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https://www.readbyqxmd.com/read/29774032/protein-o-glcnac-modification-increases-in-white-blood-cells-after-a-single-bout-of-physical-exercise
#1
Tamás Nagy, Emese Kátai, Viktória Fisi, Tamás Tibor Takács, Antal Stréda, István Wittmann, Attila Miseta
Background: Protein O-linked N -acetylglucosamine (O-GlcNAc) is a dynamic posttranslational modification influencing the function of many intracellular proteins. Recently it was revealed that O-GlcNAc regulation is modified under various stress states, including ischemia and oxidative stress. Aside from a few contradictory studies based on animal models, the effect of exercise on O-GlcNAc is unexplored. Purpose: To evaluate O-GlcNAc levels in white blood cells (WBC) of human volunteers following physical exercise...
2018: Frontiers in Immunology
https://www.readbyqxmd.com/read/29772801/ogt-o-glcnac-transferase-selectively-modifies-multiple-residues-unique-to-lamin-a
#2
Dan N Simon, Amanda Wriston, Qiong Fan, Jeffrey Shabanowitz, Alyssa Florwick, Tejas Dharmaraj, Sherket B Peterson, Yosef Gruenbaum, Cathrine R Carlson, Line M Grønning-Wang, Donald F Hunt, Katherine L Wilson
The LMNA gene encodes lamins A and C with key roles in nuclear structure, signaling, gene regulation, and genome integrity. Mutations in LMNA cause over 12 diseases ('laminopathies'). Lamins A and C are identical for their first 566 residues. However, they form separate filaments in vivo, with apparently distinct roles. We report that lamin A is β- O -linked N -acetylglucosamine- (O -GlcNAc)-modified in human hepatoma (Huh7) cells and in mouse liver. In vitro assays with purified O -GlcNAc transferase (OGT) enzyme showed robust O -GlcNAcylation of recombinant mature lamin A tails (residues 385⁻646), with no detectable modification of lamin B1, lamin C, or 'progerin' (Δ50) tails...
May 17, 2018: Cells
https://www.readbyqxmd.com/read/29771506/the-metabolic-chemical-reporter-6-azido-6-deoxy-glucose-further-reveals-the-substrate-promiscuity-of-o-glcnac-transferase-and-catalyzes-the-discovery-of-intracellular-protein-modification-by-o-glucose
#3
Narek Darabedian, Jinxu Gao, Kelly N Chuh, Christina M Woo, Matthew R Pratt
Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research labs for the identification and visualization of glycoconjugates. More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to dif-ferent sugars. Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc)...
May 17, 2018: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/29769320/o-glcnac-transferase-missense-mutations-linked-to-x-linked-intellectual-disability-deregulate-genes-involved-in-cell-fate-determination-and-signaling
#4
Nithya Selvan, Stephan George, Fatema J Serajee, Marie Shaw, Lynne Hobson, Vera M Kalscheuer, Nripesh Prasad, Shawn E Levy, Juliet Taylor, Salim Afitmos, Charles E Schwartz, Ahm M Huq, Jozef Gecz, Lance Wells
It is estimated that ~1% of the world's population has intellectual disability, with males affected more often than females. OGT is an X-linked gene encoding for the enzyme O-GlcNAc transferase (OGT), which carries out the reversible addition of N-Acetylglucosamine (GlcNAc) to Ser/Thr residues of its intracellular substrates. Three missense mutations in the tetratricopeptide (TPR) repeats of OGT have recently been reported to cause X-linked Intellectual Disability (XLID). Here we report the discovery of two additional novel missense mutations (c...
May 16, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29756380/metabolic-inhibitors-of-o-glcnac-transferase-ogt-that-act-in-vivo-implicate-decreased-o-glcnac-levels-in-leptin-mediated-nutrient-sensing
#5
Ta-Wei Liu, Wesley F Zandberg, Tracey M Gloster, Lehua Deng, Kelsey D Murray, Xiaoyang Shan, David Jaro Vocadlo
O-linked glycosylation of serine and threonine residues of nucleocytoplasmic proteins with N-acetylglucosamine (O-GlcNAc) residues is catalyzed by O-GlcNAc transferase (OGT). O-GlcNAc is conserved within mammals and is implicated in a wide range of physiological processes. Here we describe metabolic precursor inhibitors of OGT suitable for use both in cells and in vivo in mice. These 5-thiosugar analogues of N-acetylglucosamine are assimilated through a convergent metabolic pathway, most likely involving N-acetylglucosamine-6-phosphate de-N-acetylase (NAGA) to generate a common OGT inhibitor within cells...
