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PRMT5

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https://www.readbyqxmd.com/read/29262329/prmt5-is-a-critical-regulator-of-breast-cancer-stem-cell-function-via-histone-methylation-and-foxp1-expression
#1
Kelly Chiang, Agnieszka E Zielinska, Abeer M Shaaban, Maria Pilar Sanchez-Bailon, James Jarrold, Thomas L Clarke, Jingxian Zhang, Adele Francis, Louise J Jones, Sally Smith, Olena Barbash, Ernesto Guccione, Gillian Farnie, Matthew J Smalley, Clare C Davies
Breast cancer progression, treatment resistance, and relapse are thought to originate from a small population of tumor cells, breast cancer stem cells (BCSCs). Identification of factors critical for BCSC function is therefore vital for the development of therapies. Here, we identify the arginine methyltransferase PRMT5 as a key in vitro and in vivo regulator of BCSC proliferation and self-renewal and establish FOXP1, a winged helix/forkhead transcription factor, as a critical effector of PRMT5-induced BCSC function...
December 19, 2017: Cell Reports
https://www.readbyqxmd.com/read/29250158/function-of-mir-25-in-the-invasion-and-metastasis-of-esophageal-squamous-carcinoma-cells-and-bioinformatical-analysis-of-the-mir-106b-25-cluster
#2
Meng Wang, Yangyang Ou Yang, Qingtao Jin, Linlin Shang, Jian Zhang
MicroRNAs (miRNAs/miRs) are a class of small, non-coding RNA molecules that serve a key function in carcinogenesis and tumor progression. Recent evidence indicates that miRNAs may act as powerful regulators of migration and invasion. The present study aimed to investigate the effect of miR-25 on the invasion and metastasis of KYSE-150 and EC109 esophageal squamous cell carcinoma (ESCC) cells, and predict the mechanism of this effect by bioinformatically analyzing the miR-106b-25 cluster. In order to alter the expression of miR-25 in the two cell lines, a miR-25 inhibitor or mimic were transfected into the cells, which were then studied via Transwell migration and invasion assays...
January 2018: Experimental and Therapeutic Medicine
https://www.readbyqxmd.com/read/29227283/sharpin-mediated-regulation-of-protein-arginine-methyltransferase-5-controls-melanoma-growth
#3
Hironari Tamiya, Hyungsoo Kim, Oleksiy Klymenko, Heejung Kim, Yongmei Feng, Tongwu Zhang, Ji Yun Han, Ayako Murao, Scott J Snipas, Lucia Jilaveanu, Kevin Brown, Harriet Kluger, Hao Zhang, Kazuhiro Iwai, Ze'ev A Ronai
SHARPIN, an adaptor for the linear ubiquitin chain assembly complex (LUBAC), plays important roles in NF-κB signaling and inflammation. Here, we have demonstrated a LUBAC-independent role for SHARPIN in regulating melanoma growth. We observed that SHARPIN interacted with PRMT5, a type II protein arginine methyltransferase, and increased its multiprotein complex and methyltransferase activity. Activated PRMT5 controlled the expression of the transcription factors SOX10 and MITF by SHARPIN-dependent arginine dimethylation and inhibition of the transcriptional corepressor SKI...
December 11, 2017: Journal of Clinical Investigation
https://www.readbyqxmd.com/read/29185119/prmt5-determines-the-sensitivity-to-chemotherapeutics-by-governing-stemness-in-breast-cancer
#4
Zhe Wang, Jing Kong, Ying Wu, Juliang Zhang, Ting Wang, Nanlin Li, Jing Fan, Hui Wang, Jian Zhang, Rui Ling
PURPOSE: Acquired resistance to chemotherapeutic agents in breast cancer is a major clinical challenge. Recent studies have shown that the emergence of cancer stem cells contributes to the development of drug resistance, and the protein arginine methyltransferase 5 (PRMT5) was crucial for the maintenance of stemness. However, the roles of PRMT5 in breast cancer cell stemness and the development of cancer drug resistance have not been clarified. In this study, we investigated the effect of PRMT5 on the sensitivity to doxorubicin and cell stemness in breast cancer...
November 28, 2017: Breast Cancer Research and Treatment
https://www.readbyqxmd.com/read/29158558/protein-arginine-methyltransferase-5-prmt5-has-prognostic-relevance-and-is-a-druggable-target-in-multiple-myeloma
#5
A Gullà, T Hideshima, G Bianchi, M Fulciniti, M K Samur, J Qi, Y-T Tai, T Harada, E Morelli, N Amodio, R Carrasco, P Tagliaferri, N C Munshi, P Tassone, K C Anderson
Arginine methyltransferases critically regulate cellular homeostasis by modulating the functional outcome of their substrates. The protein arginine methyltransferase 5 (PRMT5) is an enzyme involved in growth and survival pathways promoting tumorigenesis. However, little is known about the biologic function of PRMT5 and its therapeutic potential in multiple myeloma (MM). In the present study, we identified and validated PRMT5 as a new therapeutic target in MM. PRMT5 is overexpressed in patient MM cells and associated with decreased PFS and OS...
