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https://www.readbyqxmd.com/read/27903134/o-glcnac-glycosylation-stoichiometry-of-the-fet-protein-family-only-ews-is-glycosylated-with-a-high-stoichiometry
#1
Kazuo Kamemura
Of the FET (fused in sarcoma [FUS]/Ewing sarcoma protein [EWS]/TATA binding protein-associated factor 15 [TAF15]) family of heterogeneous nuclear ribonucleoprotein particle proteins, FUS and TAF15 are consistently and EWS variably found in inclusion bodies in neurodegenerative diseases such as frontotemporal lobar degeneration associated with FUS. It is speculated that dysregulation of FET proteins at the post-translational level is involved in their cytoplasmic deposition. Here, the O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation stoichiometry of the FET proteins was chemoenzymatically analyzed, and it was found that only EWS is dynamically glycosylated with a high stoichiometry in the neural cell lines tested and in mouse brain...
December 1, 2016: Bioscience, Biotechnology, and Biochemistry
https://www.readbyqxmd.com/read/27864466/thiamet-g-mediates-neuroprotection-in-experimental-stroke-by-modulating-microglia-macrophage-polarization-and-inhibiting-nf-%C3%AE%C2%BAb-p65-signaling
#2
Yating He, Xiaofeng Ma, Daojing Li, Junwei Hao
Inflammatory responses are accountable for secondary injury induced by acute ischemic stroke (AIS). Previous studies indicated that O-GlcNAc modification (O-GlcNAcylation) is involved in the pathology of AIS, and increase of O-GlcNAcylation by glucosamine attenuated the brain damage after ischemia/reperfusion. Inhibition of β-N-acetylglucosaminidase (OGA) with thiamet G (TMG) is an alternative option for accumulating O-GlcNAcylated proteins. In this study, we investigate the neuroprotective effect of TMG in a mouse model of experimental stroke...
November 18, 2016: Journal of Cerebral Blood Flow and Metabolism
https://www.readbyqxmd.com/read/27845045/o-linked-n-acetylglucosamine-transferase-is-associated-with-metastatic-spread-of-human-papillomavirus-e6-and-e7-oncoproteins-to-the-lungs-of-mice
#3
Sung Hwan Kim, Yoon Sook Kim, Mee Young Choi, Minjun Kim, Jun Ho Yang, Hyun Oh Park, In Seok Jang, Sung Ho Moon, Hyun Ok Kim, Dae Hyun Song, Dong Hoon Lee, Gu Seob Roh, Hyun Joon Kim, Sang Soo Kang, Gyeong Jae Cho, Jun Young Choi, Wan Sung Choi
High-risk human papilloma virus (HPV) 16/18 infections are often found in lung cancer. The cellular mechanisms involved in the metastatic spread of HPV-infected cervical cancer cells remain largely elusive. High O-linked-N-acetylglucosamine (O-GlcNAc) modification has also been observed in lung cancer. In the present study, we assessed the relationship between O-GlcNAc transferase (OGT) and HPV 16/18 E6/E7, or C-X-C chemokine receptor type 4 (CXCR4), in HeLa cells and in lungs of xenografted mice. Depleting OGT with an OGT-specific shRNA significantly decreased levels of E6 and E7 oncoproteins in HeLa cells and xenograft tumors, and reduced tumor formation in vivo...
November 11, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27830009/glycosylation-patterns-and-pha-e-associated-glycoprotein-profiling-associated-with-early-hepatic-encephalopathy-in-chinese-hepatocellular-carcinoma-patients
#4
Tian-Hua Liu, Deng-He Liu, Cui-Ju Mo, Lu Sun, Xiao-Xia Liu, Wei Li, Shu Zhang, Yin-Kun Liu, Kun Guo
Hepatic encephalopathy (HE) as a severe neuropsychiatric complication is commonly present in the end stage of Hepatocellular Carcinoma (HCC). However, widely accepted biomarkers for diagnosing early HE are still absent. Here, we screened glycosylation patterns of serum proteins from Chinese HCC patients with or without early HE by lectin microarray. Then, phaseolus vulgaris erythroagglutinin (PHA-E) as a lectin binding with bisecting GlcNAc structure which was significantly decreased in sera from Chinese HCC patients with early HE, was chosen to perform lectin affinity chromatography, following by in-gel digestion, Mass Spectrometry (MS) analysis and bioinformatics analysis...
