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https://www.readbyqxmd.com/read/28642969/diverse-metabolic-effects-of-o-glcnacylation-in-the-pancreas-but-limited-effects-in-insulin-sensitive-organs-in-mice
#1
Shogo Ida, Katsutaro Morino, Osamu Sekine, Natsuko Ohashi, Shinji Kume, Tokuhiro Chano, Kanako Iwasaki, Norio Harada, Nobuya Inagaki, Satoshi Ugi, Hiroshi Maegawa
AIMS/HYPOTHESIS: O-GlcNAcylation is characterised by the addition of N-acetylglucosamine to various proteins by O-GlcNAc transferase (OGT) and serves in sensing intracellular nutrients by modulating various cellular processes. Although it has been speculated that O-GlcNAcylation is associated with glucose metabolism, its exact role in whole body glucose metabolism has not been fully elucidated. Here, we investigated whether loss of O-GlcNAcylation globally and in specific organs affected glucose metabolism in mammals under physiological conditions...
June 22, 2017: Diabetologia
https://www.readbyqxmd.com/read/28637651/pivotal-role-of-o-glcnac-modification-in-cold-induced-thermogenesis-by-brown-adipose-tissue-through-mitochondrial-biogenesis
#2
Natsuko Ohashi, Katsutaro Morino, Shogo Ida, Osamu Sekine, Mengistu Lemecha, Shinji Kume, Shi-Young Park, Cheol Soo Choi, Satoshi Ugi, Hiroshi Maegawa
Adipose tissues considerably influence metabolic homeostasis, and both white (WAT) and brown adipose tissue (BAT) play significant roles in lipid and glucose metabolism. O-GlcNAc modification is characterized by the addition of N-acetylglucosamine to various proteins by O-GlcNAc transferase (Ogt), subsequently modulating various cellular processes. However, little is known about the role of O-GlcNAc modification in adipose tissues. Here, we report the critical role of O-GlcNAc modification in cold-induced thermogenesis...
June 21, 2017: Diabetes
https://www.readbyqxmd.com/read/28628081/o-glcnacylation-of-fumarase-maintains-tumour-growth-under-glucose-deficiency
#3
Ting Wang, Qiujing Yu, Jingjie Li, Bin Hu, Qin Zhao, Chunmin Ma, Wenhua Huang, Lingang Zhuo, Houqin Fang, Lujian Liao, Y Eugene Chin, Yuhui Jiang
Chromatin-associated fumarase (FH) affects histone methylation via its metabolic activity. However, whether this effect is involved in gene transcription remains to be clarified. In this study, we show that under glucose deprivation conditions, AMPK phosphorylates FH at Ser75, which in turn forms a complex with ATF2 and participates in promoter activation. FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest...
June 19, 2017: Nature Cell Biology
https://www.readbyqxmd.com/read/28627871/the-sulfur-linked-analog-of-o-glcnac-s-glcnac-is-an-enzymatically-stable-and-a-reasonable-structural-surrogate-for-o-glcnac-at-the-peptide-and-protein-levels
#4
Cesar A De Leon, Paul M Levine, Timothy W Craven, Matthew R Pratt
Synthetic proteins bearing site-specific posttranslational modifications have revolutionized our understanding of their biological functions in vitro and in vivo. One such modification, O-GlcNAcylation, is the dynamic addition of β-N-acetyl glucosamine to the side-chains of serine and threonine residues of proteins. Yet, our understanding of the site-specific impact of O-GlcNAcylation remains difficult to evaluate in vivo due to the potential for enzymatic removal by endogenous O-GlcNAcase (OGA). Thioglycosides are generally perceived to be enzymatically stable structural mimics of O-GlcNAc; however, in vitro experiments small-molecule GlcNAc thioglycosides have demonstrated that OGA can hydrolyze these linkages, indicating thatS-linked-β-N-acetyl glucosamine (S-GlcNAc) on peptides or proteins may not be completely stable...
June 19, 2017: Biochemistry
https://www.readbyqxmd.com/read/28625484/nuclear-factor-erythroid-2-related-transcription-factor-1-nrf1-is-regulated-by-o-glcnac-transferase
#5
Jeong Woo Han, Joshua L Valdez, Daniel V Ho, Candy S Lee, Hyun Min Kim, Xiaorong Wang, Lan Huang, Jefferson Y Chan
The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis. Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1. Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1. Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability...
