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https://www.readbyqxmd.com/read/29129692/prmt1-mediates-podocyte-injury-and-glomerular-fibrosis-through-phosphorylation-of-erk-pathway
#1
Yu Zhu
Diabetic nephropathy (DN) is characterized by a change of glomerular structure and dysfunction of filtration barrier, which significantly accompanied by podocytes apoptosis and glomerular fibrosis. Angiotensin Ⅱ(Ang Ⅱ) induced activation of ERK1/2 signaling plays important roles in causing apoptosis of podocytes in DN kidneys. Previous studies have shown that PRMT1 have a pro-inflammatory function through activating ERK1/2 signaling pathway during development of chronic pulmonary disease, however, its role in DN development has not been investigated...
November 10, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29128891/prmt1-promotes-hyperglycemia-in-a-foxo1-dependent-manner-affecting-glucose-metabolism-during-hypobaric-hypoxia-exposure-in-rat-model
#2
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...
November 11, 2017: Endocrine
https://www.readbyqxmd.com/read/29119338/elevated-levels-of-adma-are-associated-with-lower-ddah2-and-higher-prmt1-in-lps-induced-endometritis-rats
#3
Hong-Bo Xiao, Guo-Guang Sui, Xiang-Yang Lu, Zhi-Liang Sun
Chronic endometritis is a continuous inflammation of uterine endometrium. Recent research has shown that higher asymmetric dimethylarginine (ADMA) levels contribute to endothelial dysfunction. In the present study, we tested whether there is a correlation between endometritis and ADMA in LPS-induced endometritis rat and the mechanisms involved. Thirty-six rats were divided into two groups: blank control group and rat model of endometritis group. The entire infused uterus were removed to observe the changes of histopathology, production of myeloperoxidase (MPO), tumor necrosis factor-α (TNF-α), interleukin (IL)-6, 8-isoprostane, and reactive oxygen species (ROS), and gene expression of dimethylarginine dimethylaminohydrolase 2 (DDAH2), protein-methyl transferase 1 (PRMT1), TNF-α, and IL-6...
November 8, 2017: Inflammation
https://www.readbyqxmd.com/read/29113301/ucp2-and-prmt1-are-key-prognostic-markers-for-lung-carcinoma-patients
#4
Corina T Madreiter-Sokolowski, Balázs Győrffy, Christiane Klec, Armin A Sokolowski, Rene Rost, Markus Waldeck-Weiermair, Roland Malli, Wolfgang F Graier
Cancer cells have developed unique strategies to meet their high energy demand. Therefore, they have established a setting of Ca(2+)-triggered high mitochondrial activity. But mitochondrial Ca(2+) uptake has to be strictly controlled to avoid mitochondrial Ca(2+) overload that would cause apoptotic cell death. Methylation by protein arginine methyl transferase 1 (PRMT1) desensitizes the mitochondrial Ca(2+) uptake machinery and reduces mitochondrial Ca(2+) accumulation in cancer cells. In case of PRMT1-driven methylation, proper mitochondrial Ca(2+) uptake is reestablished by increased activity of uncoupling protein 2 (UCP2), pointing to an importance of these proteins for cancer cell survival and activity...
October 6, 2017: Oncotarget
https://www.readbyqxmd.com/read/29112789/kinetic-analysis-of-prmt1-reveals-multifactorial-processivity-and-a-sequential-ordered-mechanism
#5
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 reveal human protein arginine N-methyltransferase 1 (PRMT1) enzyme kinetics are dependent on substrate sequence. Further, peptides containing a Nη-hydroxyarginine generally demonstrate substrate inhibition and have improved KM values, which evokes a possible role in inhibitor design...
November 7, 2017: Chembiochem: a European Journal of Chemical Biology
https://www.readbyqxmd.com/read/29112628/exercise-induced-protein-arginine-methyltransferase-expression-in-skeletal-muscle
#6
Tiffany L vanLieshout, Derek W Stouth, Tania Tajik, Vladimir Ljubicic
PURPOSE: This study aimed to determine protein arginine methyltransferase 1 (PRMT1), -4 (also known as coactivator-associated arginine methyltransferase 1; CARM1), and -5 expression and function during acute, exercise-induced skeletal muscle remodelling in vivo. METHODS: C57BL/6 mice were assigned to one of three experimental groups: sedentary, acute bout of exercise, or acute exercise followed by 3 hours of recovery. The mice in the exercise groups performed a single bout of treadmill running at 15 m/min for 90 minutes...
