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https://www.readbyqxmd.com/read/28643125/the-role-of-prmt1-in-egfr-methylation-and-signaling-in-mda-mb-468-triple-negative-breast-cancer-cells
#1
Katsuya Nakai, Weiya Xia, Hsin-Wei Liao, Mitsue Saito, Mien-Chie Hung, Hirohito Yamaguchi
BACKGROUND: Epidermal growth factor receptor (EGFR) is often overexpressed in triple-negative breast cancer (TNBC). However, clinical studies have shown that therapies against EGFR are not effective in patients with TNBC. Recently, it has been reported that arginine 198/200 in EGFR extracellular domain is methylated by PRMT1 and that the methylation confers resistance to EGFR monoclonal antibody cetuximab in colorectal cancer cells. To explore a potential mechanism underlying intrinsic resistance to anti-EGFR therapy in TNBC, we investigated the role of PRMT1 in EGFR methylation and signaling in MDA-MB-468 (468) TNBC cells...
June 22, 2017: Breast Cancer: the Journal of the Japanese Breast Cancer Society
https://www.readbyqxmd.com/read/28604453/management-of-primary-retroperitoneal-mucinous-tumors-a-retrospective-meta-analysis
#2
Benjamin Wolf, Christin Kunert, Lars-Christian Horn, Jens Einenkel
OBJECTIVE: Primary retroperitoneal mucinous tumors (PRMTs) are rare epithelial neoplasms arising in the retroperitoneal space whose pathogenesis is poorly understood. To date, only single-case reports and small case series on diagnosis and management of these tumors exist. The aim of this first-time meta-analysis was to provide more reliable data to inform the management of PRMTs. METHODS: Database searches were conducted to identify case reports and case series between the years of 1975 and 2015...
June 10, 2017: International Journal of Gynecological Cancer
https://www.readbyqxmd.com/read/28506031/identification-and-characterization-of-protein-arginine-methyltransferase-1-in-acanthamoeba-castellanii
#3
Eun-Kyung Moon, Hyun-Hee Kong, Yeonchul Hong, Hae-Ahm Lee, Fu-Shi Quan
Protein arginine methyltransferase (PRMT) is an important epigenetic regulator in eukaryotic cells. During encystation, an essential process for Acanthamoeba survival, the expression of a lot of genes involved in the encystation process has to be regulated in order to be induced or inhibited. However, the regulation mechanism of these genes is yet unknown. In this study, the full-length 1,059 bp cDNA sequence of Acanthamoeba castellanii PRMT1 (AcPRMT1) was cloned for the first time. The AcPRMT1 protein comprised of 352 amino acids with a SAM-dependent methyltransferase PRMT-type domain...
April 2017: Korean Journal of Parasitology
https://www.readbyqxmd.com/read/28502835/the-adma-ddah-no-pathway-in-human-vein-endothelial-cells-exposed-to-arsenite
#4
Citlalli Osorio-Yáñez, Miguel Chin-Chan, Luz C Sánchez-Peña, Octavio G Atzatzi-Aguilar, Jesus A Olivares-Reyes, José Segovia, Luz M Del Razo
Inorganic arsenic (iAs) exposure is related to cardiovascular disease, which is characterized by endothelial dysfunction and nitric oxide (NO) depletion. The mechanisms underlying NO depletion as related to iAs exposure are not fully understood. The endogenous inhibitor of nitric oxide synthase, asymmetric dimethylarginine (ADMA), might be a molecular target of iAs. ADMA concentrations are regulated by proteins involved in its synthesis (arginine methyl transferase 1 [PRMT-1]) and degradation (dimethylarginine dimethylaminohydrolase [DDAH])...
May 11, 2017: Toxicology in Vitro: An International Journal Published in Association with BIBRA
https://www.readbyqxmd.com/read/28454353/prmt8-demonstrates-variant-specific-expression-in-cancer-cells-and-correlates-with-patient-survival-in-breast-ovarian-and-gastric-cancer
#5
Sarah J Hernandez, David M Dolivo, Tanja Dominko
Recent emphasis has been placed on the role of epigenetic regulators and epigenetic marks as biomarkers for cancer diagnosis and prognosis, and as therapeutic targets for treatment. One such class of regulators is the protein arginine methyltransferase (PRMT) family. The present study examined available curated data regarding the expression and alteration of one of the least studied PRMT family members, PRMT8, in various types of cancer and cancer cell lines. Publicly available cancer data on PRMT8 expression were examined using the Human Protein Atlas and the Kaplan-Meier Plotter, and reverse transcription-polymerase chain reaction was used to screen a selection of human cell lines for variant-specific PRMT8 expression...
