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https://www.readbyqxmd.com/read/28934323/identification-chromosomal-arrangements-and-expression-analyses-of-the-evolutionarily-conserved-prmt1-gene-in-chicken-in-comparison-with-its-vertebrate-paralogue-prmt8
#1
Yi-Chun Wang, Chien-Wen Wang, Wen-Chang Lin, Yun-Jung Tsai, Chien-Ping Chang, Yu-Jen Lee, Min-Jon Lin, Chuan Li
Nine protein arginine methyltransferases (PRMTs) are conserved in mammals and fish. Among these, PRMT1 is the major type I PRMT for asymmetric dimethylarginine (ADMA) formation and is the most conserved and widely distributed one. Two chicken prmt1 splicing variants were assembled and confirmed by RT-PCR experiments. However, only two scaffolds containing single separate prmt1 exon with high GC contents are present in the current chicken genome assembly. Besides, prmt1 exons are scattered in separate small scaffolds in most avian species...
2017: PloS One
https://www.readbyqxmd.com/read/28927791/design-and-synthesis-of-novel-prmt1-inhibitors-and-investigation-of-their-binding-preferences-using-molecular-modelling
#2
Hao Yang, Yifan Ouyang, Hao Ma, Hui Cong, Chunlin Zhuang, Wun-Taai Lok, Zhe Wang, Xuanli Zhu, Yutong Sun, Wei Hong, Hao Wang
Protein arginine methyltransferase 1 (PRMT1) catalyses the methylation of substrate arginine by transferring the methyl group from SAM (S-adenosyl-l-methionine), which leads to the formation of S-adenosyl homocysteine (SAH) and methylated arginine. We have shown previously that the Asp84 on PRMT1 could be a potential inhibitor binding site. In the current study, 28 compounds were designed and synthesized that were predicted to bind the Asp84 and substrate arginine sites together. Among them, 6 compounds were identified as potential PRMT1 inhibitors, and showed strong inhibitory effects on cancer cell lines, especially HepG2...
September 8, 2017: Bioorganic & Medicinal Chemistry Letters
https://www.readbyqxmd.com/read/28883095/lps-modulates-p300-and-sirt1-to-promote-prmt1-stability-via-a-scf-fbxl17-recognized-acetyldegron
#3
Yandong Lai, Jin Li, Xiuying Li, Chunbin Zou
E3 ubiquitin ligase recognizes its protein substrates via specific molecular signatures for ubiquitin proteasomal degradation. However, the role of acetylation/ deacetylation in the process of E3 ubiquitin ligase recognizing its protein substrate is not fully studied. Here we report that a tandem IK motif in protein arginine methyltransferase 1 (PRMT1) forms an acetyldegron to recruit ubiquitin E3 ligase SCF (Skp1-Cullin1-Fbox protein)-Fbxl17. PRMT1 is poly-ubiquitinated for proteasome degradation with a half-life of approximate 4 h in lung epithelial cells...
September 7, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28857308/a-novel-splicing-isoform-of-protein-arginine-methyltransferase-1-prmt1-that-lacks-the-dimerization-arm-and-correlates-with-cellular-malignancy
#4
Odysseas Patounas, Ioanna Papacharalampous, Carmen Eckerich, Georgios S Markopoulos, Evangelos Kolettas, Frank O Fackelmayer
Methylation of arginine residues is an important modulator of protein function that is involved in epigenetic gene regulation, DNA damage response and RNA maturation, as well as in cellular signaling. The enzymes that catalyze this post-translational modification are called protein arginine methyltransferases (PRMTs), of which PRMT1 is the predominant enzyme. Human PRMT1 has previously been shown to occur in seven splicing isoforms, which are differentially abundant in different tissues, and have distinct substrate specificity and intracellular localization...
August 31, 2017: Journal of Cellular Biochemistry
https://www.readbyqxmd.com/read/28801457/correction-for-yu-et-al-a-mouse-prmt1-null-allele-defines-an-essential-role-for-arginine-methylation-in-genome-maintenance-and-cell-proliferation
#5
Zhenbao Yu, Taiping Chen, Josée Hébert, En Li, Stéphane Richard
No abstract text is available yet for this article.