May 14, 2018: Angewandte Chemie
https://www.readbyqxmd.com/read/29746846/o-linked-n-acetyl-glucosamine-deposition-in-placental-proteins-varies-according-to-maternal-glycemic-levels
#6
Vanessa Dela Justina, Rinaldo R Dos Passos Junior, Alecsander F Bressan, Rita C Tostes, Fernando S Carneiro, Thaigra S Soares, Gustavo T Volpato, Victor Vitorino Lima, Sebastian San Martin, Fernanda R Giachini
AIMS: Hyperglycemia increases glycosylation with O-linked N‑acetyl‑glucosamine (O-GlcNAc) contributing to placental dysfunction and fetal growth impairment. Our aim was to determine how O-GlcNAc levels are affected by hyperglycemia and the O-GlcNAc distribution in different placental regions. MAIN METHODS: Female Wistar rats were divided into the following groups: severe hyperglycemia (>300 mg/dL; n = 5); mild hyperglycemia (>140 mg/dL, at least than two time points during oral glucose tolerance test; n = 7) or normoglycemia (<120 mg/dL; n = 6)...
May 7, 2018: Life Sciences
https://www.readbyqxmd.com/read/29723473/thio-linked-udp-peptide-conjugates-as-o-glcnac-transferase-inhibitors
#7
Karim Rafie, Andrii Gorelik, Riccardo Trapannone, Vladimir S Borodkin, Daan M F Aalten
O-GlcNAc transferase (OGT) is an essential glycosyltransferase that installs the O-GlcNAc posttranslational modification on the nucleocytoplasmic proteome. We report the development of S-linked UDP-peptide conjugates as potent bisubstrate OGT inhibitors. These compounds were assembled in a modular fashion by photo-initiated thiol-ene conjugation of allyl-UDP and optimal acceptor peptides in which the acceptor serine was replaced with cysteine. The conjugate VTPVC(S-propyl-UDP)TA (Ki = 1.3 µM) inhibits the OGT activity in HeLa cell lysates...
May 3, 2018: Bioconjugate Chemistry
https://www.readbyqxmd.com/read/29720943/microrna-200a-200b-modulate-high-glucose-induced-endothelial-inflammation-by-targeting-o-linked-n-acetylglucosamine-transferase-expression
#8
Wan-Yu Lo, Wen-Kai Yang, Ching-Tien Peng, Wan-Yu Pai, Huang-Joe Wang
Background and Aims: Increased O -linked N -acetylglucosamine ( O -GlcNAc) modification of proteins by O -GlcNAc transferase (OGT) is associated with diabetic complications. Furthermore, oxidative stress promotes endothelial inflammation during diabetes. A previous study reported that microRNA-200 (miR-200) family members are sensitive to oxidative stress. In this study, we examined whether miR-200a and miR-200b regulate high-glucose (HG)-induced OGT expression in human aortic endothelial cells (HAECs) and whether miRNA-200a/200b downregulate OGT expression to control HG-induced endothelial inflammation...
2018: Frontiers in Physiology
https://www.readbyqxmd.com/read/29717537/crosstalk-between-phosphorylation-and-o-glcnacylation-friend-or-foe
#9
REVIEW
Saar A M van der Laarse, Aneika C Leney, Albert J R Heck
A wide variety of protein post-translational modifications (PTMs) decorate cellular proteins, regulating their structure, interactions and ultimately their function. The density of co-occurring PTMs on proteins can be very high, where multiple PTMs can positively or negatively influence each others actions, nowadays termed PTM crosstalk. In this review we highlight recent progress in the area of PTM crosstalk, whereby we focus on crosstalk between protein phosphorylation and O-GlcNAcylation. These two PTMs largely target identical (i...
May 2, 2018: FEBS Journal
https://www.readbyqxmd.com/read/29706631/o-glcnac-elevation-through-activation-of-the-hexosamine-biosynthetic-pathway-enhances-cancer-cell-chemoresistance
#10
Yubo Liu, Yu Cao, Xiaoqing Pan, Meiyun Shi, Qiong Wu, Tianmiao Huang, Hui Jiang, Wenli Li, Jianing Zhang
Chemoresistance has become a major obstacle to the success of cancer therapy, but the mechanisms underlying chemoresistance are not yet fully understood. O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions. Here we assessed the role of O-GlcNAcylation in chemoresistance and investigated the underlying cellular mechanisms. The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation...
