Relevant bibliographies by topics / DDAH1

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Academic literature on the topic 'DDAH1'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "DDAH1"

1

Ivashchenko, Christine Y., Benjamin T. Bradley, Zhaohui Ao, James Leiper, Patrick Vallance, and Douglas G. Johns. "Regulation of the ADMA-DDAH system in endothelial cells: a novel mechanism for the sterol response element binding proteins, SREBP1c and -2." American Journal of Physiology-Heart and Circulatory Physiology 298, no. 1 (January 2010): H251—H258. http://dx.doi.org/10.1152/ajpheart.00195.2009.

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Asymmetric dimethylarginine (ADMA) has been implicated in the progression of cardiovascular disease as an endogenous inhibitor of nitric oxide synthase. The regulation of dimethylarginine dimethylaminohydrolase (DDAH), the enzyme responsible for metabolizing ADMA, is poorly understood. The transcription factor sterol response element binding protein (SREBP) is activated by statins via a reduction of membrane cholesterol content. Because the promoters of both DDAH1 and DDAH2 isoforms contain sterol response elements, we tested the hypothesis that simvastatin regulates DDAH1 and DDAH2 transcription via SREBP. In cultured endothelial cells, simvastatin increased DDAH1 mRNA expression compared with vehicle. In an ADMA loading experiment, simvastatin treatment resulted in a decrease in ADMA content, an indication of increased DDAH activity. The knockdown of SREBP1c protein led to an increase in DDAH1 mRNA expression and activity, whereas the knockdown of SREBP2 led to a decrease in DDAH1 mRNA expression. The role of SREBP2 in the activation of the DDAH1 was supported by chromatin immunoprecipitation studies demonstrating increased binding of SREBP2 to the DDAH1 promoter upon simvastatin stimulation. These data indicate that SREBP1c might act as a repressor and SREBP2 as an activator of DDAH transcription and activity. This study describes a novel mechanism of reciprocal regulation by the SREBP family members of the DDAH-ADMA system, which represents a potential link between cellular cholesterol content and endothelial dysfunction observed in cardiovascular disease.
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Dayal, Sanjana, Roman N. Rodionov, Erland Arning, Teodoro Bottiglieri, Masumi Kimoto, Daryl J. Murry, John P. Cooke, Frank M. Faraci, and Steven R. Lentz. "Tissue-specific downregulation of dimethylarginine dimethylaminohydrolase in hyperhomocysteinemia." American Journal of Physiology-Heart and Circulatory Physiology 295, no. 2 (August 2008): H816—H825. http://dx.doi.org/10.1152/ajpheart.01348.2007.

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Asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide (NO) synthase, has been proposed to be a mediator of vascular dysfunction during hyperhomocysteinemia. Levels of ADMA are regulated by dimethylarginine dimethylaminohydrolase (DDAH). Using both in vitro and in vivo approaches, we tested the hypothesis that hyperhomocysteinemia causes downregulation of the two genes encoding DDAH ( Ddah1 and Ddah2). In the MS-1 murine endothelial cell line, the addition of homocysteine decreased NO production but did not elevate ADMA or alter levels of Ddah1 or Ddah2 mRNA. Mice heterozygous for cystathionine β-synthase ( Cbs) and their wild-type littermates were fed either a control diet or a high-methionine/low-folate (HM/LF) diet to produce varying degrees of hyperhomocysteinemia. Maximal relaxation of the carotid artery to the endothelium-dependent dilator acetylcholine was decreased by ∼50% in Cbs+/− mice fed the HM/LF diet compared with Cbs+/+ mice fed the control diet ( P < 0.001). Compared with control mice, hyperhomocysteinemic mice had lower levels of Ddah1 mRNA in the liver ( P < 0.001) and lower levels of Ddah2 mRNA in the liver, lung, and kidney ( P < 0.05). Downregulation of DDAH expression in hyperhomocysteinemic mice did not result in an increase in plasma ADMA, possibly due to a large decrease in hepatic methylation capacity ( S-adenosylmethionine-to- S-adenosylhomocysteine ratio). Our findings demonstrate that hyperhomocysteinemia causes tissue-specific decreases in DDAH expression without altering plasma ADMA levels in mice with endothelial dysfunction.
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Sasaki, Akihito, Shouzaburoh Doi, Shuki Mizutani, and Hiroshi Azuma. "Roles of accumulated endogenous nitric oxide synthase inhibitors, enhanced arginase activity, and attenuated nitric oxide synthase activity in endothelial cells for pulmonary hypertension in rats." American Journal of Physiology-Lung Cellular and Molecular Physiology 292, no. 6 (June 2007): L1480—L1487. http://dx.doi.org/10.1152/ajplung.00360.2006.