November 6, 2017: Medicine and Science in Sports and Exercise
https://www.readbyqxmd.com/read/29097184/protein-arginine-methyltransferase-1-coordinates-the-epithelial-mesenchymal-transition-proliferation-dichotomy-in-gastric-cancer-cells
#7
Youli Zhang, Dawei Wang, Meiting Zhang, Hong Wei, Ying Lu, Yaocheng Sun, Meng Zhou, Shuming Gu, Wen Feng, Huizhi Wang, Jian Zeng, Aihua Gong, Min Xu
Protein arginine methyltransferase 1 (PRMT1) is up-regulated and promotes migration, invasion and proliferation in wide range of cancers. However, we for the first time identify that PRMT1 promotes migration and invasion and inhibits proliferation in gastric cancer cells, a phenomenon called "migration-proliferation dichotomy". First, we find that PRMT1 overexpression promotes migration and invasion and inhibits proliferation,whereas PRMT1 knockdown reverses the above abilities. Next, PRMT1 reduces the expression of epithelial marker E-cadherin and increases the expression of mesenchymal markers including N-cadherin, Vimentin, snail and β-catenin in gastric cancer cells...
October 30, 2017: Experimental Cell Research
https://www.readbyqxmd.com/read/29092819/protein-arginine-methyltransferase-expression-localization-and-activity-during-disuse-induced-skeletal-muscle-plasticity
#8
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/29075615/pharmacologic-targeting-of-chromatin-modulators-as-therapeutics-of-acute-myeloid-leukemia
#9
REVIEW
Rui Lu, Gang Greg Wang
Acute myeloid leukemia (AML), a common hematological cancer of myeloid lineage cells, generally exhibits poor prognosis in the clinic and demands new treatment options. Recently, direct sequencing of samples from human AMLs and pre-leukemic diseases has unveiled their mutational landscapes and significantly advanced the molecular understanding of AML pathogenesis. The newly identified recurrent mutations frequently "hit" genes encoding epigenetic modulators, a wide range of chromatin-modifying enzymes and regulatory factors involved in gene expression regulation, supporting aberration of chromatin structure and epigenetic modification as a main oncogenic mechanism and cancer-initiating event...
2017: Frontiers in Oncology
https://www.readbyqxmd.com/read/29055959/impaired-arginine-metabolism-coupled-to-a-defective-redox-conduit-contributes-to-low-plasma-nitric-oxide-in-polycystic-ovary-syndrome
#10
Meera B Krishna, Annu Joseph, Philip Litto Thomas, Belinda Dsilva, Sathy M Pillai, Malini Laloraya
BACKGROUND: Though oxidative stress is associated with Polycystic Ovary Syndrome (PCOS), the status of nitric oxide is still unclear. Nitric Oxide (NO) plays pivotal roles in many physiological functions which are compromised in PCOS. Our recent study reveals lowered T-regulatory cells (Tregs) in PCOS, and Treg generation is known to be regulated by NO levels. However concrete evidences are lacking on mechanisms modulating NO levels under PCOS. METHODS: This is a retrospective case-control cohort study, comprised of PCOS women (N=29) and normal menstruating women as controls (N=20)...
October 20, 2017: Cellular Physiology and Biochemistry
https://www.readbyqxmd.com/read/29026071/arginine-methylation-catalyzed-by-prmt1-is-required-for-b-cell-activation-and-differentiation
#11
Simona Infantino, Amanda Light, Kristy O'Donnell, Vanessa Bryant, Danielle T Avery, Michael Elliott, Stuart G Tangye, Gabrielle Belz, Fabienne Mackay, Stephane Richard, David Tarlinton
Arginine methylation catalyzed by protein arginine methyltransferases (PRMT) is a common post-translational modification in mammalian cells, regulating many important functions including cell signalling, proliferation and differentiation. Here we show the role of PRMT1 in B-cell activation and differentiation. PRMT1 expression and activity in human and mouse peripheral B cells increases in response to in vitro or in vivo activation. Deletion of the Prmt1 gene in mature B cells establishes that although the frequency and phenotype of peripheral B cell subsets seem unaffected, immune responses to T-cell-dependent and -independent antigens are substantially reduced...
