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Karin Säljö, Angela Barone, Dzeneta Vizlin-Hodzic, Bengt R Johansson, Michael E Breimer, Keiko Funa, Susann Teneberg
High expectations are held for human-induced pluripotent stem cells (hiPSC) since they are established from autologous tissues thus overcoming the risk of allogeneic immune rejection when used in regenerative medicine. However, little is known regarding the cell-surface carbohydrate antigen profile of hiPSC compared with human embryonic stem cells (hESC). Here, glycosphingolipids were isolated from an adipocyte-derived hiPSC line, and hiPSC and hESC glycosphingolipids were compared by concurrent characterization by binding assays with carbohydrate-recognizing ligands and mass spectrometry...
December 8, 2016: Glycobiology
Ken Hanzawa, Noriko Suzuki, Shunji Natsuka
Zebrafish is a model organism suitable for studying vertebrate development. We analyzed the N-glycan structures of zebrafish embryos and their alterations during zebrafish embryogenesis to obtain basic data for studying the roles of N-glycosylation. Multiple modes of high-performance liquid chromatography and multistage mass spectrometry were used for structural analysis of N-glycans. The N-glycans from deyolked embryos at 36 hours postfertilization, a mid-pharyngula stage, contained relatively higher amounts of complex- and hybrid-type glycans with LacNAc (Galβ1-4GlcNAc) and/or sialyl LacNAc without additional β1,4-Gal, which are commonly found in mammalian tissues, as well as abundant oligomannose-type glycans...
December 8, 2016: Glycobiology
María Florencia Festari, Felipe Trajtenberg, Nora Berois, Sergio Pantano, Leslie Revoredo, Yun Kong, Patricia Solari-Saquieres, Yoshiki Narimatsu, Teresa Freire, Sylvie Bay, Carlos Robello, Jean Bénard, Thomas A Gerken, Henrik Clausen, Eduardo Osinaga
Polypeptide GalNAc-transferases (GalNAc-Ts) constitute a family of 20 human glycosyltransferases (comprising 9 subfamilies), which initiate mucin-type O-glycosylation. The O-glycoproteome is thought to be differentially regulated via the different substrate specificities and expression patterns of each GalNAc-T isoforms. Here, we present a comprehensive in vitro analysis of the peptide substrate specificity of GalNAc-T13, showing that it essentially overlaps with the ubiquitous expressed GalNAc-T1 isoform found in the same subfamily as T13...
November 22, 2016: Glycobiology
M Osman Sheikh, Stephanie M Halmo, Sneha Patel, Dustin Middleton, Hideyuki Takeuchi, Christopher M Schafer, Christopher M West, Robert S Haltiwanger, Fikri Y Avci, Kelley W Moremen, Lance Wells
Determining the correct enzymatic activity of putative glycosyltransferases (GTs) can be challenging as these enzymes can utilize multiple donor and acceptor substrates. Upon initial determination of the donor-sugar nucleotide(s), a GT utilizes various acceptor molecules that can then be tested. Here, we describe a quick method to screen sugar-nucleotide donor specificities of GTs utilizing a sensitive, nonradioactive, commercially available bioluminescent uridine diphosphate detection kit. This in vitro method allowed us to validate the sugar-nucleotide donor-substrate specificities of recombinantly expressed human, bovine, bacterial and protozoan GTs...
November 22, 2016: Glycobiology
(no author information available yet)
No abstract text is available yet for this article.
October 31, 2016: Glycobiology
S Górska, P Hermanova, J Ciekot, M Schwarzer, D Srutkova, E Brzozowska, H Kozakova, A Gamian
No abstract text is available yet for this article.