April 30, 2018: Cell Death & Disease
https://www.readbyqxmd.com/read/29689198/grasp55-senses-glucose-deprivation-through-o-glcnacylation-to-promote-autophagosome-lysosome-fusion
#11
Xiaoyan Zhang, Leibin Wang, Behnam Lak, Jie Li, Eija Jokitalo, Yanzhuang Wang
The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway. However, how the Golgi responds to glucose deprivation is so far unknown. Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions. Glucose deprivation reduces GRASP55 O-GlcNAcylation. De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes...
April 23, 2018: Developmental Cell
https://www.readbyqxmd.com/read/29688431/generation-and-characterization-of-a-site-specific-antibody-for-sirt1-o-glcnacylated-at-serine-549
#12
Hui Shan, Jiahui Sun, Minghui Shi, Xue Liu, Zhu Shi, Wengong Yu, Yuchao Gu
O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) is a dynamic post-translational modification that modifies thousands of proteins. However, the roles and mechanisms of O-GlcNAcylation have been clarified in only a few proteins, and one of the main reasons for this is the lack of site-specific anti-O-GlcNAc antibodies. Recently, we found that SIRT1, which is an NAD+-dependent deacetylase, is O-GlcNAcylated at the serine 549 site (S549) and plays a cytoprotective role under stress. However, the mechanism underlying the roles of SIRT1 O-GlcNAcylation remains unclear...
April 24, 2018: Glycobiology
https://www.readbyqxmd.com/read/29681862/increased-o-glcnacylation-of-endothelial-nitric-oxide-synthase-compromises-the-anti-contractile-properties-of-perivascular-adipose-tissue-in-metabolic-syndrome
#13
Rafael M da Costa, Josiane F da Silva, Juliano V Alves, Thiago B Dias, Diane M Rassi, Luis V Garcia, Núbia de Souza Lobato, Rita C Tostes
Under physiological conditions, the perivascular adipose tissue (PVAT) negatively modulates vascular contractility. This property is lost in experimental and human obesity and in the metabolic syndrome, indicating that changes in PVAT function may contribute to vascular dysfunction associated with increased body weight and hyperglycemia. The O -linked β-N-acetylglucosamine ( O -GlcNAc) modification of proteins ( O -GlcNAcylation) is a unique posttranslational process that integrates glucose metabolism with intracellular protein activity...
2018: Frontiers in Physiology
https://www.readbyqxmd.com/read/29671171/new-use-for-cetsa-monitoring-innate-immune-receptor-stability-via-post-translational-modification-by-ogt
#14
Walter R Drake, Ching-Wen Hou, Natasha E Zachara, Catherine Leimkuhler Grimes
O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2). Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type. Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W...
April 18, 2018: Journal of Bioenergetics and Biomembranes
https://www.readbyqxmd.com/read/29622561/o-linked-%C3%AE-n-acetylglucosamine-modification-of-a20-enhances-the-inhibition-of-nf-%C3%AE%C2%BAb-nuclear-factor-%C3%AE%C2%BAb-activation-and-elicits-vascular-protection-after-acute-endoluminal-arterial-injury
#15
Dan Yao, Lijuan Xu, Oufan Xu, Rujun Li, Mingxing Chen, Hui Shen, Huajiang Zhu, Fengyi Zhang, Deshang Yao, Yiu-Fai Chen, Suzanne Oparil, Zhengang Zhang, Kaizheng Gong
OBJECTIVE: Recently, we have demonstrated that acute glucosamine-induced augmentation of protein O-linked β-N-acetylglucosamine (O-GlcNAc) levels inhibits inflammation in isolated vascular smooth muscle cells and neointimal formation in a rat model of carotid injury by interfering with NF-κB (nuclear factor-κB) signaling. However, the specific molecular target for O-GlcNAcylation that is responsible for glucosamine-induced vascular protection remains unclear. In this study, we test the hypothesis that increased A20 O-GlcNAcylation is required for glucosamine-mediated inhibition of inflammation and vascular protection...