March 2017: Oncology Letters
https://www.readbyqxmd.com/read/28441492/caenorhabditis-elegans-prmt-7-and-prmt-9-are-evolutionarily-conserved-protein-arginine-methyltransferases-with-distinct-substrate-specificities
#6
Andrea Hadjikyriacou, Steven G Clarke
Caenorhabditis elegans protein arginine methyltransferases PRMT-7 and PRMT-9 are two evolutionarily conserved enzymes, with distinct orthologs in plants, invertebrates, and vertebrates. Biochemical characterization of these two enzymes reveals that they share much in common with their mammalian orthologs. C. elegans PRMT-7 produces only monomethylarginine (MMA) and preferentially methylates R-X-R motifs in a broad collection of substrates, including human histone peptides and RG-rich peptides. In addition, the activity of the PRMT-7 enzyme is dependent on temperature, the presence of metal ions, and the reducing agent dithiothreitol...
May 23, 2017: Biochemistry
https://www.readbyqxmd.com/read/28397890/discovery-and-optimization-of-selective-inhibitors-of-protein-arginine-methyltransferase-5-by-docking-based-virtual-screening
#7
Yan Ye, Bidong Zhang, Ruifeng Mao, Chenhua Zhang, Yulan Wang, Jing Xing, Yu-Chih Liu, Xiaomin Luo, Hong Ding, Yaxi Yang, Bing Zhou, Hualiang Jiang, Kaixian Chen, Cheng Luo, Mingyue Zheng
Protein arginine methyltransferase 5 (PRMT5) is a type II PRMT enzyme critical for diverse cellular processes and different types of cancers. Many efforts have been made to discover novel scaffold PRMT5 inhibitors. Herein, we report the discovery of DC_P33 as a hit compound of PRMT5 inhibitor, identified by molecular docking based virtual screening and (3)H-labeled radioactive methylation assays. Structure-activity relationship (SAR) analysis was performed on the analogs of DC_P33 and then structural modifications were done to improve its activity...
May 3, 2017: Organic & Biomolecular Chemistry
https://www.readbyqxmd.com/read/28330993/transition-state-mimics-are-valuable-mechanistic-probes-for-structural-studies-with-the-arginine-methyltransferase-carm1
#8
Matthijs J van Haren, Nils Marechal, Nathalie Troffer-Charlier, Agostino Cianciulli, Gianluca Sbardella, Jean Cavarelli, Nathaniel I Martin
Coactivator associated arginine methyltransferase 1 (CARM1) is a member of the protein arginine methyltransferase (PRMT) family and methylates a range of proteins in eukaryotic cells. Overexpression of CARM1 is implicated in a number of cancers, and it is therefore seen as a potential therapeutic target. Peptide sequences derived from the well-defined CARM1 substrate poly(A)-binding protein 1 (PABP1) were covalently linked to an adenosine moiety as in the AdoMet cofactor to generate transition state mimics...
April 4, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28301308/regenerating-muscle-with-arginine-methylation
#9
Roméo S Blanc, Stéphane Richard
Protein arginine methyltransferase (PRMT) is a family of nine proteins catalyzing the methylation of arginine residues. They were recently shown to be essential for proper regeneration of skeletal muscles. However, the mechanisms triggering the methylation event, as well as how the methylated substrates regulate muscle stem cell function and fate decision remain to be determined. This point-of-view will discuss the recent findings on the specific role of PRMT1, CARM1/PRMT4, PRMT5, and PRMT7 in muscle stem cell fate guidance, and shed light on the future challenges which could help defining the therapeutic potential of PRMT inhibitors against muscular disorders and aging...
May 27, 2017: Transcription
https://www.readbyqxmd.com/read/28285332/the-role-of-l-arginine-l-homoarginine-nitric-oxide-pathway-for-aortic-distensibility-and-intima-media-thickness-in-stroke-patients
#10
Arash Haghikia, Georgi Radoslavov Yanchev, Arslan Arinc Kayacelebi, Erik Hanff, Nils Bledau, Christian Widera, Kristina Sonnenschein, Aiden Haghikia, Karin Weissenborn, Johann Bauersachs, Udo Bavendiek, Dimitrios Tsikas
Asymmetric dimethylarginine (ADMA) and L-homoarginine (hArg) are L-arginine (Arg) metabolites derived from different pathways. Protein arginine N-methyltransferase (PRMT) and subsequent proteolysis of proteins containing methylarginine residues release ADMA. Arginine:glycine amidinotransferase (AGAT) converts Arg to hArg and guanidinoacetate (GAA). While high concentrations of ADMA and low concentrations of hArg in the blood have been established as cardiovascular risk markers, the cardiovascular relevance of GAA is still unexplored...
