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https://www.readbyqxmd.com/read/27876471/cobalamin-and-folate-protect-mitochondrial-and-contractile-functions-in-a-murine-model-of-cardiac-pressure-overload
#1
Jérôme Piquereau, Maryline Moulin, Giada Zurlo, Philippe Mateo, Mélanie Gressette, Jean-Louis Paul, Christophe Lemaire, Renée Ventura-Clapier, Vladimir Veksler, Anne Garnier
PGC-1α, a key regulator of energy metabolism, seems to be a relevant therapeutic target to rectify the energy deficit observed in heart failure (HF). Since our previous work has shown positive effects of cobalamin (Cb) on PGC-1α cascade, we investigate the protective role of Cb in pressure overload-induced myocardial dysfunction. Mice were fed with normal diet (ND) or with Cb and folate supplemented diet (SD) 3weeks before and 4weeks after transverse aortic constriction (TAC). At the end, left ventricle hypertrophy and drop of ejection fraction were significantly lower in SD mice than in ND mice...
November 19, 2016: Journal of Molecular and Cellular Cardiology
https://www.readbyqxmd.com/read/27849571/arginine-methylation-by-prmt1-regulates-muscle-stem-cell-fate
#2
Roméo Sébastien Blanc, Gillian Vogel, Xing Li, Zhenbao Yu, Shawn Li, Stéphane Richard
Quiescent muscle stem cells (MSC) become activated in response to skeletal muscle injury to initiate regeneration. Activated MSCs proliferate and differentiate to repair damaged fibers or self-renew to maintain the pool and insure future regeneration. The balance between self-renewal, proliferation and differentiation is a tightly regulated process controlled by a genetic cascade involving determinant transcription factors such as Pax7, Myf5, MyoD, and MyoG. Recently there have been several reports about the role of arginine methylation as a requirement for epigenetic-mediated control of muscle regeneration...
November 14, 2016: Molecular and Cellular Biology
https://www.readbyqxmd.com/read/27834681/transient-kinetics-define-a-complete-kinetic-model-for-protein-arginine-methyltransferase-1
#3
Hao Hu, Cheng Luo, Y George Zheng
Protein arginine methyltransferases (PRMTs) are the enzymes responsible for posttranslational methylation of protein arginine residues in eukaryotic cells, particularly within the histone tails. A detailed mechanistic model of PRMT-catalyzed methylation is currently lacking, but is essential for understanding functions of PRMTs in various cellular pathways and for efficient design of PRMT inhibitors as potential treatments for a range of human diseases. In this work, we used stopped-flow fluorescence in combination with global kinetic simulation to dissect the transient kinetics of PRMT1, the predominant type-I arginine methyltransferase...
November 10, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27793800/gene-expression-profiling-of-epigenetic-chromatin-modification-enzymes-and-histone-marks-by-cigarette-smoke-implications-for-copd-and-lung-cancer
#4
Isaac Kirubakaran Sundar, Irfan Rahman
Chromatin modifying enzymes mediate DNA methylation and histone modifications upon recruitment to specific target gene loci in response to various stimuli. The key enzymes that regulate chromatin accessibility for maintenance of modifications in DNA and histones, and for modulation of gene expression patterns in response to cigarette smoke (CS), are not known. We hypothesize that CS exposure alters the gene expression patterns of chromatin modifying enzymes, which then affects multiple downstream pathways involved in the response to CS...