October 28, 2016: Glycobiology
Melissa M Lee-Sundlov, David J Ashline, Andrew J Hanneman, Renata Grozovsky, Vernon N Reinhold, Karin M Hoffmeister, Joseph Ty Lau
Glycosyltransferases, usually residing within the intracellular secretory apparatus, also circulate in the blood. Many of these blood-borne glycosyltransferases are associated with pathological states, including malignancies and inflammatory conditions. Despite the potential for dynamic modifications of glycans on distal cell surfaces and in the extracellular milieu, the glycan-modifying activities present in systemic circulation have not been systematically examined. Here, we describe an evaluation of blood-borne sialyl-, galactosyl- and fucosyltransferase activities that act upon the four common terminal glycan precursor motifs, GlcNAc monomer, Gal(β3)GlcNAc, Gal(β4)GlcNAc and Gal(β3)GalNAc, to produce more complex glycan structures...
October 26, 2016: Glycobiology
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
Yanlei Yu, Yin Chen, Paiyz Mikael, Fuming Zhang, Apryll M Stalcup, Rebecca German, Francois Gould, Jocelyn Ohlemacher, Hong Zhang, Robert J Linhardt
Heparin, a member of a family of molecules called glycosaminoglycans, is biosynthesized in mucosal mast cells. This important anticoagulant polysaccharide is primarily produced by extraction of the mast cell-rich intestinal mucosa of hogs. There is concern about our continued ability to supply sufficient heparin to support the worldwide growth of advanced medical procedures from the static population of adult hogs used as food animals. While the intestinal mucosa of adult pigs is rich in anticoagulant heparin (containing a few hundred milligrams per animal), little is known about how the content of heparin changes with animal age...
October 15, 2016: Glycobiology
Niël van Wyk, Michel Drancourt, Bernard Henrissat, Laurent Kremer
Glycoside hydrolases (GHs) are enzymes that catalyze the hydrolysis of glycosidic bonds in glycoconjugates, oligo- and polysaccharides. A classification of these enzymes based on conserved sequence and structure motifs supported by the Carbohydrate active enzyme (CAZy) database has proven useful in the systematic groupings of similar enzymes into families.The human pathogen Mycobacterium tuberculosis employs 30 GHs to perform a variety of different functions which can be divided into four broad categories: α-glucan metabolism, peptidoglycan remodelling, β-glycan hydrolysis and α-demannosylation...
October 3, 2016: Glycobiology
Pablo H H Lopez, Susan Aja, Kazuhiro Aoki, Marcus M Seldin, Xia Lei, Gabriele V Ronnett, G William Wong, Ronald L Schnaar
Sialyltransferases are a family of 20 gene products in mice and humans that transfer sialic acid from its activated precursor, CMP-sialic acid, to the terminus of glycoprotein and glycolipid acceptors. ST3Gal-II (coded by the St3gal2 gene) transfers sialic acid preferentially to the 3-position of galactose on the Galβ1-3GalNAc terminus of gangliosides GM1 and GD1b to synthesize GD1a and GT1b respectively. Mice with a targeted disruption of St3gal2 unexpectedly displayed late-onset obesity and insulin resistance...
September 28, 2016: Glycobiology
ThirumalaiSelvi Ulaganathan, Rong Shi, Deqiang Yao, Ruo-Xu Gu, Marie-Line Garron, Maia Cherney, D Peter Tieleman, Eric Sterner, Guoyun Li, Lingyun Li, Robert J Linhardt, Miroslaw Cygler
Glycosaminoglycans (GAGs) are linear polysaccharides comprised of disaccharide repeat units, a hexuronic acid, glucuronic acid or iduronic acid, linked to a hexosamine, N-acetylglucosamine (GlcNAc) or N-acetylgalactosamine. GAGs undergo further modification such as epimerization and sulfation. These polysaccharides are abundant in the extracellular matrix and connective tissues. GAGs function in stabilization of the fibrillar extracellular matrix, control of hydration, regulation of tissue, organism development by controlling cell cycle, cell behavior and differentiation...
September 12, 2016: Glycobiology
(no author information available yet)
No abstract text is available yet for this article.
December 2016: Glycobiology
(no author information available yet)
No abstract text is available yet for this article.