June 2017: Amino Acids
https://www.readbyqxmd.com/read/28279165/root-morphogenic-pathways-in-eucalyptus-grandis-are-modified-by-the-activity-of-protein-arginine-methyltransferases
#11
Krista L Plett, Anita E Raposo, Stephen Bullivant, Ian C Anderson, Sabine C Piller, Jonathan M Plett
BACKGROUND: Methylation of proteins at arginine residues, catalysed by members of the protein arginine methyltransferase (PRMT) family, is crucial for the regulation of gene transcription and for protein function in eukaryotic organisms. Inhibition of the activity of PRMTs in annual model plants has demonstrated wide-ranging involvement of PRMTs in key plant developmental processes, however, PRMTs have not been characterised or studied in long-lived tree species. RESULTS: Taking advantage of the recently available genome for Eucalyptus grandis, we demonstrate that most of the major plant PRMTs are conserved in E...
March 9, 2017: BMC Plant Biology
https://www.readbyqxmd.com/read/28173048/prmt-5-converts-monomethylarginines-into-symmetrical-dimethylarginines-in-caenorhabditis-elegans
#12
Akihiko Kanou, Koichiro Kako, Keiko Hirota, Akiyoshi Fukamizu
The transmethylation to arginine residues of proteins is catalyzed by protein arginine methyltransferases (PRMTs) that form monomethylarginine (MMA), asymmetric (ADMA) and symmetric dimethylarginines (SDMA). Although we previously demonstrated that the generation of ADMA residues in whole proteins is driven by PRMT-1 in Caenorhabditis elegans, much less is known about MMA and SDMA in vivo. In this study, we measured the amounts of different methylarginines in whole protein extracts made from wild-type (N2) C...
February 1, 2017: Journal of Biochemistry
https://www.readbyqxmd.com/read/28158808/simultaneous-ablation-of-prmt-1-and-prmt-5-abolishes-asymmetric-and-symmetric-arginine-dimethylations-in-caenorhabditis-elegans
#13
Keiko Hirota, Chihiro Shigekawa, Sho Araoi, Liang Sha, Takayuki Inagawa, Akihiko Kanou, Koichiro Kako, Hiroaki Daitoku, Akiyoshi Fukamizu
Protein arginine methyltransferases (PRMTs) catalyze the transfer of a methyl group from S-adenosylmethionine to arginine residues and are classified into two types: type I producing asymmetric dimethylarginine (ADMA) and type II producing symmetric dimethylarginine (SDMA). PRMTs have been shown to regulate many cellular processes, including signal transduction, transcriptional regulation and RNA processing. Since the loss-of-function mutation of PRMT1 and PRMT5, each of which is the predominant type I and II, respectively, causes embryonic lethality in mice, their physiological significance at the whole-body level remains largely unknown...
June 1, 2017: Journal of Biochemistry
https://www.readbyqxmd.com/read/28143887/comparative-monomethylarginine-proteomics-suggests-that-protein-arginine-methyltransferase-1-prmt1-is-a-significant-contributor-to-arginine-monomethylation-in-toxoplasma-gondii
#14
COMPARATIVE STUDY
Rama R Yakubu, Natalie C Silmon de Monerri, Edward Nieves, Kami Kim, Louis M Weiss
Arginine methylation is a common posttranslational modification found on nuclear and cytoplasmic proteins that has roles in transcriptional regulation, RNA metabolism and DNA repair. The protozoan parasite Toxoplasma gondii has a complex life cycle requiring transcriptional plasticity and has unique transcriptional regulatory pathways. Arginine methylation may play an important part in transcriptional regulation and splicing biology in this organism. The T. gondii genome contains five putative protein arginine methyltransferases (PRMTs), of which PRMT1 is important for cell division and growth...
April 2017: Molecular & Cellular Proteomics: MCP
https://www.readbyqxmd.com/read/28087667/prmt5-selective-inhibitors-suppress-inflammatory-t-cell-responses-and-experimental-autoimmune-encephalomyelitis
#15
Lindsay M Webb, Stephanie A Amici, Kyle A Jablonski, Himanshu Savardekar, Amanda R Panfil, Linsen Li, Wei Zhou, Kevin Peine, Vrajesh Karkhanis, Eric M Bachelder, Kristy M Ainslie, Patrick L Green, Chenglong Li, Robert A Baiocchi, Mireia Guerau-de-Arellano
In the autoimmune disease multiple sclerosis and its animal model, experimental autoimmune encephalomyelitis (EAE), expansion of pathogenic, myelin-specific Th1 cell populations drives active disease; selectively targeting this process may be the basis for a new therapeutic approach. Previous studies have hinted at a role for protein arginine methylation in immune responses, including T cell-mediated autoimmunity and EAE. However, a conclusive role for the protein arginine methyltransferase (PRMT) enzymes that catalyze these reactions has been lacking...