October 28, 2016: American Journal of Physiology. Lung Cellular and Molecular Physiology
https://www.readbyqxmd.com/read/27758883/oncogenic-functions-of-gli1-in-pancreatic-adenocarcinoma-are-supported-by-its-prmt1-mediated-methylation
#5
Yan Wang, Jung-Mao Hsu, Ya'an Kang, Yongkun Wei, Pei-Chih Lee, Shing-Jyh Chang, Yi-Hsin Hsu, Jennifer L Hsu, Hung-Ling Wang, Wei-Chao Chang, Chia-Wei Li, Hsin-Wei Liao, Shih-Shin Chang, Weiya Xia, How-Wen Ko, Chao-Kai Chou, Jason B Fleming, Huamin Wang, Rosa F Hwang, Yue Chen, Jun Qin, Mien-Chie Hung
The oncogenic transcription factor Gli1 is a critical effector in the Hedgehog (Hh) pathway, which is necessary for the development and progression of pancreatic ductal adenocarcinoma (PDAC). Although TGFβ and K-Ras are known regulators of Gli1 gene transcription in this setting, it is not understood how Gli1 functional activity is regulated. Here, we report the identification of Gli1 as a substrate for the protein arginine N-methyltransferase PRMT1 in PDAC. We found that PRMT1 methylates Gli1 at R597, promoting its transcriptional activity by enhancing the binding of Gli1 to its target gene promoters...
December 1, 2016: Cancer Research
https://www.readbyqxmd.com/read/27683223/chtop-chromatin-target-of-prmt1-auto-regulates-its-expression-level-via-intron-retention-and-nonsense-mediated-decay-of-its-own-mrna
#6
Keiichi Izumikawa, Harunori Yoshikawa, Hideaki Ishikawa, Yuko Nobe, Yoshio Yamauchi, Sjaak Philipsen, Richard J Simpson, Toshiaki Isobe, Nobuhiro Takahashi
Chtop (chromatin target of Prmt1) regulates various aspects of gene expression including transcription and mRNA export. Despite these important functions, the regulatory mechanism underlying Chtop expression remains undetermined. Using Chtop-expressing human cell lines, we demonstrate that Chtop expression is controlled via an autoregulatory negative feedback loop whereby Chtop binds its own mRNA to retain intron 2 during splicing; a premature termination codon present at the 5' end of intron 2 leads to nonsense-mediated decay of the mRNA...
November 16, 2016: Nucleic Acids Research
https://www.readbyqxmd.com/read/27642082/prmt1-mediated-methylation-of-micu1-determines-the-ucp2-3-dependency-of-mitochondrial-ca-2-uptake-in-immortalized-cells
#7
Corina T Madreiter-Sokolowski, Christiane Klec, Warisara Parichatikanond, Sarah Stryeck, Benjamin Gottschalk, Sergio Pulido, Rene Rost, Emrah Eroglu, Nicole A Hofmann, Alexander I Bondarenko, Tobias Madl, Markus Waldeck-Weiermair, Roland Malli, Wolfgang F Graier
Recent studies revealed that mitochondrial Ca(2+) channels, which control energy flow, cell signalling and death, are macromolecular complexes that basically consist of the pore-forming mitochondrial Ca(2+) uniporter (MCU) protein, the essential MCU regulator (EMRE), and the mitochondrial Ca(2+) uptake 1 (MICU1). MICU1 is a regulatory subunit that shields mitochondria from Ca(2+) overload. Before the identification of these core elements, the novel uncoupling proteins 2 and 3 (UCP2/3) have been shown to be fundamental for mitochondrial Ca(2+) uptake...
September 19, 2016: Nature Communications
https://www.readbyqxmd.com/read/27577262/proteome-wide-analysis-of-arginine-monomethylation-reveals-widespread-occurrence-in-human-cells
#8
Sara C Larsen, Kathrine B Sylvestersen, Andreas Mund, David Lyon, Meeli Mullari, Maria V Madsen, Jeremy A Daniel, Lars J Jensen, Michael L Nielsen
The posttranslational modification of proteins by arginine methylation is functionally important, yet the breadth of this modification is not well characterized. Using high-resolution mass spectrometry, we identified 8030 arginine methylation sites within 3300 human proteins in human embryonic kidney 293 cells, indicating that the occurrence of this modification is comparable to phosphorylation and ubiquitylation. A site-level conservation analysis revealed that arginine methylation sites are less evolutionarily conserved compared to arginines that were not identified as modified by methylation...
