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Journal articles on the topic 'DDAH1'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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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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4

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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5

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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Zhang, Ping, John T. Fassett, Guangshuo Zhu, Jingxin Li, Xinli Hu, Xin Xu, Yingjie Chen, and Robert J. Bache. "Repetitive ischemia increases myocardial dimethylarginine dimethylaminohydrolase 1 expression." Vascular Medicine 22, no. 3 (February 1, 2017): 179–88. http://dx.doi.org/10.1177/1358863x16681215.

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Pharmacologic inhibition of nitric oxide production inhibits growth of coronary collateral vessels. Dimethylarginine dimethylaminohydrolase 1 (DDAH1) is the major enzyme that degrades asymmetric dimethylarginine (ADMA), a potent inhibitor of nitric oxide synthase. Here we examined regulation of the ADMA-DDAH1 pathway in a canine model of recurrent myocardial ischemia during the time when coronary collateral growth is known to occur. Under basal conditions, DDAH1 expression was non-uniform across the left ventricular (LV) wall, with expression strongest in the subepicardium. In response to ischemia, DDAH1 expression was up-regulated in the midmyocardium of the ischemic zone, and this was associated with a significant reduction in myocardial interstitial fluid (MIF) ADMA. The decrease in MIF ADMA during ischemia was likely due to increased DDAH1 because myocardial protein arginine N-methyl transferase 1 (PRMT1) and the methylated arginine protein content (the source of ADMA) were unchanged or increased, respectively, at this time. The inflammatory mediators interleukin (IL-1β) and tumor necrosis factor (TNF-α) were also elevated in the midmyocardium where DDAH1 expression was increased. Both of these factors significantly up-regulated DDAH1 expression in cultured human coronary artery endothelial cells. Taken together, these results suggest that inflammatory factors expressed in response to myocardial ischemia contributed to up-regulation of DDAH1, which was responsible for the decrease in MIF ADMA.

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Redel, Bethany K., Kimberly J. Tessanne, Lee D. Spate, Clifton N. Murphy, and Randall S. Prather. "Arginine increases development of in vitro-produced porcine embryos and affects the protein arginine methyltransferase–dimethylarginine dimethylaminohydrolase–nitric oxide axis." Reproduction, Fertility and Development 27, no. 4 (2015): 655. http://dx.doi.org/10.1071/rd14293.

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Culture systems promote development at rates lower than the in vivo environment. Here, we evaluated the embryo’s transcriptome to determine what the embryo needs during development. A previous mRNA sequencing endeavour found upregulation of solute carrier family 7 (cationic amino acid transporter, y+ system), member 1 (SLC7A1), an arginine transporter, in in vitro- compared with in vivo-cultured embryos. In the present study, we added different concentrations of arginine to our culture medium to meet the needs of the porcine embryo. Increasing arginine from 0.12 to 1.69 mM improved the number of embryos that developed to the blastocyst stage. These blastocysts also had more total nuclei compared with controls and, specifically, more trophectoderm nuclei. Embryos cultured in 1.69 mM arginine had lower SLC7A1 levels and a higher abundance of messages involved with glycolysis (hexokinase 1, hexokinase 2 and glutamic pyruvate transaminase (alanine aminotransferase) 2) and decreased expression of genes involved with blocking the tricarboxylic acid cycle (pyruvate dehydrogenase kinase, isozyme 1) and the pentose phosphate pathway (transaldolase 1). Expression of the protein arginine methyltransferase (PRMT) genes PRMT1, PRMT3 and PRMT5 throughout development was not affected by arginine. However, the dimethylarginine dimethylaminohydrolase 1 (DDAH1) and DDAH2 message was found to be differentially regulated through development, and the DDAH2 protein was localised to the nuclei of blastocysts. Arginine has a positive effect on preimplantation development and may be affecting the nitric oxide–DDAH–PRMT axis.

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Sun, Gwo-Ching, Tzyy-Yue Wong, Hsin-Hung Chen, Chiu-Yi Ho, Tung-Chen Yeh, Wen-Yu Ho, Ching-Jiunn Tseng, and Pei-Wen Cheng. "Angiotensin II inhibits DDAH1–nNOS signaling via AT1R and μOR dimerization to modulate blood pressure control in the central nervous system." Clinical Science 133, no. 23 (December 2019): 2401–13. http://dx.doi.org/10.1042/cs20191005.

