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https://www.readbyqxmd.com/read/29456659/prmt1-rbm15-axis-regulates-megakaryocytic-differentiation-of-human-umbilical-cord-blood-cd34-cells
#1
Shuiling Jin, Yanfang Mi, Jing Song, Peipei Zhang, Yanyan Liu
Protein arginine methyltransferase 1 (PRMT1) serves pivotal roles in various cellular processes. However, its role in megakaryocytic differentiation has not been clearly reported. The aim of the present study was to explore the role of the PRMT-RNA binding motif protein 15 (RBM15) axis in human MK differentiation and the feasibility of targeting PRMT1 for leukemia treatment. In the present study, PRMT1 was overexpressed and the RBM15 protein was knocked down in human umbilical cord blood cluster of differentiation (CD)34+ cells and the cells were then cultured in megakaryocytic differentiation medium...
March 2018: Experimental and Therapeutic Medicine
https://www.readbyqxmd.com/read/29378138/phe-71-in-type-iii-trypanosomal-protein-arginine-methyltransferase-7-tbprmt7-restricts-the-enzyme-to-monomethylation
#2
Tamar Caceres, Abishek Thakur, Owen M Price, Nicole Ippolito, Jun Li, Jun Qu, Orlando Acevedo, Joan Michelle Hevel
Protein arginine methyltransferase 7 (PRMT7) is unique within the PRMT family as it is the only isoform known to exclusively make monomethylarginine (MMA). Given its role in epigenetics, the mechanistic basis for the strict monomethylation activity is under investigation. It is thought that PRMT7 enzymes are unable to add a second methyl group because of steric hindrances in the active site which restrict them to monomethylation. To test this, we probed the active site of Trypanosomal PRMT7 (TbPRMT7) using accelerated molecular dynamics, site-directed mutagenesis, kinetic, binding, and product analyses...
January 29, 2018: Biochemistry
https://www.readbyqxmd.com/read/29361115/the-gata-transcription-factor-elt-2-modulates-both-the-expression-and-methyltransferase-activity-of-prmt-1-in-caenorhabditis-elegans
#3
Sho Araoi, Hiroaki Daitoku, Atsuko Yokoyama, Koichiro Kako, Keiko Hirota, Akiyoshi Fukamizu
Protein Arginine Methyltransferase 1 (PRMT1) catalyzes asymmetric arginine dimethylation of cellular proteins and thus modulates various biological processes, including gene regulation, RNA metabolism, cell signaling and DNA repair. Since prmt-1 null mutant completely abolishes asymmetric dimethylarginine in C. elegans, PRMT-1 is thought to play a crucial role in determining levels of asymmetric arginine dimethylation. However, the mechanism underlying the regulation of PRMT-1 activity remains largely unknown...
January 18, 2018: Journal of Biochemistry
https://www.readbyqxmd.com/read/29346429/the-farnesoid-x-receptor-agonist-obeticholic-acid-upregulates-biliary-excretion-of-asymmetric-dimethylarginine-via-mate-1-during-hepatic-ischemia-reperfusion-injury
#4
Andrea Ferrigno, Laura Giuseppina Di Pasqua, Clarissa Berardo, Veronica Siciliano, Vittoria Rizzo, Luciano Adorini, Plinio Richelmi, Mariapia Vairetti
BACKGROUND: We previously showed that increased asymmetric dimethylarginine (ADMA) biliary excretion occurs during hepatic ischemia/reperfusion (I/R), prompting us to study the effects of the farnesoid X receptor (FXR) agonist obeticholic acid (OCA) on bile, serum and tissue levels of ADMA after I/R. MATERIAL AND METHODS: Male Wistar rats were orally administered 10mg/kg/day of OCA or vehicle for 5 days and were subjected to 60 min partial hepatic ischemia or sham-operated...
2018: PloS One
https://www.readbyqxmd.com/read/29337056/comparison-of-epithelial-mesenchymal-transition-mediated-tyrosine-kinase-inhibitor-resistance-in-non-small-cell-lung-cancer-cell-lines-with-wild-type-egfr-and-mutant-type-egfr
#5
Tsatsral Iderzorig, Joseph Kellen, Chike Osude, Sanjana Singh, James A Woodman, Christian Garcia, Neelu Puri
In the United States, lung cancer is the second most common cancer in men and women. In 2017, 222,500 new cases and 155,870 deaths from lung cancer are estimated to have occurred. A tyrosine kinase receptor, epidermal growth factor receptor (EGFR) is over expressed or mutated in non-small cell lung cancer (NSCLC) resulting in increased cell proliferation and survival. Tyrosine kinase inhibitors (TKIs) are currently being used as therapy for NSCLC patients, however, they have limited efficacy in NSCLC patients due to acquisition of resistance...
