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https://www.readbyqxmd.com/read/29659998/the-arginine-methyltransferase-carm1-represses-p300%C3%A2-act%C3%A2-crem%C3%AF-activity-and-is-required-for-spermiogenesis
#1
Jianqiang Bao, Sophie Rousseaux, Jianjun Shen, Kevin Lin, Yue Lu, Mark T Bedford
CARM1 is a protein arginine methyltransferase (PRMT) that has been firmly implicated in transcriptional regulation. However, the molecular mechanisms by which CARM1 orchestrates transcriptional regulation are not fully understood, especially in a tissue-specific context. We found that Carm1 is highly expressed in the mouse testis and localizes to the nucleus in spermatids, suggesting an important role for Carm1 in spermiogenesis. Using a germline-specific conditional Carm1 knockout mouse model, we found that it is essential for the late stages of haploid germ cell development...
April 5, 2018: Nucleic Acids Research
https://www.readbyqxmd.com/read/29628326/identification-of-a-novel-selective-small-molecule-inhibitor-of-protein-arginine-methyltransferase-5-prmt5-by-virtual-screening-resynthesis-and-biological-evaluations
#2
Kongkai Zhu, Chengshi Jiang, Hongrui Tao, Jingqiu Liu, Hua Zhang, Cheng Luo
As one of the most promising anticancer target in protein arginine methyltransferase (PRMT) family, PRMT5 has been drawing more and more attentions, and many efforts have been devoted to develop its inhibitors. In this study, three PRMT5 inhibitors (9, 16, and 23) with novel scaffolds were identified by performing pharmacophore- and docking-based virtual screening combined with in vitro radiometric-based scintillation proximity assay (SPA). Substructure search based on the scaffold of the most active 9 afforded 26 additional analogues, and SPA results indicated that two analogues (9-1 and 9-2) showed increased PRMT5 inhibitory activity compared with the parental compound...
March 30, 2018: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/29603830/prmt9-promotes-hepatocellular-carcinoma-invasion-and-metastasis-via-activating-pi3k-akt-gsk-3%C3%AE-snail-signalling
#3
Hai Jiang, Zhenyu Zhou, Shaowen Jin, Kang Xu, Heyun Zhang, Junyang Xu, Qing Sun, Jie Wang, Junyao Xu
Protein arginine methyltransferases (PRMTs) catalyse protein arginine methylation and play an important role in many biological processes. Aberrant PRMT expression in tumour cells has been documented in several common cancer types; however, its precise contribution to hepatocellular carcinoma (HCC) cell invasion and metastasis is not fully understood. In this study, we identified a new oncogene, PRMT9, whose overexpression strongly promotes HCC invasion and metastasis. PRMT9 expression was detected more frequently in HCC tissues than in adjacent noncancerous tissues...
March 30, 2018: Cancer Science
https://www.readbyqxmd.com/read/29603824/expression-of-protein-arginine-methyltransferase-5-in-oral-squamous-cell-carcinoma-and-its-significance-in-epithelial-to-mesenchymal-transition
#4
Yusuke Amano, Daisuke Matsubara, Taichiro Yoshimoto, Tomoko Tamura, Hiroshi Nishino, Yoshiyuki Mori, Toshiro Niki
Protein arginine methyltransferases (PRMT) 5, a member of type II arginine methyltransferases, catalyzes the symmetrical dimethylation of arginine residues on histone and non-histone substrates. Although the overexpression of PRMT5 has been reported in various cancers, its role in oral squamous cell carcinoma (OSCC) has not been elucidated. In the present study, we immunohistochemically examined the expression of PRMT5 in surgically resected oral epithelial dysplasia (OED, n = 8), oral intraepithelial neoplasia (OIN)/carcinoma in situ (CIS) (n = 11) and OSCC (n = 52) with or without contiguous OED lesions...