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Nitric oxide (NO) has been suggested to play a key role in the pathogenesis of pulmonary hypertension (PH). To determine which mechanism exists to affect NO production, we examined the concentration of endogenous nitric oxide synthase (NOS) inhibitors and their catabolizing enzyme dimethylarginine dimethylaminohydrolase (DDAH) activity and protein expression (DDAH1 and DDAH2) in pulmonary artery endothelial cells (PAECs) of rats given monocrotaline (MCT). We also measured NOS and arginase activities and NOS protein expression. Twenty-four days after MCT administration, PH and right ventricle (RV) hypertrophy were established. Endothelium-dependent, but not endothelium-independent, relaxation and cGMP production were significantly impaired in pulmonary artery specimens of MCT group. The constitutive NOS activity and protein expression in PAECs were significantly reduced in MCT group, whereas the arginase, which shares l-arginine as a common substrate with NOS, activity was significantly enhanced in PAECs of MCT group. The contents of monomethylarginine (MMA) and asymmetric dimethylarginine (ADMA), but not symmetric dimethylarginine (SDMA), were increased in PAECs of MCT group. The DDAH activity and DDAH1, but not DDAH2, protein expression were significantly reduced in PAECs of MCT group. These results suggest that the impairment of cGMP production as a marker of NO production is possibly due to the blunted endothelial NOS activity resulting from the downregulation of endothelial NOS protein, accumulation of endogenous NOS inhibitors, and accelerated arginase activity in PAECs of PH rats. The decreased overall DDAH activity accompanied by the downregulation of DDAH1 would bring about the accumulation of endogenous NOS inhibitors.
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Wang, Zhong, Shaoze Chen, Lina Zhang, Guilin Lu, Chengming Zhou, Dao Wen Wang, Li Wang, Bayinbate Badengmu, Zhihong Zhai, and Lian Qin. "Association between variation in the genes DDAH1 and DDAH2 and hypertension among Uygur, Kazakh and Han ethnic groups in China." Sao Paulo Medical Journal 134, no. 3 (January 19, 2016): 205–10. http://dx.doi.org/10.1590/1516-3180.2015.01150108.

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CONTEXT AND OBJECTIVE: Dimethylarginine dimethylaminohydrolase enzymes (DDAH), which are encoded by the genes DDAH1 and DDAH2, play a fundamental role in maintaining endothelial function. We conducted a case-control study on a Chinese population that included three ethnic groups (Han, Kazakh and Uygur), to systemically investigate associations between variations in the genes DDAH1 and DDAH2 and hypertension. DESIGN AND SETTING: Experimental study at the Department of Internal Medicine and Genetic Diagnosis, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology. METHODS: This case-control study included 1,224 patients with hypertension and 967 healthy unrelated individuals as controls. DDAH1 -396 4N (GCGT) del>ins, rs3087894, rs805304 and rs9267551 were genotyped using the TaqMan 5' nuclease assay. RESULTS: The G/C genotype of rs3087894 in DDAH1 was a risk factor for hypertension in the Kazakh group in the co-dominant model (G/C versus G/G) (OR 1.39; 95% CI: 1.02-1.88; P < 0.05), with the same result in the dominant model (G/C + C/C versus G/G) (OR 1.38; 95% CI: 1.03-1.84; P < 0.05). In contrast, the C/C genotype of rs3087894 seemed to be a protective factor against hypertension in the Uygur group in the recessive model (C/C versus G/G + G/C) (OR 0.62; 95% CI: 0.39- 0.97; P < 0.05). Similar findings for rs3087894 were also observed after adjusting the variable for the age covariate. CONCLUSION: Our results indicated that the C-allele of rs3087894 in DDAH1 was a risk factor for hypertension in the Kazakh group but a protective factor in the Uygur group.
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Jarzebska, Natalia, Arduino A. Mangoni, Jens Martens-Lobenhoffer, Stefanie M. Bode-Böger, and Roman N. Rodionov. "The Second Life of Methylarginines as Cardiovascular Targets." International Journal of Molecular Sciences 20, no. 18 (September 17, 2019): 4592. http://dx.doi.org/10.3390/ijms20184592.