January 11, 2018: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29226078/identification-and-in%C3%A2-silico-structural-analysis-of-gallus-gallus-protein-arginine-methyltransferase-4-prmt4
#6
Hannah Berberich, Felix Terwesten, Sinja Rakow, Peeyush Sahu, Caroline Bouchard, Marion Meixner, Sjaak Philipsen, Peter Kolb, Uta-Maria Bauer
Protein arginine methyltransferase 4 (PRMT4) is an essential epigenetic regulator of fundamental and conserved processes during vertebrate development, such as pluripotency and differentiation. Surprisingly, PRMT4 homologs have been identified in nearly all vertebrate classes except the avian genome. This raises the possibility that in birds PRMT4 functions are taken over by other PRMT family members. Here, we reveal the existence of a bona fide PRMT4 homolog in the chicken, Gallus gallus. Using a biochemical approach, we initially purified a putative chicken PRMT4 protein and thus provided the first evidence for the presence of an endogenous PRMT4-specific enzymatic activity toward histone H3 arginine 17 (H3R17) in avian cells...
December 2017: FEBS Open Bio
https://www.readbyqxmd.com/read/29208765/protein-arginine-methyltransferase-expression-and-activity-during-myogenesis
#7
Nicole Y Shen, Sean Y Ng, Stephen L Toepp, Vladimir Ljubicic
Despite the emerging importance of protein arginine methyltransferases (PRMTs) in regulating skeletal muscle plasticity, PRMT biology during muscle development is complex and not completely understood. Therefore, our purpose was to investigate PRMT1, -4, and -5 expression and function in skeletal muscle cells during the phenotypic remodeling elicited by myogenesis. C2C12 muscle cell maturation, assessed during the myoblast (MB) stage, and during days 1, 3, 5, and 7 of differentiation, was employed as an in vitro model of myogenesis...
February 28, 2018: Bioscience Reports
https://www.readbyqxmd.com/read/29163212/regulation-of-skeletal-muscle-plasticity-by-protein-arginine-methyltransferases-and-their-potential-roles-in-neuromuscular-disorders
#8
REVIEW
Derek W Stouth, Tiffany L vanLieshout, Nicole Y Shen, Vladimir Ljubicic
Protein arginine methyltransferases (PRMTs) are a family of enzymes that catalyze the methylation of arginine residues on target proteins, thereby mediating a diverse set of intracellular functions that are indispensable for survival. Indeed, full-body knockouts of specific PRMTs are lethal and PRMT dysregulation has been implicated in the most prevalent chronic disorders, such as cancers and cardiovascular disease (CVD). PRMTs are now emerging as important mediators of skeletal muscle phenotype and plasticity...
2017: Frontiers in Physiology
https://www.readbyqxmd.com/read/29154828/interaction-assessments-of-the-first-s-adenosylmethionine-competitive-inhibitor-and-the-essential-interacting-partner-methylosome-protein-50-with-protein-arginine-methyltransferase-5-by-combined-computational-methods
#9
Kongkai Zhu, Cheng-Shi Jiang, Junchi Hu, Xigong Liu, Xue Yan, Hongrui Tao, Cheng Luo, Hua Zhang
Protein arginine methyltransferase 5 (PRMT5) is the most promising anticancer target in PRMT family. In this study, based on the first S-adenosylmethionine (SAM) competitive small molecule inhibitor (17, compound number is from original paper) of PRMT5 reported in our recent paper, we determined the molecular mechanism of 17 interacting with PRMT5 by computational methods. Previously reported CMP5 was also thought of as a SAM competitive inhibitor of PRMT5, but the direct inhibition activity against PRMT5 at enzymatic level was not provided...
November 14, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29131380/upregulation-of-prmt6-by-lps-suppresses-klotho-expression-through-interaction-with-nf-%C3%AE%C2%BAb-in-glomerular-mesangial-cells
#10
Kuen-Daw Tsai, Wen-Xi Lee, Wei Chen, Bo-Yu Chen, Kuan-Lin Chen, Tzu-Chia Hsiao, Sue-Hong Wang, Yi-Ju Lee, Shan-Yuan Liang, Jia-Ching Shieh, Ting-Hui Lin
Lipopolysaccharide (LPS) released from gram-negative bacteria stimulates immune responses in infected cells. Epigenetic modifications such as DNA methylation and protein methylation modulate LPS-induced innate immune gene expressions. Expression of the Klotho protein decreased with LPS treatment in rats. In a cellular model, information regarding the effect of LPS on Klotho expression was meager. In the present study, we demonstrated that LPS triggered global DNA and protein methylation in glomerular mesangial MES-13 cells...