2016: Science Signaling
https://www.readbyqxmd.com/read/27571165/protein-arginine-methyltransferase-1-is-a-novel-regulator-of-mycn-in-neuroblastoma
#9
Allison Eberhardt, Jeanne N Hansen, Jan Koster, Louis T Lotta, Simeng Wang, Emmett Livingstone, Kun Qian, Linda J Valentijn, Yujun George Zheng, Nina F Schor, Xingguo Li
Amplification or overexpression of MYCN is associated with poor prognosis of human neuroblastoma. We have recently defined a MYCN-dependent transcriptional signature, including protein arginine methyltransferase 1 (PRMT1), which identifies a subgroup of patients with high-risk disease. Here we provide several lines of evidence demonstrating PRMT1 as a novel regulator of MYCN and implicating PRMT1 as a potential therapeutic target in neuroblastoma pathogenesis. First, we observed a strong correlation between MYCN and PRMT1 protein levels in primary neuroblastoma tumors...
August 23, 2016: Oncotarget
https://www.readbyqxmd.com/read/27545444/understanding-protein-arginine-methyltransferase-1-prmt1-product-specificity-from-molecular-dynamics
#10
Symon Gathiaka, Brittany Boykin, Tamar Cáceres, Joan M Hevel, Orlando Acevedo
Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of specific arginyl groups within targeted proteins to regulate fundamental biological responses in eukaryotic cells. The major Type I PRMT enzyme, PRMT1, strictly generates monomethyl arginine (MMA) and asymmetric dimethylarginine (ADMA), but not symmetric dimethylarginine (SDMA). Multiple diseases can arise from the dysregulation of PRMT1, including heart disease and cancer, which underscores the need to elucidate the origin of product specificity...
October 15, 2016: Bioorganic & Medicinal Chemistry
https://www.readbyqxmd.com/read/27521225/lactate-induced-hif-1%C3%AE-prmt1-cross-talk-affects-mhc-i-expression-in-monocytes
#11
Piyushi Gupta, Ankita Singh, Pruthvi Gowda, Sadashib Ghosh, Arpita Chatterjee, Ellora Sen
Tumor infiltrating monocytes play a crucial role in tumor immune surveillance. As lactate is an important component of the tumor milieu, we investigated its role in the transcriptional regulation of MHC I which is crucial for mounting effective immune responses against tumors. Lactate elevated MHC class I expression in monocytes. Increase in HLAB expression was concomitant with increase in HIF-1α and decrease in PRMT1 levels. Interestingly, a reciprocal relationship was observed between PRMT1 and HIF-1α. While HIF-1α inhibition decreased lactate induced MHC I, both pharmacological inhibition and siRNA mediated knockdown of PRMT1 upregulated HLAB levels...
October 1, 2016: Experimental Cell Research
https://www.readbyqxmd.com/read/27520967/arginine-methylation-enhances-the-rna-chaperone-activity-of-the-west-nile-virus-host-factor-auf1-p45
#12
Susann Friedrich, Tobias Schmidt, Angelika Schierhorn, Hauke Lilie, Grit Szczepankiewicz, Sandra Bergs, Uwe G Liebert, Ralph P Golbik, Sven-Erik Behrens
A prerequisite for the intracellular replication process of the Flavivirus West Nile virus (WNV) is the cyclization of the viral RNA genome, which enables the viral replicase to initiate RNA synthesis. Our earlier studies indicated that the p45 isoform of the cellular AU-rich element binding protein 1 (AUF1) has an RNA chaperone activity, which supports RNA cyclization and viral RNA synthesis by destabilizing a stem structure at the WNV RNA's 3'-end. Here we show that in mammalian cells, AUF1 p45 is consistently modified by arginine methylation of its C terminus...