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Endogenous methylarginines were proposed as cardiovascular risk factors more than two decades ago, however, so far, this knowledge has not led to the development of novel therapeutic approaches. The initial studies were primarily focused on the endogenous inhibitors of nitric oxide synthases asymmetric dimethylarginine (ADMA) and monomethylarginine (MMA) and the main enzyme regulating their clearance dimethylarginine dimethylaminohydrolase 1 (DDAH1). To date, all the screens for DDAH1 activators performed with the purified recombinant DDAH1 enzyme have not yielded any promising hits, which is probably the main reason why interest towards this research field has started to fade. The relative contribution of the second DDAH isoenzyme DDAH2 towards ADMA and MMA clearance is still a matter of controversy. ADMA, MMA and symmetric dimethylarginine (SDMA) are also metabolized by alanine: glyoxylate aminotransferase 2 (AGXT2), however, in addition to methylarginines, this enzyme also has several cardiovascular protective substrates, so the net effect of possible therapeutic targeting of AGXT2 is currently unclear. Recent studies on regulation and functions of the enzymes metabolizing methylarginines have given a second life to this research direction. Our review discusses the latest discoveries and controversies in the field and proposes novel directions for targeting methylarginines in clinical settings.
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Krzystek-Korpacka, Małgorzata, Mariusz G. Fleszar, Iwona Bednarz-Misa, Łukasz Lewandowski, Izabela Szczuka, Radosław Kempiński, and Katarzyna Neubauer. "Transcriptional and Metabolomic Analysis of L-Arginine/Nitric Oxide Pathway in Inflammatory Bowel Disease and Its Association with Local Inflammatory and Angiogenic Response: Preliminary Findings." International Journal of Molecular Sciences 21, no. 5 (February 28, 2020): 1641. http://dx.doi.org/10.3390/ijms21051641.

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L-arginine/nitric oxide pathway in Crohn’s disease (CD) and ulcerative colitis (UC) is poorly investigated. The aim of current study is to quantify pathway serum metabolites in 52 CD (40 active), 48 UC (33 active), and 18 irritable bowel syndrome patients and 40 controls using mass spectrometry and at determining mRNA expression of pathway-associated enzymes in 91 bowel samples. Arginine and symmetric dimethylarginine decreased (p < 0.05) in active-CD (129 and 0.437 µM) compared to controls (157 and 0.494 µM) and active-UC (164 and 0.52 µM). Citrulline and dimethylamine increased (p < 0.05) in active-CD (68.7 and 70.9 µM) and active-UC (65.9 and 73.9 µM) compared to controls (42.7 and 50.4 µM). Compared to normal, CD-inflamed small bowel had downregulated (p < 0.05) arginase-2 by 2.4-fold and upregulated dimethylarginine dimethylaminohydrolase (DDAH)-2 (1.5-fold) and arginine N-methyltransferase (PRMT)-2 (1.6-fold). Quiescent-CD small bowel had upregulated (p < 0.05) arginase-2 (1.8-fold), DDAH1 (2.9-fold), DDAH2 (1.5-fold), PRMT1 (1.5-fold), PRMT2 (1.7-fold), and PRMT5 (1.4-fold). Pathway enzymes were upregulated in CD-inflamed/quiescent and UC-inflamed colon as compared to normal. Compared to inflamed, quiescent CD-colon had upregulated DDAH1 (5.7-fold) and ornithine decarboxylase (1.6-fold). Concluding, the pathway is deregulated in CD and UC, also in quiescent bowel, reflecting inflammation severity and angiogenic potential. Functional analysis of PRMTs and DDAHs as potential targets for therapy is warranted.
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Jacobi, Johannes, Renke Maas, Nada Cordasic, Kilian Koch, Roland E. Schmieder, Rainer H. Böger, and Karl F. Hilgers. "Role of asymmetric dimethylarginine for angiotensin II-induced target organ damage in mice." American Journal of Physiology-Heart and Circulatory Physiology 294, no. 2 (February 2008): H1058—H1066. http://dx.doi.org/10.1152/ajpheart.01103.2007.