2016: American Journal of Translational Research
https://www.readbyqxmd.com/read/27816939/o-glcnacylation-of-ogg1-impairs-oxidative-mitochondrial-dna-lesion-repair-in-diabetic-hearts
#5
Federico Cividini, Brian T Scott, Anzhi Dai, Wenlong Han, Jorge Suarez, Julieta Diaz-Juarez, Tanja Diemer, Darren E Casteel, Wolfgang H Dillmann
Mitochondrial DNA (mtDNA) damage in cardiac myocytes resulting from increased oxidative stress is emerging as an important factor in the pathogenesis of diabetic cardiomyopathy. A prevalent lesion that occurs in mtDNA damage is the formation of 8-hydroxy-2-deoxyguanosine (8-OHdG), which can cause mutations if not repaired properly by 8-oxoguanine DNA glycosylase (Ogg1). Although the mtDNA repair machinery has been described in cardiac myocytes, the regulation of this repair has been incompletely investigated...
November 5, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27798069/recombinant-fungal-lectin-as-a-new-tool-to-investigate-o-glcnacylation-processes
#6
Oriane Machon, Steffi F Baldini, João P Ribeiro, Agata Steenackers, Annabelle Varrot, Tony Lefebvre, Anne Imberty
Glycosylation is a group of post-translational modifications that displays a large variety of structures and are implicated in a plethora of biological processes. Therefore, studying glycosylation requires different technical approaches and reliable tools, lectins being part of them. Here we describe the use of the recombinant mushroom lectin PVL to discriminate O-GlcNAcylation, a modification consisting in the attachment of a single N-acetylglucosamine residue to proteins confined within the cytosolic, nuclear and mitochondrial compartments...
October 18, 2016: Glycobiology
https://www.readbyqxmd.com/read/27776166/glucosamine-downregulates-the-il-1%C3%AE-induced-expression-of-proinflammatory-cytokine-genes-in-human-synovial-mh7a-cells-by-o-glcnac-modification-dependent-and-independent-mechanisms
#7
Akimasa Someya, Takako Ikegami, Koji Sakamoto, Isao Nagaoka
Osteoarthritis (OA) is one of the major joint diseases, and the synovial inflammation is involved in the pathogenesis and progression of OA. Glucosamine (GlcN) is widely used as a dietary supplement for OA, and is expected to exert the antiinflammatory action in OA. However, the detailed mechanism for the antiinflammatory action of GlcN remains poorly understood. In this study, to elucidate the molecular mechanism involved in the GlcN-medicated regulation of synovial cell activation, we comprehensively analyzed the effect of GlcN on the gene expression using a human synovial cell line MH7A by DNA microarray...
2016: PloS One
https://www.readbyqxmd.com/read/27751836/hyper-o-glcnacylation-of-yb-1-affects-ser102-phosphorylation-and-promotes-cell-proliferation-in-hepatocellular-carcinoma
#8
Qingqing Liu, Tao Tao, Fang Liu, Runzhou Ni, Cuihua Lu, Aiguo Shen
As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility. Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes...
October 14, 2016: Experimental Cell Research
https://www.readbyqxmd.com/read/27716624/targeting-the-hexosamine-biosynthetic-pathway-and-o-linked-n-acetylglucosamine-cycling-for-therapeutic-and-imaging-capabilities-in-diffuse-large-b-cell-lymphoma
#9
Lan V Pham, Jerry L Bryant, Richard Mendez, Juan Chen, Archito T Tamayo, Zijun Y Xu-Monette, Ken H Young, Ganiraju C Manyam, David Yang, L Jeffrey Medeiros, Richard J Ford
The hexosamine biosynthetic pathway (HBP) requires two key nutrients glucose and glutamine for O-linked N-acetylglucosamine (O-GlcNAc) cycling, a post-translational protein modification that adds GlcNAc to nuclear and cytoplasmic proteins. Increased GlcNAc has been linked to regulatory factors involved in cancer cell growth and survival. However, the biological significance of GlcNAc in diffuse large B-cell lymphoma (DLBCL) is not well defined. This study is the first to show that both the substrate and the endpoint O-GlcNAc transferase (OGT) enzyme of the HBP were highly expressed in DLBCL cell lines and in patient tumors compared with normal B-lymphocytes...
October 3, 2016: Oncotarget
https://www.readbyqxmd.com/read/27713473/identification-of-the-nuclear-localisation-signal-of-o-glcnac-transferase-and-its-nuclear-import-regulation
#10
Hyeon Gyu Seo, Han Byeol Kim, Min Jueng Kang, Joo Hwan Ryum, Eugene C Yi, Jin Won Cho
Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues. Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear. Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase. OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted...