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Abstract G protein-coupled receptors (GPCRs) are important drug targets. Blocking angiotensin II (Ang II) type 1 receptor signaling alleviates hypertension and improves outcomes in patients with heart failure. Changes in structure and trafficking of GPCR, and desensitization of GPCR signaling induce pathophysiological processes. We investigated whether Ang II, via induction of AT1R and μ-opioid receptor (μOR) dimerization in the nucleus tractus solitarius (NTS), leads to progressive hypertension. Ang II signaling increased μOR and adrenergic receptor α2A (α2A-AR) heterodimer levels and decreased expression of extracellular signal-regulated kinases 1/2T202/Y204, ribosomal protein S6 kinaseT359/S363, and nNOSS1416 phosphorylation. Dimethylarginine dimethylaminohydrolase 1 (DDAH1) expression was abolished in the NTS of adult spontaneously hypertensive rats (SHRs). Endomorphin-2 was overexpressed in NTS of adult SHRs compared with that in 6-week-old Wistar-Kyoto rats (WKY). Administration of μOR agonist into the NTS of WKY increased blood pressure (BP), decreased nitric oxide (NO) production, and decreased DDAH1 activity. μOR agonist significantly reduced the activity of DDAH1 and decreased neuronal NO synthase (nNOS) phosphorylation. The AT1R II inhibitor, losartan, significantly decreased BP and abolished AT1R-induced formation of AT1R and μOR, and α2A-AR and μOR, heterodimers. Losartan also significantly increased the levels of nNOSS1416 phosphorylation and DDAH1 expression. These results show that Ang II may induce expression of endomorphin-2 and abolished DDAH1 activity by enhancing the formation of AT1R and μOR heterodimers in the NTS, leading to progressive hypertension.

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Liu, Xiaoyu, John Fassett, Yidong Wei, and Yingjie Chen. "Regulation of DDAH1 as a Potential Therapeutic Target for Treating Cardiovascular Diseases." Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/619207.

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Asymmetric dimethylarginine (ADMA) is an endogenous nitric oxide synthase inhibitor that blocks nitric oxide production, while congestive heart failure is associated with increased plasma and tissue ADMA content. Increased plasma ADMA is a strong and independent predictor of all-cause mortality in the community and the strongest predictor of mortality in patients after myocardial infarction. Recent studies demonstrated that dimethylarginine dimethylaminohydrolase-1 (DDAH1) is the critical enzyme for ADMA degradation and thereby plays an important role in maintaining cardiovascular nitric oxide bioavailability. Interestingly, activation of the farnesoid X receptor (FXR) through the bile acid ursodeoxycholic acid (UDCA) or synthetic FXR agonists, such as GW4064, can increase DDAH1 expression. Thus, modulating DDAH1 activity through FXR receptor agonists such as UDCA could be a therapeutic target for treating reduced nitric oxide bioavailability in congestive heart failure and other cardiovascular diseases.

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Wu, Chih-Cheng, Mu-Yang Hsieh, Chih-Kuo Lee, Shao-Yuan Chuang, Ming-Yi Chung, and Chih-Ching Lin. "Dimethylarginine Dimethylaminohydrolase 1 Polymorphisms and Venous Intimal Hyperplasia in Hemodialysis Patients." American Journal of Nephrology 50, no. 6 (2019): 454–64. http://dx.doi.org/10.1159/000503949.

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Background: After angioplasty, veins are more prone to intimal hyperplasia than arteries. Veins tend to produce less nitric oxide (NO), which could lead to endothelial dysfunction. Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of NO synthase and contributes to cardiovascular disease. In humans, dimethylarginine dimethylaminohydrolase 1 (DDAH1) is the major enzyme for ADMA degradation. In this study, we aim to determine whether venous intimal hyperplasia in hemodialysis (HD) vascular access is influenced by common polymorphisms in the DDAH1 genes. Methods: This is a prospective observational cohort study. A total of 473 HD patients referred for the angioplasty of vascular access were enrolled. There were 190 arteriovenous grafts (AVG) and 283 arteriovenous fistulas (AVF). The follow-up lasted for 2 years after the interventions. Seven single nucleotide polymorphisms (SNPs) in DDAH1 were genotyped and ADMA were measured at baseline. The primary outcome was restenosis after angioplasty. Results: Among the 7 SNPs, plasma ADMA levels were significantly different in DDAH1 rs233112 (GA + GG vs. AA, 0.86 ± 0.23 vs. 0.82 ± 0.19 μM, p = 0.03) and rs1498373 (CT + TT vs. CC, 0.87 ± 0.23 vs. 0.82 ± 0.20 μM, p = 0.02) genotypes. The AVF group with GG + GA genotype of rs233112 and CT + TT genotype of rs1498373 had higher risks of early restenosis at 3 months. In the AVG group, only GG + GA genotype of rs233112 was associated with early restenosis. A combined analysis of AVG and AVF groups showed that patients with rs233112 GA + GG genotype and rs1498373 CT + TT genotype had higher risks of early restenosis (both p < 0.001). The multivariate analysis results showed that the association of these genotypes with early restenosis is independent of clinical, access, or biochemical factors. Conclusions: Our findings suggest that certain DDAH1 polymorphisms modulate circulating ADMA levels and are associated with venous intimal hyperplasia.