October 2016: RNA
https://www.readbyqxmd.com/read/27466704/protein-arginine-methylation-facilitates-kcnq-channel-pip2-interaction-leading-to-seizure-suppression
#13
Hyun-Ji Kim, Myong-Ho Jeong, Kyung-Ran Kim, Chang-Yun Jung, Seul-Yi Lee, Hanna Kim, Jewoo Koh, Tuan Anh Vuong, Seungmoon Jung, Hyunwoo Yang, Su-Kyung Park, Dahee Choi, Sung Hun Kim, KyeongJin Kang, Jong-Woo Sohn, Joo Min Park, Daejong Jeon, Seung-Hoi Koo, Won-Kyung Ho, Jong-Sun Kang, Seong-Tae Kim, Hana Cho
KCNQ channels are critical determinants of neuronal excitability, thus emerging as a novel target of anti-epileptic drugs. To date, the mechanisms of KCNQ channel modulation have been mostly characterized to be inhibitory via Gq-coupled receptors, Ca(2+)/CaM, and protein kinase C. Here we demonstrate that methylation of KCNQ by protein arginine methyltransferase 1 (Prmt1) positively regulates KCNQ channel activity, thereby preventing neuronal hyperexcitability. Prmt1+/- mice exhibit epileptic seizures. Methylation of KCNQ2 channels at 4 arginine residues by Prmt1 enhances PIP2 binding, and Prmt1 depletion lowers PIP2 affinity of KCNQ2 channels and thereby the channel activities...
July 28, 2016: ELife
https://www.readbyqxmd.com/read/27338245/using-oriented-peptide-array-libraries-to-evaluate-methylarginine-specific-antibodies-and-arginine-methyltransferase-substrate-motifs
#14
Sitaram Gayatri, Martis W Cowles, Vidyasiri Vemulapalli, Donghang Cheng, Zu-Wen Sun, Mark T Bedford
Signal transduction in response to stimuli relies on the generation of cascades of posttranslational modifications that promote protein-protein interactions and facilitate the assembly of distinct signaling complexes. Arginine methylation is one such modification, which is catalyzed by a family of nine protein arginine methyltransferases, or PRMTs. Elucidating the substrate specificity of each PRMT will promote a better understanding of which signaling networks these enzymes contribute to. Although many PRMT substrates have been identified, and their methylation sites mapped, the optimal target motif for each of the nine PRMTs has not been systematically addressed...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27183873/methylation-of-arginine-by-prmt1-regulates-nrf2-transcriptional-activity-during-the-antioxidative-response
#15
Xin Liu, Hongyuan Li, Lingxia Liu, Yang Lu, Yanyan Gao, Pengyu Geng, Xiaoxue Li, Baiqu Huang, Yu Zhang, Jun Lu
The cap 'n' collar (CNC) family of transcription factors play important roles in resistance of oxidative and electrophilic stresses. Among the CNC family members, NF-E2-related factor 2 (Nrf2) is critical for regulating the antioxidant and phase II enzymes through antioxidant response element (ARE)-mediated transactivation. The activity of Nrf2 is controlled by a variety of post-translational modifications, including phosphorylation, ubiquitination, acetylation and sumoylation. Here we demonstrate that the arginine methyltransferase-1 (PRMT1) methylates Nrf2 protein at a single residue of arginine 437, both in vitro and in vivo...
August 2016: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/27175582/prmt1-regulates-tumor-growth-and-metastasis-of-human-melanoma-via-targeting-alcam
#16
Lei Li, Zhengwen Zhang, Tengxiao Ma, Ran Huo
Overexpression of protein arginine methyltransferases (PRMTs) is associated with various types of cancer. The present study aimed to determine the expression level of PRMT1 in human melanoma and investigate its biological function. The clinical significance of PRMT1 was determined by screening the Oncomine database, and the increased expression of PRMT in melanoma was confirmed by western blot analysis. Furthermore, the current study demonstrated that PRMT1 was overexpressed in melanoma cell lines compared with human immortalized keratinocytes and PIG1 immortalized human melanocytes...