October 7, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27703839/formal-modeling-and-analysis-of-the-hexosamine-biosynthetic-pathway-role-of-o-linked-n-acetylglucosamine-transferase-in-oncogenesis-and-cancer-progression
#11
Muhammad Tariq Saeed, Jamil Ahmad, Shahzina Kanwal, Andreana N Holowatyj, Iftikhar A Sheikh, Rehan Zafar Paracha, Aamir Shafi, Amnah Siddiqa, Zurah Bibi, Mukaram Khan, Amjad Ali
The alteration of glucose metabolism, through increased uptake of glucose and glutamine addiction, is essential to cancer cell growth and invasion. Increased flux of glucose through the Hexosamine Biosynthetic Pathway (HBP) drives increased cellular O-GlcNAcylation (hyper-O-GlcNAcylation) and contributes to cancer progression by regulating key oncogenes. However, the association between hyper-O-GlcNAcylation and activation of these oncogenes remains poorly characterized. Here, we implement a qualitative modeling framework to analyze the role of the Biological Regulatory Network in HBP activation and its potential effects on key oncogenes...
2016: PeerJ
https://www.readbyqxmd.com/read/27687229/functional-analysis-of-recombinant-human-and-yarrowia-lipolytica-o-glcnac-transferases-expressed-in-saccharomyces-cerevisiae
#12
Hye Ji Oh, Hye Yun Moon, Seon Ah Cheon, Yoonsoo Hahn, Hyun Ah Kang
O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is an important post-translational modification in many cellular processes. It is mediated by O-GlcNAc transferases (OGTs), which catalyze the addition of O-GlcNAc to serine or threonine residues of the target proteins. In this study, we expressed a putative Yarrowia lipolytica OGT (YlOGT), the only homolog identified in the subphylum Saccharomycotina through bioinformatics analysis, and the human OGT (hOGT) as recombinant proteins in Saccharomyces cerevisiae, and performed their functional characterization...
October 2016: Journal of Microbiology / the Microbiological Society of Korea
https://www.readbyqxmd.com/read/27683279/high-extent-of-o-glcnacylation-in-breast-cancer-cells-correlates-with-the-levels-of-has-enzymes-accumulation-of-hyaluronan-and-poor-outcome
#13
Satu Tiainen, Sanna Oikari, Markku Tammi, Kirsi Rilla, Kirsi Hämäläinen, Raija Tammi, Veli-Matti Kosma, Päivi Auvinen
PURPOSE: Obesity and oversupply of glucose, e.g., due to nutritional factors may shape the tumor microenvironment favorable for tumor progression. O-GlcNAcylation, a reversible modification of intracellular proteins, influences on several cellular functions and is connected to many diseases including cancer. Glycosaminoglycan hyaluronan (HA) enhances tumor progression and in breast cancer HA accumulation associates strongly with poor outcome. In vitro studies have suggested that O-GlcNAcylation may enhance HA synthesis...
November 2016: Breast Cancer Research and Treatment
https://www.readbyqxmd.com/read/27669760/combined-antibody-lectin-enrichment-identifies-extensive-changes-in-the-o-glcnac-sub-proteome-upon-oxidative-stress
#14
Albert Lee, Devin Miller, Roger Henry, Venkata D P Paruchuri, Robert N O'Meally, Tatiana Boronina, Robert N Cole, Natasha E Zachara
O-Linked N-acetyl-β-d-glucosamine (O-GlcNAc) is a dynamic post-translational modification that modifies and regulates over 3000 nuclear, cytoplasmic, and mitochondrial proteins. Upon exposure to stress and injury, cells and tissues increase the O-GlcNAc modification, or O-GlcNAcylation, of numerous proteins promoting the cellular stress response and thus survival. The aim of this study was to identify proteins that are differentially O-GlcNAcylated upon acute oxidative stress (H2O2) to provide insight into the mechanisms by which O-GlcNAc promotes survival...
October 14, 2016: Journal of Proteome Research
https://www.readbyqxmd.com/read/27664189/exercise-training-increases-protein-o-glcnacylation-in-rat-skeletal-muscle
#15
Kristin Halvorsen Hortemo, Per Kristian Lunde, Jan Haug Anonsen, Heidi Kvaløy, Morten Munkvik, Tommy Aune Rehn, Ivar Sjaastad, Ida Gjervold Lunde, Jan Magnus Aronsen, Ole M Sejersted
Protein O-GlcNAcylation has emerged as an important intracellular signaling system with both physiological and pathophysiological functions, but the role of protein O-GlcNAcylation in skeletal muscle remains elusive. In this study, we tested the hypothesis that protein O-GlcNAcylation is a dynamic signaling system in skeletal muscle in exercise and disease. Immunoblotting showed different protein O-GlcNAcylation pattern in the prototypical slow twitch soleus muscle compared to fast twitch EDL from rats, with greater O-GlcNAcylation level in soleus associated with higher expression of the modulating enzymes O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and glutamine fructose-6-phosphate amidotransferase isoforms 1 and 2 (GFAT1, GFAT2)...