October 12, 2017: Nature Communications
https://www.readbyqxmd.com/read/29023917/prmt1-and-jmjd6-dependent-arginine-methylation-regulate-hnf4%C3%AE-expression-and-hepatocyte-proliferation
#12
Jie Zhao, Abby Adams, Ben Roberts, Maura O'Neil, Anusha Vittal, Timothy Schmitt, Sean Kumer, Josiah Cox, Zhuan Li, Steven A Weinman, Irina Tikhanovich
Alcohol is a well-established risk factor for hepatocellular carcinoma, but the mechanisms by which it promotes liver cancer are not well understood. Several studies have shown that cellular protein arginine methylation is inhibited by alcohol. Arginine methylation is controlled by the reciprocal activity of protein arginine methyltransferases, primarily PRMT1, and a demethylase JMJD6. The aim of this study was to explore the role of arginine methylation changes in alcohol pathogenesis. We found that PRMT1 activity is inhibited in livers of mice fed with alcohol compared to pair-fed mice...
October 10, 2017: Hepatology: Official Journal of the American Association for the Study of Liver Diseases
https://www.readbyqxmd.com/read/28978671/transcriptional-memory-of-cells-of-origin-overrides-%C3%AE-catenin-requirement-of-mll-cancer-stem-cells
#13
Teerapong Siriboonpiputtana, Bernd B Zeisig, Magdalena Zarowiecki, Tsz Kan Fung, Maria Mallardo, Chiou-Tsun Tsai, Priscilla Nga Ieng Lau, Quoc Chinh Hoang, Pedro Veiga, Jo Barnes, Claire Lynn, Amanda Wilson, Boris Lenhard, Chi Wai Eric So
While β-catenin has been demonstrated as an essential molecule and therapeutic target for various cancer stem cells (CSCs) including those driven by MLL fusions, here we show that transcriptional memory from cells of origin predicts AML patient survival and allows β-catenin-independent transformation in MLL-CSCs derived from hematopoietic stem cell (HSC)-enriched LSK population but not myeloid-granulocyte progenitors. Mechanistically, β-catenin regulates expression of downstream targets of a key transcriptional memory gene, Hoxa9 that is highly enriched in LSK-derived MLL-CSCs and helps sustain leukemic self-renewal...
November 2, 2017: EMBO Journal
https://www.readbyqxmd.com/read/28973953/new-roles-for-old-actors-ros-and-prmt1
#14
Subba Reddy Palli
No abstract text is available yet for this article.
October 10, 2017: Proceedings of the National Academy of Sciences of the United States of America
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
#15
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/28943242/csnk1a1-regulates-prmt1-to-maintain-the-progenitor-state-in-self-renewing-somatic-tissue
#16
Xiaomin Bao, Zurab Siprashvili, Brian J Zarnegar, Rajani M Shenoy, Eon J Rios, Natalie Nady, Kun Qu, Angela Mah, Daniel E Webster, Adam J Rubin, Glenn G Wozniak, Shiying Tao, Joanna Wysocka, Paul A Khavari
Somatic progenitors sustain tissue self-renewal while suppressing premature differentiation. Protein arginine methyltransferases (PRMTs) affect many processes; however, their role in progenitor function is incompletely understood. PRMT1 was found to be the most highly expressed PRMT in epidermal progenitors and the most downregulated PRMT during differentiation. In targeted mouse knockouts and in long-term regenerated human mosaic epidermis in vivo, epidermal PRMT1 loss abolished progenitor self-renewal and led to premature differentiation...
October 23, 2017: Developmental Cell
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
#17
COMPARATIVE STUDY
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
#18
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...
October 15, 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
#19
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
#20
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
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