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Pacurari, Maricica, Dongqi Xing, Rob H. P. Hilgers, Yuan Yuan Guo, Zhengqin Yang, and Fadi G. Hage. "Endothelial cell transfusion ameliorates endothelial dysfunction in 5/6 nephrectomized rats." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 8 (October 15, 2013): H1256—H1264. http://dx.doi.org/10.1152/ajpheart.00132.2013.

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Endothelial dysfunction is prevalent in chronic kidney disease. This study tested the hypothesis that transfusion of rat aortic endothelial cells (ECs) ameliorates endothelial dysfunction in a rat model of chronic kidney disease. Male Sprague-Dawley rats underwent sham surgery or 5/6 nephrectomy (Nx). Five weeks after Nx, EC (1.5 × 106 cells/rat) or vehicle were transfused intravenously. One week later, vascular reactivity of mesenteric artery was assessed on a wire myograph. Sensitivity of endothelium-dependent relaxation to acetylcholine and maximum vasodilation were impaired by Nx and improved by EC transfusion. Using selective pharmacological nitric oxide synthase isoform inhibitors, we demonstrated that the negative effect of Nx on endothelial function and rescue by EC transfusion are, at least in part, endothelial nitric oxide synthase mediated. Plasma asymmetric dimethylarginine was increased by Nx and decreased by EC transfusion, whereas mRNA expression of dimethylarginine dimethylaminohydrolases 1 (DDAH1) was decreased by Nx and restored by EC transfusion. Immunohistochemical staining confirmed that local expression of DDAH1 is decreased by Nx and increased by EC transfusion. In conclusion, EC transfusion attenuates Nx-induced endothelium-dependent vascular dysfunction by regulating DDAH1 expression and enhancing endothelial nitric oxide synthase activity. These results suggest that EC-based therapy could provide a novel therapeutic strategy to improve vascular function in chronic kidney disease.

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Kuang, Da-bin, Ji-peng Zhou, Lin-yu Yu, Wen-jing Zeng, Jian Xiao, Gang-zhi Zhu, Zan-lin Zhang, and Xiao-ping Chen. "DDAH1-V3 transcript might act as miR-21 sponge to maintain balance of DDAH1-V1 in cultured HUVECs." Nitric Oxide 60 (November 2016): 59–68. http://dx.doi.org/10.1016/j.niox.2016.09.008.

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Tran, Cam T. L., Margaret F. Fox, Patrick Vallance, and James M. Leiper. "Chromosomal Localization, Gene Structure, and Expression Pattern of DDAH1: Comparison with DDAH2 and Implications for Evolutionary Origins." Genomics 68, no. 1 (August 2000): 101–5. http://dx.doi.org/10.1006/geno.2000.6262.

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Schwedhelm, Edzard, Eike-Christin von Leitner, Dorothee Atzler, Christine Schmitz, Johannes Jacobi, Thomas Meinertz, Thomas Münzel, et al. "Extensive characterization of the human DDAH1 transgenic mice." Pharmacological Research 60, no. 6 (December 2009): 494–502. http://dx.doi.org/10.1016/j.phrs.2009.08.001.

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Mishima, Takuya, Tsuyoshi Hamada, Kumiko Ui-Tei, Fumitaka Takahashi, Yuhei Miyata, Junko Imaki, Hidenori Suzuki, and Kazuo Yamashita. "Expression of DDAH1 in chick and rat embryos." Developmental Brain Research 148, no. 2 (February 2004): 223–32. http://dx.doi.org/10.1016/j.devbrainres.2003.09.021.