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The aim of the present study was to investigate the role of the endogenous nitric oxide synthase inhibitor asymmetric dimethylarginine (ADMA) and its degrading enzyme dimethylarginine dimethylaminohydrolase (DDAH) in angiotensin II (ANG II)-induced hypertension and target organ damage in mice. Mice transgenic for the human DDAH1 gene (TG) and wild-type (WT) mice (each, n = 28) were treated with 1.0 μg·kg−1·min−1 ANG II, 3.0 μg·kg−1·min−1 ANG II, or phosphate-buffered saline over 4 wk via osmotic minipumps. Blood pressure, as measured by tail cuff, was elevated to the same degree in TG and WT mice. Plasma levels of ADMA were lower in TG than WT mice and were not affected after 4 wk by either dose of ANG II in both TG and WT animals. Oxidative stress within the wall of the aorta, measured by fluorescence microscopy using the dye dihydroethidium, was significantly reduced in TG mice. ANG II-induced glomerulosclerosis was similar between WT and TG mice, whereas renal interstitial fibrosis was significantly reduced in TG compared with WT animals. Renal mRNA expression of protein arginine methyltransferase (PRMT)1 and DDAH2 increased during the infusion of ANG II, whereas PRMT3 and endogenous mouse DDAH1 expression remained unaltered. Chronic infusion of ANG II in mice has no effect on the plasma levels of ADMA after 4 wk. However, an overexpression of DDAH1 alleviates ANG II-induced renal interstitial fibrosis and vascular oxidative stress, suggesting a blood pressure-independent effect of ADMA on ANG II-induced target organ damage.
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Krzystek-Korpacka, Małgorzata, Berenika Szczęśniak-Sięga, Izabela Szczuka, Paulina Fortuna, Marek Zawadzki, Agnieszka Kubiak, Magdalena Mierzchała-Pasierb, et al. "L-Arginine/Nitric Oxide Pathway Is Altered in Colorectal Cancer and Can Be Modulated by Novel Derivatives from Oxicam Class of Non-Steroidal Anti-Inflammatory Drugs." Cancers 12, no. 9 (September 11, 2020): 2594. http://dx.doi.org/10.3390/cancers12092594.

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L-arginine/nitric oxide pathway metabolites are altered in colorectal cancer (CRC). We evaluated underlying changes in pathway enzymes in 55 paired tumor/tumor-adjacent samples and 20 normal mucosa using quantitative-PCR and assessed the impact of classic and novel oxicam analogues on enzyme expression and intracellular metabolite concentration (LC-MS/MS) in Caco-2, HCT116, and HT-29 cells. Compared to normal mucosa, ARG1, PRMT1, and PRMT5 were overexpressed in both tumor and tumor-adjacent tissue and DDAH2 solely in tumor-adjacent tissue. Tumor-adjacent tissue had higher expression of ARG1, DDAH1, and DDAH2 and lower NOS2 than patients-matched tumors. The ARG1 expression in tumors increased along with tumor grade and reflected lymph node involvement. Novel oxicam analogues with arylpiperazine moiety at the thiazine ring were more effective in downregulating DDAHs and PRMTs and upregulating ARG2 than piroxicam and meloxicam. An analogue distinguished by propylene linker between thiazine’s and piperazine’s nitrogen atoms and containing two fluorine substituents was the strongest inhibitor of DDAHs and PRMTs expression, while an analogue containing propylene linker but no fluorine substituents was the strongest inhibitor of ARG2 expression. Metabolic reprogramming in CRC includes overexpression of DDAHs and PRMTs in addition to ARG1 and NOS2 and is not restricted to tumor tissue but can be modulated by novel oxicam analogues.
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Hannemann, Juliane, Daniel Appel, Miriam Seeberger-Steinmeister, Tabea Brüning, Julia Zummack, and Rainer Böger. "Sequence Variation in the DDAH1 Gene Predisposes for Delayed Cerebral Ischemia in Subarachnoidal Hemorrhage." Journal of Clinical Medicine 9, no. 12 (December 1, 2020): 3900. http://dx.doi.org/10.3390/jcm9123900.

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Delayed cerebral ischemia (DCI) often causes poor long-term neurological outcome after subarachnoidal hemorrhage (SAH). Asymmetric dimethylarginine (ADMA) inhibits nitric oxide synthase (NOS) and is associated with DCI after SAH. We studied single nucleotide polymorphisms (SNPs) in the NOS3, DDAH1, DDAH2, PRMT1, and AGXT2 genes that are part of the L-arginine–ADMA–NO pathway, and their association with DCI. We measured L-arginine, ADMA and symmetric dimethylarginine (SDMA) in plasma and cerebrospinal fluid (CSF) of 51 SAH patients at admission; follow-up was until 30 days post-discharge. The primary outcome was the incidence of DCI, defined as new infarctions on cranial computed tomography, which occurred in 18 of 51 patients. Clinical scores did not significantly differ in patients with or without DCI. However, DCI patients had higher plasma ADMA and SDMA levels and higher CSF SDMA levels at admission. DDAH1 SNPs were associated with plasma ADMA, whilst AGXT2 SNPs were associated with plasma SDMA. Carriers of the minor allele of DDAH1 rs233112 had a significantly increased relative risk of DCI (Relative Risk = 2.61 (1.25–5.43), p = 0.002). We conclude that the DDAH1 gene is associated with ADMA concentration and the incidence of DCI in SAH patients, suggesting a pathophysiological link between gene, biomarker, and clinical outcome in patients with SAH.
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Tessanne, K., B. Redel, K. Whitworth, L. Spate, A. Brown, and R. S. Prather. "145 CHARACTERIZATION OF THE PROTEIN ARGININE METHYLTRANSFERASE-DIMETHYLARGININE DIMETHYLAMINOHYDROLASE-NITRIC OXIDE AXIS DURING PORCINE EMBRYO DEVELOPMENT." Reproduction, Fertility and Development 24, no. 1 (2012): 185. http://dx.doi.org/10.1071/rdv24n1ab145.