November 13, 2017: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/29128891/prmt1-promotes-hyperglycemia-in-a-foxo1-dependent-manner-affecting-glucose-metabolism-during-hypobaric-hypoxia-exposure-in-rat-model
#11
Susovon Bayen, Supriya Saini, Priya Gaur, Arul Joseph Duraisamy, Alpesh Kumar Sharma, Karan Pal, Praveen Vats, Shashi Bala Singh
PURPOSE: High-altitude (HA) environment causes changes in cellular metabolism among unacclimatized humans. Previous studies have revealed that insulin-dependent activation of protein kinase B (Akt) regulates metabolic processes via discrete transcriptional effectors. Moreover, protein arginine methyltransferase (PRMT)1-dependent arginine modification of forkhead box other (FoxO)1 protein interferes with Akt-dependent phosphorylation. The present study was undertaken to test the involvement of PRMT1 on FoxO1 activation during hypobaric hypoxia (HH) exposure in rat model...
November 11, 2017: Endocrine
https://www.readbyqxmd.com/read/29112789/kinetic-analysis-of-prmt1-reveals-multifactorial-processivity-and-a-sequential-ordered-mechanism
#12
Jennifer I Brown, Timo Koopmans, Jolinde van Strien, Nathaniel I Martin, Adam Frankel
Arginine methylation is a prevalent post-translational modification in eukaryotic cells. Two significant debates exist within the field: do these enzymes dimethylate their substrates in a processive or distributive manner, and do these enzymes operate using a random or sequential method of bisubstrate binding? We reveal human protein arginine N-methyltransferase 1 (PRMT1) enzyme kinetics are dependent on substrate sequence. Further, peptides containing a Nη-hydroxyarginine generally demonstrate substrate inhibition and have improved KM values, which evokes a possible role in inhibitor design...
November 7, 2017: Chembiochem: a European Journal of Chemical Biology
https://www.readbyqxmd.com/read/29112628/exercise-induced-protein-arginine-methyltransferase-expression-in-skeletal-muscle
#13
Tiffany L vanLieshout, Derek W Stouth, Tania Tajik, Vladimir Ljubicic
PURPOSE: This study aimed to determine protein arginine methyltransferase 1 (PRMT1), -4 (also known as coactivator-associated arginine methyltransferase 1; CARM1), and -5 expression and function during acute, exercise-induced skeletal muscle remodelling in vivo. METHODS: C57BL/6 mice were assigned to one of three experimental groups: sedentary, acute bout of exercise, or acute exercise followed by 3 hours of recovery. The mice in the exercise groups performed a single bout of treadmill running at 15 m/min for 90 minutes...
November 6, 2017: Medicine and Science in Sports and Exercise
https://www.readbyqxmd.com/read/29099132/development-of-an-alphalisa-high-throughput-technique-to-screen-for-small-molecule-inhibitors-targeting-protein-arginine-methyltransferases
#14
Lakshmi Prabhu, Lan Chen, Han Wei, Özlem Demir, Ahmad Safa, Lifan Zeng, Rommie E Amaro, Bert H O'Neil, Zhon-Yin Zhang, Tao Lu
The protein arginine methyltransferase (PRMT) family of enzymes comprises nine family members in mammals. They catalyze arginine methylation, either monomethylation or symmetric/asymmetric dimethylation of histone and non-histone proteins. PRMT methylation of its substrate proteins modulates cellular processes such as signal transduction, transcription, and mRNA splicing. Recent studies have linked overexpression of PRMT5, a member of the PRMT superfamily, to oncogenesis, making it a potential target for cancer therapy...
November 21, 2017: Molecular BioSystems
https://www.readbyqxmd.com/read/29099056/ammonia-reduces-intracellular-asymmetric-dimethylarginine-in-cultured-astrocytes-stimulating-its-y%C3%A2-%C2%BAlat2-carrier-mediated-loss
#15
Krzysztof Milewski, Małgorzata Bogacińska-Karaś, Inez Fręśko, Wojciech Hilgier, Radosław Jaźwiec, Jan Albrecht, Magdalena Zielińska
Previously we had shown that ammonia stimulates nitric oxide (NO) synthesis in astrocytes by increasing the uptake of the precursor amino acid, arginine via the heteromeric arginine/glutamine transporter y⁺LAT2. Ammonia also increases the concentration in the brain of the endogenous inhibitor of nitric oxide synthases (NOS), asymmetric dimethylarginine (ADMA), but distribution of ADMA surplus between the intraastrocytic and extracellular compartments of the brain has not been studied. Here we tested the hypothesis that ammonia modulates the distribution of ADMA and its analog symmetric dimethylarginine (SDMA) between the two compartments of the brain by competition with arginine for the y⁺LAT2 transporter...
