.2022.2212.

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Sharoyan, S., L. Karapetyan, R. Harutyunyan, S. Mardanyan, and A. Antonyan. "SAT0051 Citrullination of adenosine deaminase isoforms in rheumatoid arthritis." In Annual European Congress of Rheumatology, 14–17 June, 2017. BMJ Publishing Group Ltd and European League Against Rheumatism, 2017. http://dx.doi.org/10.1136/annrheumdis-2017-eular.1433.

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Tofovic, Stevan P., Victor Bilan, Edwin K. Jackson, and OLGA Rafikova. "Role Of Plasma Adenosine Deaminase In Hemolysis-Induced Pulmonary Hypertension." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6335.

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PARENTE, JOSÉ SÁVIO MENEZES, AMANDA VIRGINIA BATISTA CAVALCANTE, and THAÍS GUERREIRO JORGE ROCHA. "POLYARTERITIS NODOSA OR DEFICIENCY OF ADENOSINE DEAMINASE 2?: CASE REPORT." In 36º Congresso Brasileiro de Reumatologia. São Paulo: Editora Blucher, 2019. http://dx.doi.org/10.5151/sbr2019-207.

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Cho, Yu Ji, Jong Deog Lee, Eun Young Yun, Young Sil Hwang, Jung Eun Ma, Yi Yeong Jeong, Ho Cheol Kim, and Hyeon Sik Kim. "Clinical Characteristics Of Tuberculous Pleurisy Patients With Low Adenosine Deaminase Levels." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1781.

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Kiryukhina, Larisa, Marina Dyakova, and Diljara Esmedlyaeva. "Adenosine deaminase in the COPD pathogenesis in patients with pulmonary tuberculosis." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa2718.

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Trajcevska, Mirjana, and Aleksandar Sandevski. "Activity of lysozyme and adenosine deaminase in patients with pulmonary tuberculosis." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa4762.

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Londoño-R, Luz Marina, Jessica Cowell, Lin Wang, Qiping Zhao, Lei Huang, Chris Thanos, Michael J. LaBarre, Xiaoming Li, and Caglar Cekic. "Abstract 1755: PEGylated adenosine deaminase (ADA2) prevents adenosine-mediated increase in tumor growth and improves antitumor immune responses." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1755.

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Serra, Sara, Cinzia Bologna, Luz Londono, Lin Wang, Michael Shepard, Sanna Rosengren, Christopher Thanos, and Silvia Deaglio. "Abstract 5583: Pegylated adenosine deaminase 2 (PEG-ADA2) abrogates the cytoprotective effects of adenosine against chronic lymphocytic leukemia cells." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-5583.

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Xie, Jing, Hua Wei, and Xiaoxing Xiang. "AB1111 RELATIONSHIP BETWEEN SERUM ADENOSINE DEAMINASE LEVELS AND DISEASE ACTIVITY IN AUTOIMMUNE HEPATITIS." In Annual European Congress of Rheumatology, EULAR 2019, Madrid, 12–15 June 2019. BMJ Publishing Group Ltd and European League Against Rheumatism, 2019. http://dx.doi.org/10.1136/annrheumdis-2019-eular.3679.

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