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Transcriptional deep sequencing analysis by Bauer et al. (2010) revealed a significant increase in expression of the arginine transporter SLC7A1 in in vitro–cultured porcine blastocysts compared with those cultured in vivo and this was corrected through supplemental arginine. This indicates an important role for arginine during porcine embryo development. Arginine is the precursor for nitric oxide (NO) production and previous work in mice and cattle has shown decreased development when embryos were cultured with a nitric oxide synthase (NOS) inhibitor. The NOS activity is inhibited by monomethylarginine (MMA) and asymmetric dimethylarginine (ADMA) that are released during degradation of proteins methylated by protein arginine methyltransferases (PRMT). The enzyme dimethylarginine dimethylaminohydrolase (DDAH) is responsible for degrading MMA and ADMA in the cell. Therefore, the goal of this study was to investigate whether this PRMT-DDAH-NO axis exists in pre-implantation porcine embryos. To this end, expression of PRMT1, PRMT3, PRMT5, DDAH1 and endothelial NOS (NOS3) was analysed at different stages of embryonic development using real-time quantitative RT-PCR. In addition, the effect of supplemental arginine (1.69 mM) on the expression of the aforementioned genes was investigated. Production of NO in porcine embryos was also visualised using 4-amino-5-methylamino-2,7-difluorofluorescein diacetate (DAF-FM-DA). In vitro–fertilized porcine embryos were collected at the 4-cell and blastocyst stages. The RNA was isolated from pools of 18 to 20 embryos and cDNA, was synthesised using Superscript III (Invitrogen, Carlsbad, CA, USA). Real-time PCR analysis was performed and the mean fold change in gene expression from the reference gene YWHAG was analysed by t-test after a log transformation. Expression of PRMT3 and PRMT5 was significantly higher (P < 0.05) in blastocysts versus 4-cell embryos. Expression of PRMT1, however, was higher in 4-cell embryos (P < 0.05). The expression of DDAH1 was detected in 4-cell embryos, but DDAH1 became undetectable by the blastocyst stage. Previous microarray analysis in our laboratory by Whitworth et al. (2005 Biol. Reprod. 72(6), 1437–1451) also revealed a significant up-regulation of DDAH2 expression at the 4-cell stage versus blastocysts. Expression of NOS3 was undetectable in the 4-cell and blastocyst; however, NO was detected in 4-cell and blastocyst stage embryos by using DAF-FM-DA. This suggests that a different NOS may be acting in the porcine embryo. Addition of arginine did not have a significant effect on expression of the analysed genes. These results suggest that PRMT-DDAH regulated NO production may play a role during porcine embryo development. Understanding the PRMT-DDAH-NO axis and its regulation during embryonic development will further our ability to tailor in vitro culture so that it more appropriately mimics that of an in vivo environment. Funding was provided by NIH U42 RR18877.
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Dissertations / Theses on the topic "DDAH1"

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Dowsett, Laura Bethany. "The role of the NOS-ADMA-DDAH1 pathway in adipocytes and obesity." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/24709.