February 15, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/28061334/arginine-methylation-the-coming-of-age
#16
REVIEW
Roméo S Blanc, Stéphane Richard
Arginine methylation is a common post-translational modification functioning as an epigenetic regulator of transcription and playing key roles in pre-mRNA splicing, DNA damage signaling, mRNA translation, cell signaling, and cell fate decision. Recently, a wealth of studies using transgenic mouse models and selective PRMT inhibitors helped define physiological roles for protein arginine methyltransferases (PRMTs) linking them to diseases such as cancer and metabolic, neurodegenerative, and muscular disorders...
January 5, 2017: Molecular Cell
https://www.readbyqxmd.com/read/28042453/design-and-synthesis-of-selective-small-molecule-inhibitors-of-coactivator-associated-arginine-methyltransferase-1-carm1
#17
H Ü Kaniskan, M S Eram, J Liu, D Smil, M L Martini, Y Shen, V Santhakumar, P J Brown, C Arrowsmith, M Vedadi, J Jin
Coactivator-associated arginine methyltransferase 1 (CARM1) is a type I protein arginine methyltransferase (PRMT) that catalyzes the conversion of arginine into monomethylarginine (MMA) and further into asymmetric dimethylarginine (ADMA). CARM1 methylates histone 3 arginines 17 and 26, as well as numerous non-histone proteins including CBP/p300, SRC-3, NCOA2, PABP1, and SAP49, while also functioning as a coactivator for various proteins that have been linked to cancer such as p53, NF-κβ, β-catenin, E2F1 and steroid hormone receptor ERα...
September 1, 2016: MedChemComm
https://www.readbyqxmd.com/read/27998975/the-major-protein-arginine-methyltransferase-in-trypanosoma-brucei-functions-as-an-enzyme-prozyme-complex
#18
Lucie Kafková, Erik W Debler, John C Fisk, Kanishk Jain, Steven G Clarke, Laurie K Read
Prozymes are catalytically inactive enzyme paralogs that dramatically stimulate the function of weakly active enzymes through complex formation. The two prozymes described to date reside in the polyamine biosynthesis pathway of the human parasite Trypanosoma brucei, an early branching eukaryote that lacks transcriptional regulation and regulates its proteome through posttranscriptional and posttranslational means. Arginine methylation is a common posttranslational modification in eukaryotes catalyzed by protein arginine methyltransferases (PRMTs) that are typically thought to function as homodimers...
February 10, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27994012/asymmetric-arginine-dimethylation-modulates-mitochondrial-energy-metabolism-and-homeostasis-in-caenorhabditis-elegans
#19
Liang Sha, Hiroaki Daitoku, Sho Araoi, Yuta Kaneko, Yuta Takahashi, Koichiro Kako, Akiyoshi Fukamizu
Protein arginine methyltransferase 1 (PRMT-1) catalyzes asymmetric arginine dimethylation on cellular proteins and modulates various aspects of biological processes, such as signal transduction, DNA repair, and transcriptional regulation. We have previously reported that the null mutant of prmt-1 in Caenorhabditis elegans exhibits a slightly shortened life span, but the physiological significance of PRMT-1 remains largely unclear. Here we explored the role of PRMT-1 in mitochondrial function as hinted by a two-dimensional Western blot-based proteomic study...
March 15, 2017: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/27935040/network-based-characterization-of-the-synaptic-proteome-reveals-that-removal-of-epigenetic-regulator-prmt8-restricts-proteins-associated-with-synaptic-maturation
#20
Patrick Kia Ming Lee, Wilson Wen Bin Goh, Judy Chia Ghee Sng
The brain adapts to dynamic environmental conditions by altering its epigenetic state, thereby influencing neuronal transcriptional programs. An example of an epigenetic modification is protein methylation, catalyzed by protein arginine methyltransferases (PRMT). One member, Prmt8, is selectively expressed in the central nervous system during a crucial phase of early development, but little else is known regarding its function. We hypothesize Prmt8 plays a role in synaptic maturation during development. To evaluate this, we used a proteome-wide approach to characterize the synaptic proteome of Prmt8 knockout versus wild-type mice...
February 2017: Journal of Neurochemistry
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