September 1, 2017: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/28768874/pgc1%C3%AE-transcriptional-adaptor-function-governs-hepatitis-b-virus-replication-by-controlling-hbcag-p21-protein-mediated-capsid-formation
#6
Rasha E Shalaby, Saira Iram, Bülent Çakal, Claudia E Oropeza, Alan McLachlan
In the human hepatoma cell line, Huh7, co-expression of the coactivators, peroxisome proliferator-activated receptor gamma coactivator 1α (PGC1α), cAMP responsive element binding protein binding protein (CBP), steroid receptor coactivator 1 (SRC1) and protein arginine methyltransferase 1 (PRMT1) only modestly increase HBV biosynthesis. However, utilizing the human embryonic kidney cell line, HEK293T, it was possible to demonstrate that PGC1α alone can support viral biosynthesis independently of additional coactivator or transcription factor expression...
August 2, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28744817/knockdown-of-prmt1-suppresses-il-1%C3%AE-induced-cartilage-degradation-and-inflammatory-responses-in-human-chondrocytes-through-gli1-mediated-hedgehog-signaling-pathway
#7
Lei Xia, Hong-Xing Zhang, Mei-Li Xing, Yu-Ben Xu, Peng Li, Liang-Ku Huang, Jie Bai, Zhao Tian, Zan-Dong Zhao
Osteoarthritis (OA) is characterized by articular cartilage degradation and joint inflammation. The purpose of the present study is to elucidate the role of the specific function of PRMT1 in chondrocytes and its association with the pathophysiology of OA. We observed that the expression of PRMT1 was apparently upregulated in OA cartilage, as well as in chondrocytes stimulated with IL-1β. Additionally, knockdown of PRMT1 suppressed interleukin 1 beta (IL-1β)-induced extracellular matrix (ECM) metabolic imbalance by regulating the expression of MMP-13, ADAMTS-5, COL2A1, and ACAN...
July 25, 2017: Molecular and Cellular Biochemistry
https://www.readbyqxmd.com/read/28739157/cycloalkane-analogues-of-sinefungin-as-ehmt1-2-inhibitors
#8
Qing Liu, Xiaoqing Cai, Dehua Yang, Yi Chen, Yafang Wang, Liming Shao, Ming-Wei Wang
A series of cycloalkyl substituted analogues of the natural product sinefungin lacking the amino-acid moiety was designed and synthesized. Two stereoisomers (6-R and 6-S) were separated and their bioactivities examined against EHMT1/2. Of which, compound 14d showed an inhibitory activity against EHMT1/2 (88.9%, IC50=21.8μM for EHMT1 and 77.6%, IC50=39.6μM for EHMT2, respectively) similar to that of sinefungin (100.0%, IC50=28.4μM for EHMT1 and 79.5%, IC50=30.1μM for EHMT2, respectively). Further studies against other methyltransferases such as PRMT1 showed no activity except that 12d displayed about 20% inhibition...
June 21, 2017: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/28733251/rna-binding-protein-raly-promotes-protein-arginine-methyltransferase-1-alternatively-spliced-isoform-v2-relative-expression-and-metastatic-potential-in-breast-cancer-cells
#9
Emma Bondy-Chorney, R Mitchell Baldwin, Andréanne Didillon, Benoît Chabot, Bernard J Jasmin, Jocelyn Côté
Aberrant expression of Protein Arginine Methyltransferases (PRMTs) has been observed in several cancer types, including breast cancer. We previously reported that the PRMT1v2 isoform, which is generated through inclusion of alternative exon 2, is overexpressed in breast cancer cells and promotes their invasiveness. However, the precise mechanism by which expression of this isoform is controlled and how it is dysregulated in breast cancer remains unknown. Using a custom RNA interference-based screen, we identified several RNA binding proteins (RBP) which, when knocked down, altered the relative abundance of the alternatively spliced PRMT1v2 isoform...
July 18, 2017: International Journal of Biochemistry & Cell Biology
https://www.readbyqxmd.com/read/28695742/human-regulatory-protein-ki-1-57-is-a-target-of-sumoylation-and-affects-pml-nuclear-body-formation
#10
Ângela Saito, Edmarcia E Souza, Fernanda C Costa, Gabriela V Meirelles, Kaliandra A Gonçalves, Marcos T Santos, Gustavo C Bressan, Mark E McComb, Catherine E Costello, Stephen A Whelan, Jörg Kobarg
Ki-1/57 is a nuclear and cytoplasmic regulatory protein first identified in malignant cells from Hodgkin's lymphoma. It is involved in gene expression regulation on both transcriptional and mRNA metabolism levels. Ki-1/57 belongs to the family of intrinsically unstructured proteins and undergoes phosphorylation by PKC and methylation by PRMT1. Previous characterization of its protein interaction profile by yeast two-hybrid screening showed that Ki-1/57 interacts with proteins of the SUMOylation machinery, the SUMO E2 conjugating enzyme UBC9 and the SUMO E3 ligase PIAS3, which suggested that Ki-1/57 could be involved with this process...