June 15, 2017: Free Radical Biology & Medicine
https://www.readbyqxmd.com/read/28624365/o-glcnacylation-of-amyloid-%C3%AE-precursor-protein-at-threonine-576-residue-regulates-trafficking-and-processing
#6
Yoon Sun Chun, Oh-Hoon Kwon, Sungkwon Chung
The pathological hallmark of Alzheimer's disease (AD) is associated with the accumulation of amyloid-β (Aβ) derived from proteolytic processing of amyloid-β precursor protein (APP). APP undergoes post-translational modification including N- and O-glycosylation. O-GlcNAcylation is a novel type of O-glycosylation, mediated by O-GlcNAc transferase attaching O-β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of the target proteins. O-GlcNAc is removed by O-GlcNAcase. We have previously reported that increasing O-GlcNAcylated APP using the O-GlcNAcase inhibitor, PUGNAc, increases its trafficking rate to the plasma membrane and decreases its endocytosis rate, resulting in decreased Aβ production...
June 14, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28609614/direct-monitoring-of-protein-o-glcnacylation-by-high-resolution-native-mass-spectrometry
#7
Aneika C Leney, Karim Rafie, Daan M F Van Aalten, Albert J R Heck
O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications. Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism and cell division. Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry and monitor O-GlcNAcylation kinetics. Here we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates; CK2α and TAB1, without the need for radioactive labelling or chemoenzymatic tagging using large mass tags...
June 13, 2017: ACS Chemical Biology
https://www.readbyqxmd.com/read/28604694/a-mutant-o-glcnacase-enriches-drosophila-developmental-regulators
#8
Nithya Selvan, Ritchie Williamson, Daniel Mariappa, David G Campbell, Robert Gourlay, Andrew T Ferenbach, Tonia Aristotelous, Iva Hopkins-Navratilova, Matthias Trost, Daan M F van Aalten
Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA). Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis. The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage...
June 12, 2017: Nature Chemical Biology
https://www.readbyqxmd.com/read/28595377/characterization-of-tools-to-detect-and-enrich-human-and-mouse-o-glcnacase
#9
Jennifer A Groves, Natasha E Zachara
O-linked β-N-acetylglucosamine (O-GlcNAc) is an essential regulatory post-translational modification of thousands of nuclear, cytoplasmic, and mitochondrial proteins. O-GlcNAc is dynamically added and removed from proteins by the O-GlcNAc transferase and the O-GlcNAcase (OGA), respectively. Dysregulation of O-GlcNAc-cycling is implicated in the etiology of numerous diseases including tumorigenesis, metabolic dysfunction, and neurodegeneration. To facilitate studies focused on the role of O-GlcNAc and OGA in disease, we sought to identify commercially available antibodies that enable the enrichment of full-length OGA from lysates of mouse and human origin...
June 8, 2017: Glycobiology
https://www.readbyqxmd.com/read/28584052/mutations-in-n-acetylglucosamine-o-glcnac-transferase-in-patients-with-x-linked-intellectual-disability
#10
Anke P Willems, Mehmet Gundogdu, Marlies J E Kempers, Jacques C Giltay, Rolph Pfundt, Martin Elferink, Bettina F Loza, Joris Fuijkschot, Andrew T Ferenbach, Koen L I van Gassen, Daan M F van Aalten, Dirk J Lefeber
N-acetylglucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential and dynamic post-translational modification. The O-GlcNAc modification is present on numerous nuclear and cytosolic proteins and has been implicated in essential cellular functions such as signalling and gene expression. Accordingly, altered levels of protein O-GlcNAcylation have been associated with developmental defects and neurodegeneration. However, mutations in the OGT gene have not yet been functionally confirmed in humans...
June 5, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28582574/a-genetic-model-to-study-increased-hexosamine-biosynthetic-flux
#11
Sarah E Hugo, Amnon Schlegel
Recently, we identified harvest moon (hmn), a fully penetrant and expressive recessive zebrafish mutant with hepatic steatosis. Larvae showed increased triacylglycerol in the absence of other obvious defects. When we attempted to raise these otherwise normal appearing mutants to adulthood, we observed a developmental arrest and death in the early juvenile period. Here we report the positional cloning of the hmn locus and characterization of the defects caused by the mutation. Using bulk segregant analysis, fine mapping, and immunoblot assays we find that hmn mutants harbor a point mutation in an invariant residue within the sugar isomerase 1 domain of the gene encoding the rate-limiting enzyme of the hexosamine biosynthetic pathway (HBP) Glutamine-fructose-6-phosphate transamidase (Gfpt1)...