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Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide synthase (NOS) which is metabolised by two isoforms of the enzyme dimethylarginine dimethylaminohydrolase (DDAH). Inhibition of DDAH has been shown to increase ADMA concentrations both in vitro and in vivo. Clinically, high concentrations of ADMA have been associated with a range of diseases, particularly cardiovascular disease and more recently obesity. The role of the NO-ADMA-DDAH pathway has not yet been studied in adipose tissue. This thesis sets out to investigate the effects of pathological ADMA exposure firstly on adipocytes in vitro and secondly, on whole adipose physiology in vivo. In vitro the existence of the NO-ADMA-DDAH pathway was established in the 3T3-L1 cell line before investigating the effect of chronic ADMA exposure of their biology. ADMA was found to cause adipocyte hypertrophy through mTOR signalling in an NO independent manner. The effect of elevated ADMA on adipocytes in vivo was investigated through an adipocyte specific DDAH1 knockout. These mice developed visceral obesity with adipocyte hypertrophy with an increase in mTOR signalling. On a high fat diet there is a large increase in intracellular adipocyte ADMA in both knockout and control mice. Adipose vasculature is an important regulator of adipose expansion; to investigate the role of ADMA in this process an endothelial specific DDAH1 knockout mouse was developed. Angiogenesis in these mice is reduced restricting adipose growth in obesity. This thesis establishes that the NO-ADMA-DDAH1 pathway to be important in adipose physiology. Elevated ADMA in adipocytes and endothelial cells is detrimental to their function and increases various factors associated with the metabolic syndrome.
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Bernges, Isabel [Verfasser], and Elke [Akademischer Betreuer] Oetjen. "Die Metabolisierung der Dimethylarginine durch die Enzyme AGXT2 und DDAH1 und deren Anwendung für den Prozess der Drug Discovery / Isabel Bernges. Betreuer: Elke Oetjen." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2014. http://d-nb.info/1064076769/34.

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Tran, Cam Thanh Lucy. "Molecular analysis of human DDAH genes." Thesis, University College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.408021.

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Tommasi, Sara. "Design and synthesis of human dimethylarginine dimethylaminohydrolase (DDAH) inhibitors and development of a novel DDAH activity assay." Thesis, University of Aberdeen, 2015. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=227616.

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Nitric oxide (NO) is a key physiological messenger, but an excessive production of this molecule can be detrimental, leading to the onset or worsening of many pathological conditions. Dimethylarginine dimethylaminohydrolase (DDAH) is a key enzyme in the NO pathway, involved in the metabolism of asymmetric dimethylarginine (ADMA) and monomethyl arginine (L-NMMA), which are both endogenous inhibitors of NO synthesis. Two isoforms of DDAH have been identified in humans, namely DDAH-1 and DDAH-2. DDAH inhibition represents a promising strategy in the treatment of NO overproduction under pathological conditions without affecting the homeostatic role of this messenger. In this work I described the design and synthesis of 12 novel potential DDAH inhibitors together with the development of a new UPLC-MS based assay to measure the activity of HEK293T cell lysates overexpressing recombinant human DDAH-1 in metabolizing ADMA into dimethylamine and L-citrulline. The same assay was used to assess the potential of the novel compounds, as well as of the well-known DDAH inhibitor L-257, to inhibit DDAH-1 catalyzed L-citrulline formation from ADMA. Three of the novel molecules (compounds 10a, 14a and 14b) showed very interesting inhibitory activity: in particular, the methylacylsulfonamide analogue of L-257 (10a) resulted in 13-fold higher inhibition potency than L-257 itself (98% of inhibition at 1mM, IC50 = 3±3 μM and Ki = 1±0 μM). This molecule was chosen for molecular dynamics simulations to study the putative mechanism for 10a inhibition of DDAH-1 activity. Furthermore, DDAH-1 and DDAH-2 were engineered introducing a FLAG-tag at the C-terminal of the proteins to allow their purification from the lysate components by immunoprecipitation. Although the purification protocol requires some further improvement, the fusion proteins did not show to be functionally affected by the modification.
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Kelly, P. D. "Elucidation of the biochemical and physiological role of DDAH2." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1317766/.