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Wang, Zhen, Simon Lambden, Valerie Taylor, Elizabeth Sujkovic, Manasi Nandi, James Tomlinson, Alex Dyson, et al. "Pharmacological inhibition of DDAH1 improves survival, haemodynamics and organ function in experimental septic shock." Biochemical Journal 460, no. 2 (May 13, 2014): 309–16. http://dx.doi.org/10.1042/bj20131666.

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The present study shows for the first time in the most relevant possible rodent model of shock that the DDAH1 inhibitor L-257 improves morbidity and mortality in septic shock by improving cardiovascular function without impairing the immune cell function.

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Kami Reddy, Karthik Reddy, Chandrashekhar Dasari, Shalini Vandavasi, Sirisha Natani, Bhukya Supriya, Surender Singh Jadav, N. Sai Ram, Jerald Mahesh Kumar, and Ramesh Ummanni. "Novel Cellularly Active Inhibitor Regresses DDAH1 Induced Prostate Tumor Growth by Restraining Tumor Angiogenesis through Targeting DDAH1/ADMA/NOS Pathway." ACS Combinatorial Science 21, no. 4 (January 23, 2019): 241–56. http://dx.doi.org/10.1021/acscombsci.8b00133.

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Bulau, Patrick, Dariusz Zakrzewicz, Kamila Kitowska, James Leiper, Andreas Gunther, Friedrich Grimminger, and Oliver Eickelberg. "Analysis of methylarginine metabolism in the cardiovascular system identifies the lung as a major source of ADMA." American Journal of Physiology-Lung Cellular and Molecular Physiology 292, no. 1 (January 2007): L18—L24. http://dx.doi.org/10.1152/ajplung.00076.2006.

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Protein arginine methylation is catalyzed by a family of enzymes called protein arginine methyltransferases (PRMTs). Three forms of methylarginine have been identified in eukaryotes: monomethylarginine (l-NMMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA), all characterized by methylation of one or both guanidine nitrogen atoms of arginine. l-NMMA and ADMA, but not SDMA, are competitive inhibitors of all nitric oxide synthase isoforms. SDMA is eliminated almost entirely by renal excretion, whereas l-NMMA and ADMA are further metabolized by dimethylarginine dimethylaminohydrolase (DDAH). To explore the interplay between methylarginine synthesis and degradation in vivo, we determined PRMT expression and DDAH activity in mouse lung, heart, liver, and kidney homogenates. In addition, we employed HPLC-based quantification of protein-incorporated and free methylarginine, combined with immunoblotting for the assessment of tissue-specific patterns of arginine methylation. The salient findings of the present investigation can be summarized as follows: 1) pulmonary expression of type I PRMTs was correlated with enhanced protein arginine methylation; 2) pulmonary ADMA degradation was undertaken by DDAH1; 3) bronchoalveolar lavage fluid and serum exhibited almost identical ADMA/SDMA ratios, and 4) kidney and liver provide complementary routes for clearance and metabolic conversion of circulating ADMA. Together, these observations suggest that methylarginine metabolism by the pulmonary system significantly contributes to circulating ADMA and SDMA levels.

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Zhang, Ping, Xin Xu, Xinli Hu, Huan Wang, John Fassett, Yuqing Huo, Yingjie Chen, and Robert J. Bache. "DDAH1 Deficiency Attenuates Endothelial Cell Cycle Progression and Angiogenesis." PLoS ONE 8, no. 11 (November 18, 2013): e79444. http://dx.doi.org/10.1371/journal.pone.0079444.

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Akbar, Fareeza, Seppo Heinonen, Mia Pirskanen, Pekka Uimari, Tomi-Pekka Tuomainen, and Jukka T. Salonen. "Haplotypic association of DDAH1 with susceptibility to pre-eclampsia." MHR: Basic science of reproductive medicine 11, no. 1 (January 1, 2005): 73–77. http://dx.doi.org/10.1093/molehr/gah116.

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Brites-Anselmi, Guilhermo, Ana Maria Milanez Azevedo, Anderson Heiji Lima Miyazaki, Lucas Cezar Pinheiro, Fernanda Borchers Coeli-Lacchini, Murilo Ferreira de Andrade, Carlos Augusto Fernandes Molina, et al. "DDAH1 and DDAH2 polymorphisms associate with asymmetrical dimethylarginine plasma levels in erectile dysfunction patients but not in healthy controls." Nitric Oxide 92 (November 2019): 11–17. http://dx.doi.org/10.1016/j.niox.2019.08.001.