June 5, 2017: Endocrinology
https://www.readbyqxmd.com/read/28571750/measuring-o-glcnac-cleavage-by-oga-and-cell-lysates-on-a-peptide-microarray
#12
Suhela Sharif, Jie Shi, Mostafa Bourakba, Rob Ruijtenbeek, Roland J Pieters
O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins. In addition, O-GlcNAcylated proteins can be phosphorylated, which suggests the possibility for crosstalk between O-GlcNAcylation and phosphorylation. Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis...
May 29, 2017: Analytical Biochemistry
https://www.readbyqxmd.com/read/28541657/chemical-modulation-of-protein-o-glcnacylation-via-ogt-inhibition-promotes-human-neural-cell-differentiation
#13
Lissette M Andres, Ian W Blong, Angela C Evans, Neil G Rumachik, Teppei Yamaguchi, Nam D Pham, Pamela Thompson, Jennifer J Kohler, Carolyn R Bertozzi
The enzymes that determine protein O-GlcNAcylation, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), act on key transcriptional and epigenetic regulators, and both are abundantly expressed in the brain. However, little is known about how alterations in O-GlcNAc cycling affect human embryonic stem cell (hESC) neural differentiation. Here, we studied the effects of perturbing O-GlcNAcylation during neural induction of hESCs using the metabolic inhibitor of OGT, peracetylated 5-thio-N-acetylglucosamine (Ac4-5SGlcNAc)...
June 19, 2017: ACS Chemical Biology
https://www.readbyqxmd.com/read/28536142/augmented-tme-o-glcnacylation-promotes-tumor-proliferation-through-the-inhibition-of-p38-mapk
#14
Kazumasa Moriwaki, Michio Asahi
O-GlcNAcylation is a dynamic O-linked glycosylation event that plays a crucial role in regulating cellular signaling. Recent studies indicate that increased O-GlcNAcylation is a general feature in cancer and contributes to various cancer phenotypes, including cell proliferation, survival, invasion, metastasis, and energy metabolism. However, the role of O-GlcNAcylation in the tumor microenvironment (TME) is not fully elucidated. Here, B16 melanoma cells were subcutaneously transplanted into O-GlcNAc transferase transgenic (Ogt-Tg) mice exhibiting elevated O-GlcNAcylation to examine the effect of O-GlcNAcylation in the TME on tumor progression...
May 23, 2017: Molecular Cancer Research: MCR
https://www.readbyqxmd.com/read/28528544/the-new-chemical-reporter-6-alkynyl-6-deoxy-glcnac-reveals-o-glcnac-modification-of-the-apoptotic-caspases-that-can-block-the-cleavage-activation-of-caspase-8
#15
Kelly N Chuh, Anna R Batt, Balyn W Zaro, Narek Darabedian, Nicholas P Marotta, Caroline K Brennan, Arya Amirhekmat, Matthew R Pratt
O-GlcNAc modification (O-GlcNAcylation) is required for survival in mammalian cells. Genetic and biochemical experiments have found that increased modification inhibits apoptosis in tissues and cell culture and that lowering O-GlcNAcylation induces cell death. However, the molecular mechanisms by which O-GlcNAcylation might inhibit apoptosis are still being elucidated. Here, we first synthesize a new metabolic chemical reporter, 6-Alkynyl-6-deoxy-GlcNAc (6AlkGlcNAc), for the identification of O-GlcNAc-modified proteins...
May 31, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28526214/high-glucose-environment-induced-intracellular-o-glcnac-glycosylation-and-reduced-galectin-7-expression-in-keratinocytes-implications-on-impaired-diabetic-wound-healing
#16
Shu-Mei Huang, Ching-Shuang Wu, Min-Hsi Chiu, Hui-Jun Yang, Gwo-Shing Chen, Cheng-Che E Lan
BACKGROUND: Diabetes is an important global health issue due to its increasing prevalence and association with various complications. Impaired wound healing is a serious complication associated with diabetes that frequently results in infection and amputation. Galectin-7 (Gal-7) has been reported to play an important role during skin wound healing. Previously, we had demonstrated that high glucose environment alters physiologic functions of keratinocytes and contributes to impaired wound healing in diabetic condition...