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The asymmetric methylarginines monomethyl-L-arginine (L-NMMA) and asymmetric dimethylarginine (ADMA) are endogenously occurring inhibitors of the nitric oxide synthase (NOS) enzymes. Elevated plasma ADMA has been identified in a range of human cardiovascular disorders, some of which are associated with impaired NO signaling. The dimethylarginine dimethlyaminohydrolase (DDAH) enzymes are responsible for the degradation of asymmetric methylarginines in vivo. The physiological link between DDAH, ADMA, and NOS was demonstrated by a mouse genetic knockout of DDAH1. Ddah1+/- mice had elevated ADMA concentrations and impaired NOmediated vasoreactivity which resulted in increased systemic vascular resistance and increased blood pressure. In 1999, a second isoform of DDAH was identified, DDAH2. This thesis reports the biochemical characterization of a novel mouse genetic knockout of DDAH2. Although ADMA is considered the most prominent methylarginine species in vivo, this study finds significant concentrations of L-NMMA are also present. Previous work has hypothesized a possible immune function for DDAH2, independent of DDAH1. Mouse peritoneal macrophages were found to contain DDAH2 and exhibit DDAH enzymatic activity, but no DDAH1 was detected. NO generation by cytokine treated peritoneal macrophages from ddah2-/- mice was significantly less then from ddah2+/+ macrophages. Conversely, pharmacological inhibition of DDAH in macrophages did not result in indirect NOS inhibition; this may be due to isoform specificity of the previously developed DDAH inhibitors. To determine the functional significance of the decreased NO generation capacity of ddah2-/- macrophages, their in vivo and in vitro antibacterial properties were investigated. Ddah2 genotype did not have any effect on the ability of peritoneal macrophages to kill S. aureus in vitro. But, in a mouse model of polymicrobial sepsis, ddah2-/- mice showed a significant increase in mortality. Follow-up characterization of this model showed a decrease in bacterial clearance by ddah2-/- mice along with a significant increase in asymmetric methylarginine concentration and changes in the concentration of several cytokines.
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Pullamsetti, Soni. "Role of Dimethylarginine Dimethylaminohydrolases (DDAH) in pulmonary arterial hypertension." Giessen VVB Laufersweiler, 2006. http://geb.uni-giessen.de/geb/volltexte/2006/2892/index.html.

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Tomlinson, James. "The role of DDAH and ADMA in kidney disease." Thesis, Imperial College London, 2013. http://hdl.handle.net/10044/1/24541.

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Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide (NO) synthesis and elevated plasma levels associate with poor cardiovascular and renal outcomes. The dimethylarginine dimethylaminohydrolase enzymes (DDAHs; 1 and 2) metabolise ADMA. A DDAH1 gene variant associates with higher kidney tissue mRNA expression, lower plasma ADMA but counter-intuitively, a steeper rate of eGFR decline. This indicates that renal DDAH1 activity may be deleterious and circulating ADMA does not necessarily reflect the NO-ADMA balance (or severity of disease) within kidney tissue. This study tests the hypothesis that reduced renal DDAH1 activity protects against the progression of kidney function decline, independent of circulating ADMA. Renal DDAH1 expression predominates within the proximal tubule. A novel proximal tubule-specific DDAH1 knock-out (PTD1KO) mouse was developed, which demonstrated tubule-specific dysregulation of ADMA and NO that was not evident systemically. Phenotyping studies in PTD1KO mice did not identify consistent alterations of urinary biochemistry at baseline or after salt loading, however, proteomic analysis revealed significant alterations of urinary peptides at baseline; including down-regulation of uromodulin and collagen. At 12 weeks following folate renal injury, the PTD1KO mouse exhibited less kidney function decline, collagen deposition and pro-fibrotic gene expression (Col12alpha, TGFbeta and ET-1) than controls. Furthermore, ADMA and DDAH1 inhibition reduced tubular sodium and fluid reabsorption in rat microperfusion studies, although studies in PTD1KO mice failed to reproduce this effect. Finally, in vitro studies using a PT cell line and primary PT culture indicated an inhibitory effect of ADMA upon PT cell proliferation. Consistent with recent human genetic studies, these data provide experimental evidence indicating a reduction of renal tubule DDAH1 activity can protect against progressive kidney fibrosis and function decline, independent of plasma ADMA. This work provides novel insights into the role of the NO-ADMA-DDAH axis within the kidney, particularly the tubule.
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Pullamsetti, Soni [Verfasser]. "Role of dimethylarginine dimethylaminohydrolases (DDAH) in pulmonary arterial hypertension / vorgelegt von Soni Pullamsetti." Giessen : VVB Laufersweiler, 2006. http://d-nb.info/98866240X/34.

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Hicks, Diana. "English language teaching teacher's guides : a critical discourse analysis of three texts." Thesis, University of Bristol, 2000. http://hdl.handle.net/1983/a13246cc-dda1-4a94-b061-7c3a415ee82e.

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Khanom, N. "Evaluation of novel arginine based inhibitors of DDAH and investigations into radical hydroacylation of vinyl sulfonates." Thesis, University College London (University of London), 2010. http://discovery.ucl.ac.uk/192842/.

