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Sialic Acid

Christina E Galuska, Jan A Dambon, Andrea Kühnle, Kim F Bornhöfft, Gerlinde Prem, Kristina Zlatina, Thomas Lütteke, Sebastian P Galuska
Neutrophils are involved in numerous immunological events. One mechanism of neutrophils to combat pathogens is the formation of neutrophil extracellular traps (NETs). Thereby, neutrophils use DNA fibers to form a meshwork of DNA and histones as well as several antimicrobial components to trap and kill invaders. However, the formation of NETs can lead to pathological conditions triggering among other things (e.g., sepsis or acute lung failure), which is mainly a consequence of the cytotoxic characteristics of accumulated extracellular histones...
2017: Frontiers in Immunology
Liping Li, Chenxue Qu, Xuelian Wu, Juhua Dai, Yao Lu, Yan Gong, Ran You, Yaqi Liu
Coronary heart disease (CHD) and diabetes mellitus (DM) have high reactivity of platelets and an increased risk of thrombosis. Platelet glycosylation is closely related to platelet function and survival. However, the alteration of platelet glycosylation in CHD and T2DM still remains unknown. Platelet samples were obtained from 55 healthy controls and 102 patients, including 33 CHD, 30 T2DM and 39 CHD complicated with T2DM (CHD + T2DM). Platelet glycosylation was detected using eight-lectin based assay by flow cytometry...
October 14, 2017: Journal of Thrombosis and Thrombolysis
Montserrat Mancera-Arteu, Estela Giménez, José Barbosa, Rosa Peracaula, Victòria Sanz-Nebot
In this work, a μZIC-HILIC-MS/MS methodology was established in negative ion mode for the characterization of glycan isomers. The possibility to separate the glycan isomers by the μZIC-HILIC strategy coupled to a high resolution tandem mass spectrometry detection permitted us to obtain valuable information about each glycan structure. The most important diagnostic ion fragments previously described to characterize structural features of glycans, were evaluated in this study using hAGP as model glycoprotein...
October 23, 2017: Analytica Chimica Acta
Fumi Ota, Yasuhiko Kizuka, Miyako Nakano, Yoshiki Yamaguchi, Shinobu Kitazume, Tomomi Ookawara, Naoyuki Taniguchi
Extracellular superoxide dismutase (EC-SOD, SOD3) protects tissues against oxidative damage by detoxifying superoxide anions, particularly in the lungs and cardiovascular system. EC-SOD undergoes several posttranslational modifications including N-glycosylation and proteolytic cleavage. While the roles of proteolytic cleavage have been well studied, the structure and function of EC-SOD N-glycans are poorly understood. Here we analyzed glycan structures on native EC-SOD purified from human sera, and identified sialylated biantennary structures...
October 4, 2017: Glycobiology
A Matsumoto, A J Stephenson-Brown, T Khan, T Miyazawa, H Cabral, K Kataoka, Y Miyahara
Boronic acids are well known for their ability to reversibly interact with the diol groups found in sugars and glycoproteins. However, they are generally indiscriminate in their binding. Herein we describe the discovery of a group of heterocyclic boronic acids demonstrating unusually high affinity and selectivity for sialic acids (SAs or N-acetylneuraminic acid), which are sugar residues that are intimately linked with tumor growth and cancer progression. Remarkably, these interactions strengthen under the weakly acidic pH conditions associated with a hypoxic tumoral microenvironment...
September 1, 2017: Chemical Science
Christa M Snyder, Xiaomei Zhou, Jonathan A Karty, Bryan R Fonslow, Milos V Novotny, Stephen C Jacobson
Through direct coupling of capillary electrophoresis (CE) to mass spectrometry (MS) with a sheathless interface, we have identified 77 potential N-glycan structures derived from human serum. We confirmed the presence of N-glycans previously identified by indirect methods, e.g., electrophoretic mobility standards, obtained 31 new N-glycan structures not identified in our prior work, differentiated co-migrating structures, and determined specific linkages on isomers featuring sialic acids. Serum N-glycans were cleaved from proteins, neutralized via methylamidation, and labeled with the fluorescent tag 8-aminopyrene-1,3,6-trisulfonic acid, which renders the glycan fluorescent and provides a -3 charge for electrophoresis and negative-mode MS detection...