November 21, 2017: Leukemia: Official Journal of the Leukemia Society of America, Leukemia Research Fund, U.K
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
#6
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/29106602/prmt5-as-a-druggable-target-for-glioblastoma-therapy
#7
Yeshavanth Kumar Banasavadi-Siddegowda, Alessandra M Welker, Min An, Xiaozhi Yang, Wei Zhou, Guqin Shi, Jaime Imitola, Chenglong Li, Sigmund Hsu, Jiang Wang, Mitch Phelps, Jianying Zhang, Christine E Beattie, Robert Baiocchi, Balveen Kaur
Background: In spite of standard multi modal therapy consisting of surgical resection followed by radiation and concurrent chemotherapy prognosis for GBM patients remains poor. The identification of both differentiated and undifferentiated "stem cell like" populations in the tumor highlights the significance of finding novel targets that affect the heterogenous tumor cell population. Protein arginine methyltransferase (PRMT5) is one such candidate gene whose nuclear expression correlates with poor survival and has been reported to be required for survival of differentiated GBM cells and self-renewal of undifferentiated GBM cells...
November 2, 2017: Neuro-oncology
https://www.readbyqxmd.com/read/29099132/development-of-an-alphalisa-high-throughput-technique-to-screen-for-small-molecule-inhibitors-targeting-protein-arginine-methyltransferases
#8
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/29092819/protein-arginine-methyltransferase-expression-localization-and-activity-during-disuse-induced-skeletal-muscle-plasticity
#9
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/29076773/targeting-protein-arginine-methyltransferase-5-in-disease
#10
André Richters
PRMT5 catalyzes the mono- and symmetric dimethylation of the arginine N-guanidine group of a wide variety of target proteins including histones, transcriptional elongation factors, kinases and tumor suppressors by utilizing the essential co-factor S-adenosylmethionine as methyl source. PRMT5 overexpression has been linked to the progression of various diseases, including cancer, and is oftentimes associated with a poor prognosis. Therefore, PRMT5 is promoted as a valuable target for drug discovery approaches and was a subject matter in recent endeavors aiming for the development of specific PRMT5 inhibitors...
October 27, 2017: Future Medicinal Chemistry
https://www.readbyqxmd.com/read/29065155/prmt5-a-novel-regulator-of-hepatitis-b-virus-replication-and-an-arginine-methylase-of-hbv-core
#11
Barbora Lubyova, Jan Hodek, Ales Zabransky, Hana Prouzova, Martin Hubalek, Ivan Hirsch, Jan Weber
In mammals, protein arginine methyltransferase 5, PRMT5, is the main type II enzyme responsible for the majority of symmetric dimethylarginine formation in polypeptides. Recent study reported that PRMT5 restricts Hepatitis B virus (HBV) replication through epigenetic repression of HBV DNA transcription and interference with encapsidation of pregenomic RNA. Here we demonstrate that PRMT5 interacts with the HBV core (HBc) protein and dimethylates arginine residues within the arginine-rich domain (ARD) of the carboxyl-terminus...
2017: PloS One
https://www.readbyqxmd.com/read/29054638/the-persistent-organochlorine-pesticide-endosulfan-modulates-multiple-epigenetic-regulators-with-oncogenic-potential-in-mcf-7-cells
#12
Krishna Ghosh, Biji Chatterjee, Aparna Geetha Jayaprasad, Santosh R Kanade
Environmental cues and chemicals can potentially modulate the phenotypic expression of genome through alterations in the epigenetic mechanisms. Endosulfan is one of the extensively used organochlorine pesticides around the world which is known for its endocrine, neuro- and reproductive toxicity. This study was aimed to investigate the potential of α-endosulfan in modulation of multiple epigenetic enzymes in MCF-7 cells. The cells were treated with DMSO (control) or α-endosulfan (1 and 10μM) and the expression of various epigenetic enzymes was assayed by real-time PCR and immunoblotting, in addition to their activity assays...
October 17, 2017: Science of the Total Environment
https://www.readbyqxmd.com/read/29050343/an-integrated-multigene-expression-panel-to-predict-long-term-survival-after-curative-hepatectomy-in-patients-with-hepatocellular-carcinoma
#13
Mitsuro Kanda, Kenta Murotani, Hiroyuki Sugimoto, Takashi Miwa, Shinichi Umeda, Masaya Suenaga, Masamichi Hayashi, Norifumi Hattori, Chie Tanaka, Daisuke Kobayashi, Suguru Yamada, Michitaka Fujiwara, Yasuhiro Kodera
Hepatocellular carcinoma (HCC) frequently recurs even after curative hepatectomy. To develop an integrated multigene expression panel, 144 patients were randomly assigned to either discovery or validation set in a 1:2 ratio. Using surgically resected HCC specimens, expression levels of 12 candidate molecular markers were determined using quantitative reverse-transcriptase PCR. In the discovery set, an expression panel was developed according to the concordance index (C-index) values for overall survival from all 4095 combinations of the 12 candidate molecular markers...