September 2016: Physiological Reports
https://www.readbyqxmd.com/read/27646831/the-regulatory-roles-of-o-glcnacylation-in-mitochondrial-homeostasis-and-metabolic-syndrome
#16
Lin Zhao, Zhihui Feng, Xiaoyong Yang, Jiankang Liu
Nutrients excess is one of the leading causes of metabolic syndrome globally. Protein post-translational O-GlcNAc modification has been recognized as an essential nutrient sensor of the cell. Emerging studies suggest that O-GlcNAcylation lies at the core linking nutritional stress to insulin resistance. Mitochondria are the major site for ATP production in most eukaryotes. Mitochondrial dysfunction and oxidative stress have long been considered as an important mechanism underlying insulin resistance. The metabolic process is under the influence of environmental and nutritional factors, thus sensing and transducing nutritional signals sit at the pivot of metabolism control...
September 20, 2016: Free Radical Research
https://www.readbyqxmd.com/read/27629714/schwann-cell-o-glcnac-glycosylation-is-required-for-myelin-maintenance-and-axon-integrity
#17
Sungsu Kim, Jason C Maynard, Yo Sasaki, Amy Strickland, Diane L Sherman, Peter J Brophy, Alma L Burlingame, Jeffrey Milbrandt
UNLABELLED: Schwann cells (SCs), ensheathing glia of the peripheral nervous system, support axonal survival and function. Abnormalities in SC metabolism affect their ability to provide this support and maintain axon integrity. To further interrogate this metabolic influence on axon-glial interactions, we generated OGT-SCKO mice with SC-specific deletion of the metabolic/nutrient sensing protein O-GlcNAc transferase that mediates the O-linked addition of N-acetylglucosamine (GlcNAc) moieties to Ser and Thr residues...
September 14, 2016: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/27622469/an-oga-resistant-probe-allows-specific-visualization-and-accurate-identification-of-o-glcnac-modified-proteins-in-cells
#18
Jing Li, Jiajia Wang, Liuqing Wen, He Zhu, Shanshan Li, Kenneth Huang, Kuan Jiang, Xu Li, Cheng Ma, Jingyao Qu, Aishwarya Parameswaran, Jing Song, Wei Zhao, Peng George Wang
O-linked β-N-acetyl-glucosamine (O-GlcNAc) is an essential and ubiquitous post-translational modification present in nucleic and cytoplasmic proteins of multicellular eukaryotes. The metabolic chemical probes such as GlcNAc or GalNAc analogues bearing ketone or azide handles, in conjunction with bioorthogonal reactions, provide a powerful approach for detecting and identifying this modification. However, these chemical probes either enter multiple glycosylation pathways or have low labeling efficiency. Therefore, selective and potent probes are needed to assess this modification...
October 14, 2016: ACS Chemical Biology
https://www.readbyqxmd.com/read/27615797/novel-o-glcnacylation-on-ser-40-of-canonical-h2a-isoforms-specific-to-viviparity
#19
Mitsuko Hirosawa, Koji Hayakawa, Chikako Yoneda, Daisuke Arai, Hitoshi Shiota, Takehiro Suzuki, Satoshi Tanaka, Naoshi Dohmae, Kunio Shiota
We report here newly discovered O-linked-N-acetylglucosamine (O-GlcNAc) modification of histone H2A at Ser(40) (H2AS40Gc). The mouse genome contains 18 H2A isoforms, of which 13 have Ser(40) and the other five have Ala(40). The combination of production of monoclonal antibody and mass spectrometric analyses with reverse-phase (RP)-high performance liquid chromatography (HPLC) fractionation indicated that the O-GlcNAcylation is specific to the Ser(40) isoforms. The H2AS40Gc site is in the L1 loop structure where two H2A molecules interact in the nucleosome...
2016: Scientific Reports
https://www.readbyqxmd.com/read/27605304/the-glycosylation-stoichiometry-of-ews-species-in-neuronal-cells
#20
Kazuo Kamemura, Hiromi Abe
Although Ewing sarcoma protein (EWS) is known to be glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc), the dynamics and stoichiometry of its glycosylation remain obscure. Here, we report a dynamic change in the glycosylation stoichiometry of EWS species during neuronal differentiation of embryonic carcinoma P19 cells. Our findings suggest that O-GlcNAc glycosylation participates in the regulation of EWS functions in neuronal cells.
September 8, 2016: Bioscience, Biotechnology, and Biochemistry
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