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Lumicisi, B. A., J. E. Cartwright, K. Leslie, A. E. Wallace, and G. S. Whitley. "Inhibition of DDAH1, but not DDAH2, results in apoptosis of a human trophoblast cell line in response to TRAIL." Human Reproduction 30, no. 8 (June 16, 2015): 1813–19. http://dx.doi.org/10.1093/humrep/dev138.

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Iannone, Lucio, Lan Zhao, Olivier Dubois, Lucie Duluc, Christopher J. Rhodes, John Wharton, Martin R. Wilkins, James Leiper, and Beata Wojciak-Stothard. "miR-21/DDAH1 pathway regulates pulmonary vascular responses to hypoxia." Biochemical Journal 462, no. 1 (July 24, 2014): 103–12. http://dx.doi.org/10.1042/bj20140486.

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miR-21 mediates the effects of hypoxia on ADMA metabolism in pulmonary endothelial cells and mouse lungs. Therapeutic targeting of miR-21 reduces lung ADMA levels, improves nitric oxide signalling and prevents early development of chronic hypoxia-induced pulmonary hypertension.

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Breckenridge, Ross A., Peter Kelly, Manasi Nandi, Patrick J. Vallance, Timothy J. Ohun, and James Leiper. "A role for Dimethylarginine Dimethylaminohydrolase 1 (DDAH1) in mammalian development." International Journal of Developmental Biology 54, no. 1 (2010): 215–26. http://dx.doi.org/10.1387/ijdb.072356rb.

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30

Yang, Dafeng, Shenglan Tan, Zhousheng Yang, Pei Jiang, Caie Qin, Qiong Yuan, Ruili Dang, et al. "Dihydromyricetin Attenuates TNF-α-Induced Endothelial Dysfunction through miR-21-Mediated DDAH1/ADMA/NO Signal Pathway." BioMed Research International 2018 (2018): 1–12. http://dx.doi.org/10.1155/2018/1047810.

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Accumulating studies demonstrate that dihydromyricetin (DMY), a compound extracted from Chinese traditional herb, Ampelopsis grossedentata, attenuates atherosclerotic process by improvement of endothelial dysfunction. However, the underlying mechanism remains poorly understood. Thus, the aim of this study is to investigate the potential mechanism behind the attenuating effects of DMY on tumor necrosis factor alpha- (TNF-α-) induced endothelial dysfunction. In response to TNF-α, microRNA-21 (miR-21) expression was significantly increased in human umbilical vein endothelial cells (HUVECs), in line with impaired endothelial dysfunction as evidenced by decreased tube formation and migration, endothelial nitric oxide synthase (eNOS) (ser1177) phosphorylation, dimethylarginine dimethylaminohydrolases 1 (DDAH1) expression and metabolic activity, and nitric oxide (NO) concentration as well as increased asymmetric dimethylarginine (ADMA) levels. In contrast, DMY or blockade of miR-21 expression ameliorated endothelial dysfunction in HUVECs treated with TNF-α through downregulation of miR-21 expression, whereas these effects were abolished by overexpression of miR-21. In addition, using a nonspecific NOS inhibitor, L-NAME, also abrogated the attenuating effects of DMY on endothelial dysfunction. Taken together, these data demonstrated that miR-21-mediated DDAH1/ADMA/NO signal pathway plays an important role in TNF-α-induced endothelial dysfunction, and DMY attenuated endothelial dysfunction induced by TNF-α in a miR-21-dependent manner.

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Burstein-Teitelbaum, Gayle, Joyce A. V. Er, Arthur F. Monzingo, Alfred Tuley, and Walter Fast. "Dissection, Optimization, and Structural Analysis of a Covalent Irreversible DDAH1 Inhibitor." Biochemistry 57, no. 30 (July 8, 2018): 4574–82. http://dx.doi.org/10.1021/acs.biochem.8b00554.

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Tsuda, Kazushi. "Asymmetric Dimethylarginine and DDAH1 Transcript Variants in Cardiovascular and Cerebrovascular Diseases." American Journal of Hypertension 27, no. 3 (January 27, 2014): 497. http://dx.doi.org/10.1093/ajh/hpt242.

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Chen, YingJie, Soon Park, Yunfang Li, Emil Missov, Mingxiao Hou, Xinqiang Han, Jennifer L. Hall, Leslie W. Miller, and Robert J. Bache. "Alterations of gene expression in failing myocardium following left ventricular assist device support." Physiological Genomics 14, no. 3 (August 15, 2003): 251–60. http://dx.doi.org/10.1152/physiolgenomics.00022.2003.