September 19, 2017: Oncotarget
https://www.readbyqxmd.com/read/29018151/correction-prmt5-selective-inhibitors-suppress-inflammatory-t-cell-responses-and-experimental-autoimmune-encephalomyelitis
#14
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
No abstract text is available yet for this article.
October 15, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
https://www.readbyqxmd.com/read/29017049/exploiting-the-hidden-treasure-of-detained-introns
#15
Xiang-Dong Fu
Many mammalian genes contain poorly spliced introns, resulting in nuclear detention of partially spliced transcripts, which may be exploited to modulate gene expression. In this issue of Cancer Cell, Braun et al. report that the arginine methyltransferase PRMT5 is critical for tumor cell proliferation by regulating numerous detained introns.
October 9, 2017: Cancer Cell
https://www.readbyqxmd.com/read/28987382/arginine-methyltransferase-inhibitor-1-inhibits-gastric-cancer-by-downregulating-eif4e-and-targeting-prmt5
#16
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/28986365/the-splicing-regulator-prmt5-is-critical-for-glioblastoma-proliferation
#17
(no author information available yet)
PRMT5 regulates the splicing of detained introns in proliferation-associated genes in GBM.
October 6, 2017: Cancer Discovery
https://www.readbyqxmd.com/read/28977470/the-prmt5-wdr77-complex-regulates-alternative-splicing-through-znf326-in-breast-cancer
#18
Madhumitha Rengasamy, Fan Zhang, Ajay Vashisht, Won-Min Song, Francesca Aguilo, Yifei Sun, SiDe Li, Weijia Zhang, Bin Zhang, James A Wohlschlegel, Martin J Walsh
We observed overexpression and increased intra-nuclear accumulation of the PRMT5/WDR77 in breast cancer cell lines relative to immortalized breast epithelial cells. Utilizing mass spectrometry and biochemistry approaches we identified the Zn-finger protein ZNF326, as a novel interaction partner and substrate of the nuclear PRMT5/WDR77 complex. ZNF326 is symmetrically dimethylated at arginine 175 (R175) and this modification is lost in a PRMT5 and WDR77-dependent manner. Loss of PRMT5 or WDR77 in MDA-MB-231 cells leads to defects in alternative splicing, including inclusion of A-T rich exons in target genes, a phenomenon that has previously been observed upon loss of ZNF326...
August 21, 2017: Nucleic Acids Research
https://www.readbyqxmd.com/read/28972166/histone-arginine-demethylase-jmjd6-is-linked-to-stress-granule-assembly-through-demethylation-of-the-stress-granule-nucleating-protein-g3bp1
#19
Wei-Chih Tsai, Lucas C Reineke, Antrix Jain, Sung Yun Jung, Richard E Lloyd
Stress granules (SG) are membrane-less organelles that are condensates of stalled translation initiation complexes and mRNAs. SG formation is a cytoprotective response to environmental stress and results from protein interactions involving regions of low amino acid complexity and poorly defined post-translational modifications of SG components. Many RNA binding proteins are methylated and we previously demonstrated that the potent SG nucleating protein G3BP1 is methylated by protein arginine methyltransferase 1 and 5 (PRMT1 and PRMT5)...
September 27, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28966034/coordinated-splicing-of-regulatory-detained-introns-within-oncogenic-transcripts-creates-an-exploitable-vulnerability-in-malignant-glioma
#20
Christian J Braun, Monica Stanciu, Paul L Boutz, Jesse C Patterson, David Calligaris, Fumi Higuchi, Rachit Neupane, Silvia Fenoglio, Daniel P Cahill, Hiroaki Wakimoto, Nathalie Y R Agar, Michael B Yaffe, Phillip A Sharp, Michael T Hemann, Jacqueline A Lees
Glioblastoma (GBM) is a devastating malignancy with few therapeutic options. We identify PRMT5 in an in vivo GBM shRNA screen and show that PRMT5 knockdown or inhibition potently suppresses in vivo GBM tumors, including patient-derived xenografts. Pathway analysis implicates splicing in cellular PRMT5 dependency, and we identify a biomarker that predicts sensitivity to PRMT5 inhibition. We find that PRMT5 deficiency primarily disrupts the removal of detained introns (DIs). This impaired DI splicing affects proliferation genes, whose downregulation coincides with cell cycle defects, senescence and/or apoptosis...
October 9, 2017: Cancer Cell
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