July 31, 2017: Journal of Proteome Research
https://www.readbyqxmd.com/read/28695568/prmt1-regulates-astrocytic-differentiation-of-embryonic-neural-stem-precursor-cells
#11
Mizuki Honda, Kinichi Nakashima, Sayako Katada
Arginine methylation is a posttranslational modification which is catalyzed by protein arginine methyltransferases (PRMTs). Here, we report that PRMT1 is highly expressed in neural stem/precursor cells (NS/PCs) of mouse embryos, and knockdown of PRMT1 in NS/PCs suppresses the generation of astrocytes. The luciferase assay demonstrated that knockdown of PRMT1 inhibits activation of the promoter of a typical astrocytic marker gene, glial fibrillary acidic protein (Gfap), in NS/PCs. The transcription factor signal transducer and activator of transcription 3 (STAT3) is known to generally be critical for astrocytic differentiation of NS/PCs...
July 11, 2017: Journal of Neurochemistry
https://www.readbyqxmd.com/read/28671608/lipotoxicity-induced-prmt1-exacerbates-mesangial-cell-apoptosis-via-endoplasmic-reticulum-stress
#12
Min-Jung Park, Ho Jae Han, Dong-Il Kim
Lipotoxicity-induced mesangial cell apoptosis is implicated in the exacerbation of diabetic nephropathy (DN). Protein arginine methyltransferases (PRMTs) have been known to regulate a variety of biological functions. Recently, it was reported that PRMT1 expression is increased in proximal tubule cells under diabetic conditions. However, their roles in mesangial cells remain unexplored. Thus, we examined the pathophysiological roles of PRMTs in mesangial cell apoptosis. Treatment with palmitate, which mimics cellular lipotoxicity, induced mesangial cell apoptosis via protein kinase RNA-like endoplasmic reticulum kinase (PERK) and ATF6-mediated endoplasmic reticulum (ER) stress signaling...
July 3, 2017: International Journal of Molecular Sciences
https://www.readbyqxmd.com/read/28656289/prmt1-expression-is-elevated-in-head-and-neck-cancer-and-inhibition-of-protein-arginine-methylation-by-adenosine-dialdehyde-or-prmt1-knockdown-downregulates-proliferation-and-migration-of-oral-cancer-cells
#13
Chun-Yi Chuang, Chien-Ping Chang, Yu-Jen Lee, Wei-Long Lin, Wen-Wei Chang, Jia-Sian Wu, Ya-Wen Cheng, Huei Lee, Chuan Li
Protein arginine methylation is a post-translational modification that has been implicated in signal transduction, gene transcription, DNA repair and RNA processing. Overexpression or deregulation of protein arginine methyltransferases (PRMTs) have been reported to be associated with various cancers but have not been studied in head and neck cancer (HNC). We investigated the involvement of the modification in HNC using oral cancer cell lines (SAS, OECM-1 and HSC-3) and an immortalized normal oral cells (S-G)...
June 21, 2017: Oncology Reports
https://www.readbyqxmd.com/read/28655788/prmt1-mediated-translation-regulation-is-a-crucial-vulnerability-of-cancer
#14
Jessie Hao-Ru Hsu, Benjamin Hubbell-Engler, Guillaume Adelmant, Jialiang Huang, Cailin E Joyce, Francisca Vazquez, Barbara A Weir, Philip Montgomery, Aviad Tsherniak, Andrew O Giacomelli, Jennifer A Perry, Jennifer Trowbridge, Yuko Fujiwara, Glenn S Cowley, Huafeng Xie, Woojin Kim, Carl D Novina, William C Hahn, Jarrod A Marto, Stuart H Orkin
Through an shRNA screen, we identified the protein arginine methyltransferase Prmt1 as a vulnerable intervention point in murine p53/Rb-null osteosarcomas, the human counterpart of which lacks effective therapeutic options. Depletion of Prmt1 in p53-deficient cells impaired tumor initiation and maintenance in vitro and in vivo Mechanistic studies reveal that translation-associated pathways were enriched for Prmt1 downstream targets, implicating Prmt1 in translation control. In particular, loss of Prmt1 led to a decrease in arginine methylation of the translation initiation complex, thereby disrupting its assembly and inhibiting translation...