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Chronic unloading of the failing heart with a left ventricular assist device (LVAD) can decrease cardiac mass and myocyte size and has the potential to improve contractile function. To study the effect of chronic ventricular unloading on myocardial gene expression, a microarray (U133A, Affymetrix) profiling gene expression was compared before and after LVAD support in seven patients with idiopathic dilated cardiomyopathy and end-stage heart failure. On average, 1,374 ± 155 genes were reported as “increased” and 1,629 ± 45 as “decreased” after LVAD support. A total of 130 gene transcripts achieved the strict criteria for upregulation and 49 gene transcripts for downregulation after LVAD support. Upregulated genes included a large proportion of transcription factors, genes related to cell growth/apoptosis/DNA repair, cell structure proteins, metabolism, and cell signaling/communication. LVAD support resulted in downregulation of genes for a group of cytokines. To validate the array data, 10 altered genes were confirmed by real-time RT-PCR. Further study showed that the phosphoinositide-3-kinase-forkhead protein pathway and proteins related to nitric oxide synthesis, including eNOS and dimethylarginine dimethylaminohydrolase isoform 1 (DDAH1, an enzyme regulating endogenous nitric oxide synthase activity), were significantly increased during the cardiac remodeling process. Increased eNOS and DDAH1 expression after LVAD support may contribute to improved endothelial function of the failing hearts.

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Abhary, Sotoodeh, Kathryn P. Burdon, Abraham Kuot, Shahrbanou Javadiyan, Malcolm J. Whiting, Nicholas Kasmeridis, Nikolai Petrovsky, and Jamie E. Craig. "Sequence Variation in DDAH1 and DDAH2 Genes Is Strongly and Additively Associated with Serum ADMA Concentrations in Individuals with Type 2 Diabetes." PLoS ONE 5, no. 3 (March 1, 2010): e9462. http://dx.doi.org/10.1371/journal.pone.0009462.

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Sun, Tao, Ji-Peng Zhou, Da-Bin Kuang, Mu-Peng Li, Yan Xiong, Jie Tang, Jian Xia, et al. "Correlations of DDAH1 Transcript Variants with Human Endothelial Asymmetric Dimethylarginine Metabolizing Activity." American Journal of Hypertension 26, no. 12 (July 17, 2013): 1437–44. http://dx.doi.org/10.1093/ajh/hpt119.

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Wang, Hongyun, Yuting Guo, Limin Liu, Longfei Guan, Ting Wang, Luyao Zhang, Yue Wang, et al. "DDAH1 plays dual roles in PM2.5 induced cell death in A549 cells." Biochimica et Biophysica Acta (BBA) - General Subjects 1860, no. 12 (December 2016): 2793–801. http://dx.doi.org/10.1016/j.bbagen.2016.03.022.

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Zhou, Ji-Peng, Da-Bin Kuang, and Xiao-Ping Chen. "Response to “Asymmetric Dimethylarginine and DDAH1 Transcript Variants in Cardiovascular and Cerebrovascular Diseases”." American Journal of Hypertension 27, no. 3 (January 27, 2014): 498–99. http://dx.doi.org/10.1093/ajh/hpt286.

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38

Liu, Xiu-Juan, Quan Hong, Zhen Wang, Yan-yan Yu, Xin Zou, and Li-hong Xu. "MicroRNA21 promotes interstitial fibrosis via targeting DDAH1: a potential role in renal fibrosis." Molecular and Cellular Biochemistry 411, no. 1-2 (October 12, 2015): 181–89. http://dx.doi.org/10.1007/s11010-015-2580-2.

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Hannemann, Juliane, Julia Zummack, Jonas Hillig, and Rainer Böger. "Metabolism of asymmetric dimethylarginine in hypoxia: from bench to bedside." Pulmonary Circulation 10, no. 1_suppl (April 14, 2020): 31–41. http://dx.doi.org/10.1177/2045894020918846.