December 2016: Glycobiology
Viktoria Dotz, Rüdiger Adam, Günter Lochnit, Horst Schroten, Clemens Kunz
Beneficial effects have been proposed for human milk oligosaccharides (HMO), as deduced from in vitro and animal studies. To date, in vivo evidence of the link between certain oligosaccharide structures in milk and their consumption by infant gut microbiota is still missing, although likely. Whereas many studies have described HMO patterns in human milk from larger cohorts, data on the excretion of HMO and possible metabolites produced in the infant gut are still very limited. From smaller-scale studies, an age-dependency according to infant gut maturation and microbiota adaptation has previously been hypothesized...
December 2016: Glycobiology
Roger A Kroes, Joseph R Moskal
The mechanism of transcriptional silencing of ST6Gal1 in gliomas has not yet been elucidated. Multiple independent promoters govern the expression of the ST6Gal I gene. Here, we investigated whether epigenetic abnormalities involving DNA methylation affect ST6Gal1 expression. Transcript-specific qRT-PCR following exposure of glioma cell lines to 5-aza-2'-deoxycytidine (5-aza-dC), a DNA methyltransferase inhibitor, resulted in the re-expression of the normally quiescent ST6Gal1 mRNA driven exclusively by the P3 promoter sequence...
December 2016: Glycobiology
Kei-Ichiro Inamori, Aaron M Beedle, Daniel Beltrán-Valero de Bernabé, Michael E Wright, Kevin P Campbell
Both LARGE1 (formerly LARGE) and its paralog LARGE2 are bifunctional glycosyltransferases with xylosy- and glucuronyltransferase activities, and are capable of synthesizing polymers composed of a repeating disaccharide [-3Xylα1,3GlcAβ1-]. Post-translational modification of the O-mannosyl glycan of α-dystroglycan (α-DG) with the polysaccharide is essential for it to act as a receptor for ligands in the extracellular matrix (ECM), and both LARGE paralogs contribute to the modification in vivo. LARGE1 and LARGE2 have different tissue distribution profiles and enzymatic properties; however, the functional difference of the homologs remains to be determined, and α-DG is the only known substrate for the modification by LARGE1 or LARGE2...
December 2016: Glycobiology
Kristin E Haugstad, Soosan Hadjialirezaei, Bjørn T Stokke, C Fred Brewer, Thomas A Gerken, Joy Burchell, Gianfranco Picco, Marit Sletmoen
The molecular mechanism(s) underlying the enhanced self-interactions of mucins possessing the Tn (GalNAcα1-Ser/Thr) or STn (NeuNAcα2-6GalNAcα1-Ser/Thr) cancer markers were investigated using optical tweezers (OT). The mucins examined included modified porcine submaxillary mucin containing the Tn epitope (Tn-PSM), ovine submaxillary mucin with the STn epitope (STn-OSM), and recombinant MUC1 analogs with either the Tn and STn epitope. OT experiments in which the mucins were immobilized onto polystyrene beads revealed identical self-interaction characteristics for all mucins...
December 2016: Glycobiology
Carmen Jiménez-Castells, Rhiannon Stanton, Shi Yan, Paul Kosma, Iain Bh Wilson
Glycan arrays have become a technique of choice to screen glycan-protein interactions in a high-throughput manner with high sensitivity and low sample consumption. Here, the synthesis of a new multifunctional fluorescent linker for glycan labeling via aminoxy ligation and immobilization is described; the linker features a fluorescent naphthalene group suitable for highly sensitive high-performance liquid chromatography-based purification and an azido- or amino-modified pentanoyl moiety for the immobilization onto solid supports...
December 2016: Glycobiology
Juan M Romero, Madia Trujillo, Darío A Estrin, Gabriel A Rabinovich, Santiago Di Lella
Endogenous lectins can control critical biological responses, including cell communication, signaling, angiogenesis and immunity by decoding glycan-containing information on a variety of cellular receptors and the extracellular matrix. Galectin-1 (Gal-1), a prototype member of the galectin family, displays only one carbohydrate recognition domain and occurs in a subtle homodimerization equilibrium at physiologic concentrations. Such equilibrium critically governs the function of this lectin signaling by allowing tunable interactions with a preferential set of glycosylated receptors...
December 2016: Glycobiology
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