July 2016: Molecular Medicine Reports
https://www.readbyqxmd.com/read/27080477/epigallocatechin-3-gallate-ameliorates-erectile-function-in-aged-rats-via-regulation-of-prmt1-ddah-adma-nos-metabolism-pathway
#17
Dong Chen, Ke-Qin Zhang, Bo Li, Ding-Qi Sun, Hui Zhang, Qiang Fu
Aging-related ED is predominantly attributed to neurovascular dysfunction mediated by NO suppression and increased oxidative stress in penis. The alterations of protein arginine methyltransferases 1 (PRMT1)/dimethylarginine dimethylaminohydrolase (DDAH)/asymmetrical dimethylarginine (ADMA)/NO synthase (NOS) pathway regulate NO production in the vascular endothelium. Epigallocatechin-3-gallate (EGCG) is one of the most abundant and antioxidative ingredients isolated from green tea. In the present study, 40 Sprague-Dawley rats were randomly distributed into four groups: one young rat group and three aged rat groups treated with daily gavage feedings of EGCG at doses of 0, 10 mg kg-1 and 100 mg kg-1 for 12 weeks, respectively...
April 15, 2016: Asian Journal of Andrology
https://www.readbyqxmd.com/read/27069327/identification-of-differential-protein-expression-in-hepatocellular-carcinoma-induced-wistar-albino-rats-by-2d-electrophoresis-and-maldi-tof-ms-analysis
#18
Vadanasundari Vedarethinam, Karthik Dhanaraj, Ilavenil Soundherrajan, Ravikumar Sivanesan
Hepato cellular carcinoma (HCC) is a type of malignant tumor. To investigate the proteins in cancer molecular mechanism and its role in HCC, we have used proteomic tools such as 2DE and MALDI-TOF-MS. Our investigation ravels that, plasma α-fetoprotein and carcinoembryonic antigen levels were elevated in DEN induced rats and gradually decreased after the treatment with 1,3BPMU. 2DE and MALDI-TOF-MS tool offers to identify the up and down regulation of proteins in HCC. Proteomic study reveals that, five differentially expressed proteins were identified in DEN induced rats and 1,3BPMU treated rats i...
April 2016: Indian Journal of Clinical Biochemistry: IJCB
https://www.readbyqxmd.com/read/27051065/asymmetric-arginine-dimethylation-of-rela-provides-a-repressive-mark-to-modulate-tnf%C3%AE-nf-%C3%AE%C2%BAb-response
#19
Anja Reintjes, Julian E Fuchs, Leopold Kremser, Herbert H Lindner, Klaus R Liedl, Lukas A Huber, Taras Valovka
Nuclear factor kappa B (NF-κB) is an inducible transcription factor that plays critical roles in immune and stress responses and is often implicated in pathologies, including chronic inflammation and cancer. Although much has been learned about NF-κB-activating pathways, the specific repression of NF-κB is far less well understood. Here we identified the type I protein arginine methyltransferase 1 (PRMT1) as a restrictive factor controlling TNFα-induced activation of NF-κB. PRMT1 forms a cellular complex with NF-κB through direct interaction with the Rel homology domain of RelA...
April 19, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/27041824/the-role-of-protein-arginine-methyltransferases-in-inflammatory-responses
#20
REVIEW
Ji Hye Kim, Byong Chul Yoo, Woo Seok Yang, Eunji Kim, Sungyoul Hong, Jae Youl Cho
Protein arginine methyltransferases (PRMTs) mediate the methylation of a number of protein substrates of arginine residues and serve critical functions in many cellular responses, including cancer development, progression, and aggressiveness, T-lymphocyte activation, and hepatic gluconeogenesis. There are nine members of the PRMT family, which are divided into 4 types (types I-IV). Although most PRMTs do not require posttranslational modification (PTM) to be activated, fine-tuning modifications, such as interactions between cofactor proteins, subcellular compartmentalization, and regulation of RNA, via micro-RNAs, seem to be required...
2016: Mediators of Inflammation
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