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Acute hypoxia and chronic hypoxia induce pulmonary vasoconstriction. While hypoxic pulmonary vasoconstriction is a physiological response if parts of the lung are affected, global exposure to hypoxic conditions may lead to clinical conditions like high-altitude pulmonary hypertension. Nitric oxide is the major vasodilator released from the vascular endothelium. Nitric oxide-dependent vasodilation is impaired in hypoxic conditions. Inhibition of nitric oxide synthesis is the most rapid and easily reversible molecular mechanism to regulate nitric oxide-dependent vascular function in response to physiological and pathophysiological stimuli. Asymmetric dimethylarginine is an endogenous, competitive inhibitor of nitric oxide synthase and a risk marker for major cardiovascular events and mortality. Elevated asymmetric dimethylarginine has been observed in animal models of hypoxia as well as in human cohorts under chronic and chronic intermittent hypoxia at high altitude. In lowlanders, asymmetric dimethylarginine is high in patients with pulmonary hypertension. We have recently shown that high asymmetric dimethylarginine at sea level is a predictor for high-altitude pulmonary hypertension. Asymmetric dimethylarginine is a highly regulated molecule, both by its biosynthesis and metabolism. Methylation of L-arginine by protein arginine methyltransferases was shown to be increased in hypoxia. Furthermore, the metabolism of asymmetric dimethylarginine by dimethylarginine dimethylaminohydrolases (DDAH1 and DDAH2) is decreased in animal models of hypoxia. Whether these changes are caused by transcriptional or posttranslational modifications remains to be elucidated. Current data suggest a major role of asymmetric dimethylarginine in regulating pulmonary arterial nitric oxide production in hypoxia. Further studies are needed to decipher the molecular mechanisms regulating asymmetric dimethylarginine in hypoxia and to understand their clinical significance.

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Trocha, Małgorzata, Anna Merwid-Ląd, Tomasz Sozański, Ewa Chlebda, Dorota Nowak, Piotr Dzięgiel, Małgorzata Pieśniewska, Agnieszka Gomułkiewicz, Tomasz Piasecki, and Adam Szeląg. "Impact of ischemia/reperfusion (IR) and sitagliptin administration on dimethylarginine dimethylaminohydrolase (DDAH) activity and protein arginine methyltransferase (PRMT) and DDAH1 mRNA expression in rat liver." Pharmacological Reports 67 (September 2015): 42. http://dx.doi.org/10.1016/j.pharep.2015.06.127.

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41

Ye, Jianxin, Jie Xu, Yun Li, Qiang Huang, Jinsheng Huang, Jinzhou Wang, Wenjing Zhong, Xinjian Lin, Wannan Chen, and Xu Lin. "DDAH1 mediates gastric cancer cell invasion and metastasis via Wnt/β-catenin signaling pathway." Molecular Oncology 11, no. 9 (June 22, 2017): 1208–24. http://dx.doi.org/10.1002/1878-0261.12089.

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42

Ding, Xubei, Junjun Zheng, and Mingxiang Cao. "Circ_0004771 Accelerates Cell Carcinogenic Phenotypes via Suppressing miR-1253-Mediated DDAH1 Inhibition in Breast Cancer." Cancer Management and Research Volume 13 (January 2021): 1–11. http://dx.doi.org/10.2147/cmar.s273783.

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43

Tomlinson, James, Ben Caplin, Olga Boruc, Pedro Cutillas, Dirk Dorman, Peter Faull, Sanjay Khadayate, et al. "Reduced renal dimethylarginine dimethylaminohydrolase 1 (DDAH1) activity protects against progressive kidney fibrosis and eGFR decline." Nitric Oxide 42 (November 2014): 130–31. http://dx.doi.org/10.1016/j.niox.2014.09.095.

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Liu, Yun-En, Cang-Ci Tong, Yu-Biao Zhang, Pei-Fang Cong, Xiu-Yun Shi, Ying Liu, Lin Shi, Zhou Tong, Hong-Xu Jin, and Ming-Xiao Hou. "Chitosan oligosaccharide ameliorates acute lung injury induced by blast injury through the DDAH1/ADMA pathway." PLOS ONE 13, no. 2 (February 7, 2018): e0192135. http://dx.doi.org/10.1371/journal.pone.0192135.

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Jia, Su-Jie, Kui Song, Guang-Ping Wang, Yuan-Jian Li, Hong-Ya Xin, De-Jian Jiang, and Fang-Ping Chen. "Regulation by DDAH/ADMA pathway of lipopolysaccharideinduced tissue factor expression in endothelial cells." Thrombosis and Haemostasis 97, no. 05 (2007): 830–38. http://dx.doi.org/10.1160/th06-11-0656.