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The thesis is in two main sections. In the first section, studies on methylarginine processing enzymes are presented. Dimethyalrginine dimethylaminohydrolase (DDAH) is a class of enzymes involved in the metabolism of methylarginines ADMA and L-NMMA, which indirectly regulate physiological nitric oxide levels. It is desirable to inhibit excess NO in pathological situations, and the arginine mimetic L-257 is a DDAH inhibitor which reduces levels of NO. Synthesis of ester analogues of L-257 proved to be troublesome with a low yielding key guanidine forming reaction. However, amide analogues were readily synthesised, and testing for DDAH inhibition showed the dimethylamide analogue possessed similar activity to L-257. Further design and synthesis of a 7-membered cyclic analogue, based on the crystal structure of huDDAH1 with L-257, provided a novel analogue with no significant inhibition for rat kidney DDAH. Purified and isolated huDDAH2 protein showed activity after incubation with substrate L-NMMA. In the second part studies on aldehyde auto-oxidation are presented. Aldehydes autoxidise to their acids, via an acyl radical, which can undergo addition reactions with electron-deficient acceptors in a radical hydroacylation reaction. An α- iodo and α-chloro hexanal failed to autoxidise, however 7-hydroxycitronellal readily autoxidised and added to pentafluorophenyl(PFP)-vinyl sulfonate. Further studies on hydroacylation of butanal with PFP-vinyl sulfonate led to functionalised β-ketosulfonates which undergo elimination to form an enone and can then undergo further conjugate addition in situ by nucleophiles. Conjugate addition was carried out using carbon, nitrogen, oxygen and phosphorus nucleophiles, providing a method of obtaining products which are challenging to make via hydroacylation of electron-rich alkenes. Decarbonylation of pivaldehyde to the t-butyl radical, via auto-oxidation, was optimised and the alkyl radical captured by a number of electron-deficient acceptors, providing a complementary method to current methods of t-butyl addition using metal reagents.
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Books on the topic "DDAH1"

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Desorden de Deficit de Atencion - DDAH. Publicaciones Puertorriquenas, 2006.

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Conference papers on the topic "DDAH1"

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Lota, HK, CJ Stock, EA Renzoni, AU Wells, and JM Leiper. "S141 A novel dimethylarginine dimethylaminohydrolase 1 (DDAH1) genetic variant associated with lower asymmetric dimethylarginine (ADMA) levels predicts accelerated lung function decline and mortality in idiopathic pulmonary fibrosis." In British Thoracic Society Winter Meeting 2018, QEII Centre, Broad Sanctuary, Westminster, London SW1P 3EE, 5 to 7 December 2018, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2018. http://dx.doi.org/10.1136/thorax-2018-212555.147.

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Sharma, Shruti, Sanjiv Kumar, Saurabh Aggarwal, Neetu Sud, Yali Hou, Connie Snead, David Fulton, John D. Catravas, and Stephen Black. "LPS Decreases Dimethylarginine Dimethylaminohydrolase (DDAH) Activity Through The Activation Of Pp60Src." 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.a6476.

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Bakr, Adel G. M., Natascha Sommer, Hossein Ghofrani, Ralph Schermuly, Werner Seeger, Friedrich Grimminger, Farid Hamada, et al. "Effects Of Dimethylarginine Dimethylaminohydrolase 1 (DDAH-1) In Acute And Sustained Hypoxia Induced Pulmonary Vasoconstriction." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5497.

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Lota, Harpreet K., and James M. Leiper. "Role of the nitric oxide-asymmetric dimethylarginine-dimethylarginine dimethylaminohydrolase (NO-ADMA-DDAH) axis in TGF-β mediated epithelial-mesenchymal transition." In Annual Congress 2015. European Respiratory Society, 2015. http://dx.doi.org/10.1183/13993003.congress-2015.pa3049.

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Bachmann, A., J. Singh, Y. Lee, M. Sturek, T. Karn, and N. Sänger. "Polyzystisches Ovarsyndrom (PCOS) und kardiovaskuläres Risiko: Unterschiede in der Aktivität von Dimethylarginin Dimethylaminohydrolase 1 (DDAH 1) in der Leber von Ossabaw Miniaturschweinen." In 62. Kongress der Deutschen Gesellschaft für Gynäkologie und Geburtshilfe – DGGG'18. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1671619.

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Reports on the topic "DDAH1"

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CALS TEST NETWORK WRIGHT-PATTERSON AFB OH. Technical Publication Transfer Using: Texas Instruments' Data Supporting: U.S. Army Missile Command's TOW ITAS Program, Contract DDAH01-93-C-0206 MIL-STD- 1840A, MIL-M-28001A (SGML), MIL-D-28003 (CGM). Quick Short Test Report. Fort Belvoir, VA: Defense Technical Information Center, April 1994. http://dx.doi.org/10.21236/ada312855.

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