April 5, 2018: Arteriosclerosis, Thrombosis, and Vascular Biology
https://www.readbyqxmd.com/read/29606577/the-o-glcnac-transferase-intellectual-disability-mutation-l254f-distorts-the-tpr-helix
#16
Mehmet Gundogdu, Salomé Llabrés, Andrii Gorelik, Andrew T Ferenbach, Ulrich Zachariae, Daan M F van Aalten
O-linked β-N-acetyl-D -glucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential post-translational modification that is abundant in the brain. Recently, OGT mutations have been associated with intellectual disability, although it is not understood how they affect OGT structure and function. Using a multi-disciplinary approach we show that the L254F OGT mutation leads to conformational changes of the tetratricopeptide repeats and reduced activity, revealing the molecular mechanisms contributing to pathogenesis...
March 23, 2018: Cell Chemical Biology
https://www.readbyqxmd.com/read/29594839/o-glcnac-in-cancer-an-oncometabolism-fueled-vicious-cycle
#17
REVIEW
John A Hanover, Weiping Chen, Michelle R Bond
Cancer cells exhibit unregulated growth, altered metabolism, enhanced metastatic potential and altered cell surface glycans. Fueled by oncometabolism and elevated uptake of glucose and glutamine, the hexosamine biosynthetic pathway (HBP) sustains glycosylation in the endomembrane system. In addition, the elevated pools of UDP-GlcNAc drives the O-GlcNAc modification of key targets in the cytoplasm, nucleus and mitochondrion. These targets include transcription factors, kinases, key cytoplasmic enzymes of intermediary metabolism, and electron transport chain complexes...
March 29, 2018: Journal of Bioenergetics and Biomembranes
https://www.readbyqxmd.com/read/29588363/effects-of-hypo-o-glcnacylation-on-drosophila-development
#18
Daniel N Mariappa, Andrew Ferenbach, Daan M F van Aalten
Post-translational modification of serine/threonine residues in nucleocytoplasmic proteins with N-acetylglucosamine (O -GlcNAcylation) is an essential regulatory mechanism in many cellular processes. In Drosophila , null mutants of the polycomb gene O-GlcNAc transferase (OGT, also known as super sex combs [ sxc ]) display homeotic phenotypes. To dissect the requirement for O -GlcNAc signaling in Drosophila development, we used CRISPR/Cas9 gene editing to generate rationally designed sxc catalytically hypomorphic or null point mutants...
March 27, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29577901/o-glcnac-site-mapping-of-liver-x-receptor-%C3%AE-and-o-glcnac-transferase
#19
Qiong Fan, Anders Moen, Jan Haug Anonsen, Christian Bindesbøll, Thomas Sæther, Cathrine Rein Carlson, Line M Grønning-Wang
The Liver X Receptor α (LXRα) belongs to the nuclear receptor superfamily and plays an essential role in regulating cholesterol, lipid and glucose metabolism and inflammatory responses. We have previously shown that LXRα is post-translationally modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) with increased transcriptional activity. Moreover, we showed that LXRα associates with O-GlcNAc transferase (OGT) in vitro and in vivo in mouse liver. In this study, we report that human LXRα is O-GlcNAc modified in its N-terminal domain (NTD) by identifying a specific O-GlcNAc site S49 and a novel O-GlcNAc modified peptide20 LWKPGAQDASSQAQGGSSCILRE42 ...
March 22, 2018: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29562282/aanl-agrocybe-aegerita-lectin-2-is-a-new-facile-tool-to-probe-for-o-glcnacylation
#20
Wei Liu, Guanghui Han, Yalin Yin, Shuai Jiang, Guojun Yu, Qing Yang, Wenhui Yu, Xiangdong Ye, Yanting Su, Yajun Yang, Gerald W Hart, Hui Sun
O-linked N-acetylglucosamine (O-GlcNAcylation) is an important post-translational modification on serine or threonine of proteins, mainly observed in nucleus or cytoplasm. O-GlcNAcylation regulates many cell processes, including transcription, cell cycle, neural development, and nascent polypeptide chains stabilization. However, the facile identification of O-GlcNAc is a major bottleneck in O-GlcNAcylation research. Herein, we report that a lectin, AANL (Agrocybe aegerita GlcNAc specific lectin), also reported as AAL2, can be used as a powerful probe for O-GlcNAc identification...
March 19, 2018: Glycobiology
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