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SummaryPrevious studies have shown the regulatory effect of nitric oxide (NO) on endotoxin-induced tissue factor (TF) in endothelial cells. Asymmetric dimethylarginine (ADMA), a major endogenous NO synthase (NOS) inhibitor, could inhibit NO production in vivo and in vitro. ADMA and its major hydrolase dimethylarginine dimethylaminohydrolase (DDAH) have recently been thought of as a novel regulatory system of endogenous NO production. The aim of the present study was to determine whether the DDAH/ADMA pathway is involved in the effect of lipopolysaccharide (LPS) on TF expression in endothelial cells. Human umbilical vein endothelial cells (HUVECs) were treated with LPS (1 µ g/ml) to induce TF expression. Exogenous ADMA significantly enhanced the increase in both TF mRNA level and activity induced by LPS, whereas L-arginine, the NOS substrate, markedly attenuated the LPS-induced TF increment. LPS markedly increased the level of ADMA in cultured medium and decreased DDAH activity in endothelial cells, and overexpression of DDAH2 could significantly suppress LPS-induced TF increment in endothelial cells. LPS could increase intracellular reactive oxygen species (ROS) production and activate nuclear factor-κ B, which were enhanced by exogenous ADMA and attenuated by either L-arginine or overexpression of DDAH2. Therefore, our present results for the first time suggest that the DDAH/ADMA pathway can regulate LPS-inducedTF expression via ROS-nuclear factor- κ B-dependent pathway in endothelial cells.

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Hulin, Julie-Ann, Sara Tommasi, David Elliot, and Arduino A. Mangoni. "Small molecule inhibition of DDAH1 significantly attenuates triple negative breast cancer cell vasculogenic mimicry in vitro." Biomedicine & Pharmacotherapy 111 (March 2019): 602–12. http://dx.doi.org/10.1016/j.biopha.2018.12.117.

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Wojciak-Stothard, Beata, Belen Torondel, Lan Zhao, Thomas Renné, and James M. Leiper. "Modulation of Rac1 Activity by ADMA/DDAH Regulates Pulmonary Endothelial Barrier Function." Molecular Biology of the Cell 20, no. 1 (January 2009): 33–42. http://dx.doi.org/10.1091/mbc.e08-04-0395.

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Endogenously produced nitric oxide synthase inhibitor, asymmetric methylarginine (ADMA) is associated with vascular dysfunction and endothelial leakage. We studied the role of ADMA, and the enzymes metabolizing it, dimethylarginine dimethylaminohydrolases (DDAH) in the regulation of endothelial barrier function in pulmonary macrovascular and microvascular cells in vitro and in lungs of genetically modified heterozygous DDAHI knockout mice in vivo. We show that ADMA increases pulmonary endothelial permeability in vitro and in in vivo and that this effect is mediated by nitric oxide (NO) acting via protein kinase G (PKG) and independent of reactive oxygen species formation. ADMA-induced remodeling of actin cytoskeleton and intercellular adherens junctions results from a decrease in PKG-mediated phosphorylation of vasodilator-stimulated phosphoprotein (VASP) and a subsequent down-regulation of Rac1 activity. The effects of ADMA on endothelial permeability, Rac1 activation and VASP phosphorylation are prevented by overexpression of active DDAHI and DDAHII, whereas inactive DDAH mutants have no effect. These findings demonstrate for the first time that ADMA metabolism critically determines pulmonary endothelial barrier function by modulating Rac1-mediated remodeling of the actin cytoskeleton and intercellular junctions.

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Trittmann, Jennifer K., Hanadi Almazroue, Yi Jin, John Barba, Avante D. Milton, and Leif D. Nelin. "DDAH1 Overexpression in Human Pulmonary Vascular Endothelial Cells Co‐Cultured with Human Pulmonary Artery Smooth Muscle Cells." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.01937.

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Chen, Po, Ke Xia, Zhenyu Zhao, Xu Deng, and Tianlun Yang. "Atorvastatin modulates the DDAH1/ADMA system in high-fat diet-induced insulin-resistant rats with endothelial dysfunction." Vascular Medicine 17, no. 6 (November 26, 2012): 416–23. http://dx.doi.org/10.1177/1358863x12467492.

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Mei, Xi, Jun Zeng, Dong-Fang Liu, Ye Zhao, Hui-Lan Yang, Yao Li, Ping Qiu, and Ming-Wei Tang. "Abnormalities of the PRMT1-ADMA-DDAH1 metabolism axis and probucol treatment in diabetic patients and diabetic rats." Annals of Palliative Medicine 10, no. 3 (March 2021): 3343–53. http://dx.doi.org/10.21037/apm-21-417.

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