April 30, 2017: Journal of Dermatological Science
https://www.readbyqxmd.com/read/28521765/inhibition-of-o-glcnacase-leads-to-elevation-of-o-glcnac-tau-and-reduction-of-tauopathy-and-cerebrospinal-fluid-tau-in-rtg4510-mice
#17
Nicholas B Hastings, Xiaohai Wang, Lixin Song, Brent D Butts, Diane Grotz, Richard Hargreaves, J Fred Hess, Kwok-Lam Karen Hong, Cathy Ruey-Ruey Huang, Lynn Hyde, Maureen Laverty, Julie Lee, Diane Levitan, Sherry X Lu, Maureen Maguire, Veeravan Mahadomrongkul, Ernest J McEachern, Xuesong Ouyang, Thomas W Rosahl, Harold Selnick, Michaela Stanton, Giuseppe Terracina, David J Vocadlo, Ganfeng Wang, Joseph L Duffy, Eric M Parker, Lili Zhang
BACKGROUND: Hyperphosphorylation of microtubule-associated protein tau is a distinct feature of neurofibrillary tangles (NFTs) that are the hallmark of neurodegenerative tauopathies. O-GlcNAcylation is a lesser known post-translational modification of tau that involves the addition of N-acetylglucosamine onto serine and threonine residues. Inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc modification, has been shown to reduce tau pathology in several transgenic models...
May 18, 2017: Molecular Neurodegeneration
https://www.readbyqxmd.com/read/28515473/placental-o-glcnac-transferase-expression-and-interactions-with-the-glucocorticoid-receptor-are-sex-specific-and-regulated-by-maternal-corticosterone-exposure-in-mice
#18
Marie Pantaleon, Sarah E Steane, Kathryn McMahon, James S M Cuffe, Karen M Moritz
Maternal stress programs offspring disease in a sexually dimorphic manner with males often more adversely affected. Previous studies of maternal glucocorticoid exposure suggest male vulnerability may derive from placental alterations. The hexosamine signalling pathway and O-linked glycosylation (O-GlcNAcylation) are part of an essential adaptive survival response in healthy cells. The key enzyme involved is O-linked-N-acetylglucosamine transferase (OGT), a gene recently identified as a sex-specific placental biomarker of maternal stress...
May 17, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28514044/specific-identification-of-glycoproteins-bearing-the-tn-antigen-in-human-cells
#19
Jiangnan Zheng, Haopeng Xiao, Ronghu Wu
Glycoproteins contain a wealth of valuable information regarding the development and disease status of cells. In cancer cells, some glycans (such as the Tn antigen) are highly up-regulated, but this remains largely unknown for glycoproteins with a particular glycan. Herein, an innovative method combining enzymatic and chemical reactions was first designed to enrich glycoproteins with the Tn antigen. Using synthetic glycopeptides with O-GalNAc (the Tn antigen) or O-GlcNAc, we demonstrated that the method is selective for glycopeptides with O-GalNAc and can distinguish between these two modifications...
June 12, 2017: Angewandte Chemie
https://www.readbyqxmd.com/read/28510447/synthesis-of-a-highly-azide-reactive-and-thermosensitive-biofunctional-reagent-for-efficient-enrichment-and-large-scale-identification-of-o-glcnac-proteins-by-mass-spectrometry
#20
Wanjun Zhang, Tong Liu, Hangyan Dong, Haihong Bai, Fang Tian, Zhaomei Shi, Mingli Chen, Jianhua Wang, Weijie Qin, Xiaohong Qian
O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous post-translational modification of proteins in eukaryotic cells. Despite their low abundance, O-GlcNAc-modified proteins play many important roles in regulating gene expression, signal transduction, and cell cycle. Aberrant O-GlcNAc proteins are correlated with many major human diseases, such as Alzheimer's disease, diabetes, and cancer. Because of the extremely low stoichiometry of O-GlcNAc proteins, enrichment is required before mass spectrometry analysis for large-scale identification and in-depth understanding of their cellular function...
June 6, 2017: Analytical Chemistry
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