September 1, 2017: Cancer Research
https://www.readbyqxmd.com/read/28652407/arginine-methylation-regulates-c-myc-dependent-transcription-by-altering-promoter-recruitment-of-the-acetyltransferase-p300
#15
Irina Tikhanovich, Jie Zhao, Brian Bridges, Sean Kumer, Ben Roberts, Steven A Weinman
Protein arginine methyltransferase 1 (PRMT1) is an essential enzyme controlling about 85% of the total cellular arginine methylation in proteins. We have shown previously that PRMT1 is an important regulator of innate immune responses and that it is required for M2 macrophage differentiation. c-Myc is a transcription factor that is critical in regulating cell proliferation and also regulates the M2 transcriptional program in macrophages. Here, we sought to determine whether c-Myc in myeloid cells is regulated by PRMT1-dependent arginine methylation...
August 11, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28649316/discovery-of-decamidine-as-a-new-and-potent-prmt1-inhibitor
#16
Jing Zhang, Kun Qian, Chunli Yan, Maomao He, Brenson A Jassim, Ivaylo Ivanov, Yujun George Zheng
Protein arginine methyltransferase 1 (PRMT1) is a key player for the dynamic regulation of arginine methylation. Its dysregulation and aberrant expression are implicated in various pathological conditions, and a plethora of evidence suggests that PRMT1 inhibition is of significant therapeutic value. Herein, we reported the modification of a series of diamidine compounds with varied lengths in the middle alkyl linker for PRMT1 inhibition. Decamidine (2j), which possesses the longest linker in the series, displayed 2- and 4- fold increase in PRMT1 inhibition (IC50 = 13 μM), as compared with furamdine and stilbamidine...
February 1, 2017: MedChemComm
https://www.readbyqxmd.com/read/28644004/intricate-effects-of-%C3%AE-amino-and-lysine-modifications-on-arginine-methylation-of-the-n-terminal-tail-of-histone-h4
#17
Melody D Fulton, Jing Zhang, Maomao He, Meng-Chiao Ho, Y George Zheng
Chemical modifications of the DNA and nucleosomal histones tightly control the gene transcription program in eukaryotic cells. The "histone code" hypothesis proposes that the frequency, combination, and location of post-translational modifications (PTMs) of the core histones compose a complex network of epigenetic regulation. Currently, there are at least 23 different types and >450 histone PTMs that have been discovered, and the PTMs of lysine and arginine residues account for a crucial part of the histone code...
July 18, 2017: Biochemistry
https://www.readbyqxmd.com/read/28643125/the-role-of-prmt1-in-egfr-methylation-and-signaling-in-mda-mb-468-triple-negative-breast-cancer-cells
#18
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/28636189/discovery-of-alkyl-bis-oxy-dibenzimidamide-derivatives-as-novel-protein-arginine-methyltransferase-1-prmt1-inhibitors
#19
Wei-Yao Zhang, Wen-Chao Lu, Hao Jiang, Zheng-Bing Lv, Yi-Qian Xie, Fu-Lin Lian, Zhong-Jie Liang, Yu-Xi Jiang, Da-Jin Wang, Cheng Luo, Jia Jin, Fei Ye
Protein arginine methylation, a post-translational modification critical for a variety of biological processes, is catalyzed by protein arginine N-methyltransferases (PRMTs). In particular, PRMT1 is responsible for over 85% of the arginine methylation in mammalian cells. Dysregulation of PRMT1 is involved in diverse pathological diseases including cancers. However, most current PRMT1inhibitors are lack of specificity, efficacy, and bioavailability. Herein, a series of alkyl bis(oxy)dibenzimidamide derivatives were identified as selective PRMT1 inhibitors...
June 21, 2017: Chemical Biology & Drug Design
https://www.readbyqxmd.com/read/28628091/the-btg2-prmt1-module-limits-pre-b-cell-expansion-by-regulating-the-cdk4-cyclin-d3-complex
#20
Elmar Dolezal, Simona Infantino, Friedel Drepper, Theresa Börsig, Aparajita Singh, Thomas Wossning, Gina J Fiala, Susana Minguet, Bettina Warscheid, David M Tarlinton, Hassan Jumaa, David Medgyesi, Michael Reth
Developing pre-B cells in the bone marrow alternate between proliferation and differentiation phases. We found that protein arginine methyl transferase 1 (PRMT1) and B cell translocation gene 2 (BTG2) are critical components of the pre-B cell differentiation program. The BTG2-PRMT1 module induced a cell-cycle arrest of pre-B cells that was accompanied by re-expression of Rag1 and Rag2 and the onset of immunoglobulin light chain gene rearrangements. We found that PRMT1 methylated cyclin-dependent kinase 4 (CDK4), thereby preventing the formation of a CDK4-Cyclin-D3 complex and cell cycle progression...
August 2017: Nature Immunology
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