November 2, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/29092819/protein-arginine-methyltransferase-expression-localization-and-activity-during-disuse-induced-skeletal-muscle-plasticity
#16
Derek W Stouth, Alexander Manta, Vladimir Ljubicic
Protein arginine methyltransferase 1 (PRMT1), PRMT4, and PRMT5 catalyze the methylation of arginine residues on target proteins. Previous work suggests that these enzymes regulate skeletal muscle plasticity. However, the function of PRMTs during disuse-induced muscle remodelling is unknown. The purpose of our study was to determine whether denervation-induced muscle disuse alters PRMT expression and activity in skeletal muscle, as well as to contextualize PRMT biology within the early disuse-evoked events that precede atrophy, which remain largely undefined...
November 1, 2017: American Journal of Physiology. Cell Physiology
https://www.readbyqxmd.com/read/29026071/arginine-methylation-catalyzed-by-prmt1-is-required-for-b-cell-activation-and-differentiation
#17
Simona Infantino, Amanda Light, Kristy O'Donnell, Vanessa Bryant, Danielle T Avery, Michael Elliott, Stuart G Tangye, Gabrielle Belz, Fabienne Mackay, Stephane Richard, David Tarlinton
Arginine methylation catalyzed by protein arginine methyltransferases (PRMT) is a common post-translational modification in mammalian cells, regulating many important functions including cell signalling, proliferation and differentiation. Here we show the role of PRMT1 in B-cell activation and differentiation. PRMT1 expression and activity in human and mouse peripheral B cells increases in response to in vitro or in vivo activation. Deletion of the Prmt1 gene in mature B cells establishes that although the frequency and phenotype of peripheral B cell subsets seem unaffected, immune responses to T-cell-dependent and -independent antigens are substantially reduced...
October 12, 2017: Nature Communications
https://www.readbyqxmd.com/read/29019697/development-of-potent-type-i-protein-arginine-methyltransferase-prmt-inhibitors-of-leukemia-cell-proliferation
#18
Chen Wang, Hao Jiang, Jia Jin, Yiqian Xie, Zhifeng Chen, Hao Zhang, Fulin Lian, Yu-Chih Liu, Chenhua Zhang, Hong Ding, Shijie Chen, Naixia Zhang, Yuanyuan Zhang, Hualiang Jiang, Kaixian Chen, Fei Ye, Zhiyi Yao, Cheng Luo
Protein Arginine Methyltransferases (PRMTs) are crucial players in diverse biological processes, and dysregulation of PRMTs has been linked to various human diseases, especially cancer. Therefore, small molecules targeting PRMTs have profound impact for both academic functional studies and clinical disease treatment. Here, we report the discovery of N(1)-(2-((2-chlorophenyl)thio)benzyl)-N(1)-methylethane-1,2-diamine (28d, DCPR049_12), a highly potent inhibitor of type I PRMTs that has good selectivity against a panel of other methyltransferases...
October 27, 2017: Journal of Medicinal Chemistry
https://www.readbyqxmd.com/read/28987382/arginine-methyltransferase-inhibitor-1-inhibits-gastric-cancer-by-downregulating-eif4e-and-targeting-prmt5
#19
Baolai Zhang, Su Zhang, Lijuan Zhu, Xue Chen, Yunfeng Zhao, Li Chao, Juanping Zhou, Xing Wang, Xinyang Zhang, Nengqian Ma
Arginine methylation is carried out by protein arginine methyltransferase (PRMTs) family. Arginine methyltransferase inhibitor 1 (AMI-1) is mainly used to inhibit type I PRMT activity in vitro. However, the effects of AMI-1 on type II PRMT5 activity and gastric cancer (GC) remain unclear. In this study, we provided the first evidence that AMI-1 significantly inhibited GC cell proliferation and migration while induced GC cell apoptosis, and reduced the expression of PRMT5, eukaryotic translation initiation factor 4E (eIF4E), symmetric dimethylation of histone 3 (H3R8me2s) and histone 4 (H4R3me2s)...
October 4, 2017: Toxicology and Applied Pharmacology
https://www.readbyqxmd.com/read/28943242/csnk1a1-regulates-prmt1-to-maintain-the-progenitor-state-in-self-renewing-somatic-tissue
#20
Xiaomin Bao, Zurab Siprashvili, Brian J Zarnegar, Rajani M Shenoy, Eon J Rios, Natalie Nady, Kun Qu, Angela Mah, Daniel E Webster, Adam J Rubin, Glenn G Wozniak, Shiying Tao, Joanna Wysocka, Paul A Khavari
Somatic progenitors sustain tissue self-renewal while suppressing premature differentiation. Protein arginine methyltransferases (PRMTs) affect many processes; however, their role in progenitor function is incompletely understood. PRMT1 was found to be the most highly expressed PRMT in epidermal progenitors and the most downregulated PRMT during differentiation. In targeted mouse knockouts and in long-term regenerated human mosaic epidermis in vivo, epidermal PRMT1 loss abolished progenitor self-renewal and led to premature differentiation...
October 23, 2017: Developmental Cell
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