March 30, 2018: Pathology International
https://www.readbyqxmd.com/read/29535867/detection-of-prmt1-inhibitors-with-stopped-flow-fluorescence
#5
Kun Qian, Hao Hu, Hui Xu, Y George Zheng
Protein arginine methyltransferases (PRMTs) are crucial epigenetic regulators in eukaryotic organisms that serve as histone writers for chromatin remodeling. PRMTs also methylate a variety of non-histone protein substrates to modulate their function and activity. The development of potent PRMT inhibitors has become an emerging and imperative research area in the drug discovery field to provide novel therapeutic agents for treating diseases and as tools to investigate the biological functions of PRMTs. PRMT1 is the major type I enzyme that catalyzes the formation of asymmetric dimethyl arginine, and PRMT1 plays important regulatory roles in signal transduction, transcriptional activation, RNA splicing, and DNA repair...
2018: Signal Transduction and Targeted Therapy
https://www.readbyqxmd.com/read/29501774/protein-arginine-methyltransferase-5-mediates-enolase-1-cell-surface-trafficking-in-human-lung-adenocarcinoma-cells
#6
Dariusz Zakrzewicz, Miroslava Didiasova, Marcus Krüger, Benedetto Daniele Giaimo, Tilman Borggrefe, Maren Mieth, Andreas C Hocke, Anna Zakrzewicz, Liliana Schaefer, Klaus T Preissner, Malgorzata Wygrecka
OBJECTIVES: Enolase-1-dependent cell surface proteolysis plays an important role in cell invasion. Although enolase-1 (Eno-1), a glycolytic enzyme, has been found on the surface of various cells, the mechanism responsible for its exteriorization remains elusive. Here, we investigated the involvement of post-translational modifications (PTMs) of Eno-1 in its lipopolysaccharide (LPS)-triggered trafficking to the cell surface. RESULTS: We found that stimulation of human lung adenocarcinoma cells with LPS triggered the monomethylation of arginine 50 (R50me) within Eno-1...
March 1, 2018: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/29471522/prmt-5-converts-monomethylarginines-into-symmetrical-dimethylarginines-in-caenorhabditis-elegans
#7
Akihiko Kanou, Koichiro Kako, Keiko Hirota, Akiyoshi Fukamizu
No abstract text is available yet for this article.
February 19, 2018: Journal of Biochemistry
https://www.readbyqxmd.com/read/29471495/arginine-methylation-of-the-c-terminus-rgg-motif-promotes-top3b-topoisomerase-activity-and-stress-granule-localization
#8
Lifeng Huang, Zhihao Wang, Nithya Narayanan, Yanzhong Yang
DNA topoisomerase 3B (TOP3B) is unique among all mammalian topoisomerases for its dual activities that resolve both DNA and RNA topological entanglements to facilitate transcription and translation. However, the mechanism by which TOP3B activity is regulated is still elusive. Here, we have identified arginine methylation as an important post-translational modification (PTM) for TOP3B activity. Protein arginine methyltransferase (PRMT) 1, PRMT3 and PRMT6 all methylate TOP3B in vitro at its C-terminal arginine (R) and glycine (G)-rich motif...
February 19, 2018: Nucleic Acids Research
https://www.readbyqxmd.com/read/29456659/prmt1-rbm15-axis-regulates-megakaryocytic-differentiation-of-human-umbilical-cord-blood-cd34-cells
#9
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
#10
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
#11
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...
May 1, 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
#12
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-emt-mediated-tyrosine-kinase-inhibitor-resistance-in-nsclc
#13
COMPARATIVE STUDY
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...
February 5, 2018: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29226078/identification-and-in-silico-structural-analysis-of-gallus-gallus-protein-arginine-methyltransferase-4-prmt4
#14
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
#15
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. C2 C12 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
#16
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
#17
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...
January 1, 2018: 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
#18
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...
April 2018: 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
#19
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...
January 2018: Endocrine
https://www.readbyqxmd.com/read/29112789/kinetic-analysis-of-prmt1-reveals-multifactorial-processivity-and-a-sequential-ordered-mechanism
#20
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 revealed that human protein arginine N-methyltransferase 1 (PRMT1) enzyme kinetics are dependent on substrate sequence. Further, peptides containing an Nη-hydroxyarginine generally demonstrated substrate inhibition and had improved KM values, which evoked a possible role in inhibitor design...
January 4, 2018: Chembiochem: a European Journal of Chemical Biology
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