September 9, 2017: Journal of Chromatography. A
Seonghun Kim
Mucin-type O-glycans are involved in biological functions on the cell surface as well as the glycoproteins and can also be used as specific carbohydrate biomarkers of many diseases. In this study, we purified a novel core 1 O-linked glycan specific lectin, Hericium erinaceus lecin (HeL), from the fruiting body of the mushroom Hericium erinaceus, which is known as the natural source for a sialic acid-binding lectin. Upon optimization of the purification conditions, a sequence of ion exchange, affinity, ion exchange, and size-exclusion chromatography resulted in the highest yield and best quality of lectin without protease activity...
October 6, 2017: International Journal of Biological Macromolecules
S V Kononova
Formation of appropriate gut microbiota is essential for human health. The first two years of life is the critical period for this process. Selection of mutualistic microorganisms of the intestinal microbiota is controlled by the FUT2 and FUT3 genes that encode fucosyltransferases, enzymes responsible for the synthesis of fucosylated glycan structures of mucins and milk oligosaccharides. In this review, the mechanisms of the selection and maintenance of intestinal microorganisms that involve fucosylated oligosaccharides of breast milk and mucins of the newborn's intestine are described...
September 2017: Biochemistry. Biokhimii︠a︡
Keita Nishiyama, Yuji Yamamoto, Makoto Sugiyama, Takashi Takaki, Tadasu Urashima, Satoru Fukiya, Atsushi Yokota, Nobuhiko Okada, Takao Mukai
Bifidobacterium is a natural inhabitant of the human gastrointestinal (GI) tract. We studied the role of the extracellular sialidase (SiaBb2, 835 amino acids [aa]) from Bifidobacterium bifidum ATCC 15696 in mucosal surface adhesion and carbohydrate catabolism. Human milk oligosaccharides (HMOs) or porcine mucin oligosaccharides as the sole carbon source enhanced B. bifidum growth. This was impaired in a B. bifidum ATCC 15696 strain harboring a mutation in the siabb2 gene. Mutant cells in early to late exponential growth phase also showed decreased adhesion to human epithelial cells and porcine mucin relative to the wild-type strain...
October 3, 2017: MBio
Volkan Seyrantepe, Secil Akyildiz Demir, Zehra Kevser Timur, Johanna Von Gerichten, Christian Marsching, Esra Erdemli, Emin Oztas, Kohta Takahashi, Kazunori Yamaguchi, Nurselin Ates, Buket Dönmez Demir, Turgay Dalkara, Katrin Erich, Carsten Hopf, Roger Sandhoff, Taeko Miyagi
Tay-Sachs disease is a severe lysosomal storage disorder caused by mutations in Hexa, the gene that encodes for the α subunit of lysosomal β-hexosaminidase A (HEXA), which converts GM2 to GM3 ganglioside. Unexpectedly, Hexa(-/-) mice have a normal lifespan and show no obvious neurological impairment until at least one year of age. These mice catabolize stored GM2 ganglioside using sialidase(s) to remove sialic acid and form the glycolipid GA2, which is further processed by β-hexosaminidase B. Therefore, the presence of the sialidase (s) allows the consequences of the Hexa defect to be bypassed...
September 30, 2017: Experimental Neurology
Henrik Wegener, Álvaro Mallagaray, Tobias Schöne, Thomas Peters, Julia Lockhauserbäumer, Hao Yan, Charlotte Uetrecht, Grant Hansman, Stefan Taube
Human noroviruses (HuNoV), members of the family Caliciviridae are the major cause of acute viral gastroenteritis worldwide. Successful infection is linked to the ability of the protruding (P) domain of the viral capsid to bind histo-blood group antigens (HBGA). Binding to gangliosides plays a major role for many non-human calici- and noroviruses. Increasing evidence points to a broader role of sialylated carbohydrates such as gangliosides in norovirus infection. Here, we compare HBGA and ganglioside binding of a GII...
September 4, 2017: Glycobiology
Brian J McMorran, M Carrie Miceli, Linda G Baum
Our understanding of muscle glycosylation to date has derived from studies in mouse models and a limited number of human lectin histochemistry studies. As various therapeutic approaches aimed at treating patients with muscular dystrophies are being translated from rodent models to human, it is critical to better understand human muscle glycosylation and relevant disease-specific differences between healthy and dystrophic muscle. Here, we report the first quantitative characterization of human muscle glycosylation, and identify differentiation- and disease-specific differences in human muscle glycosylation...
August 23, 2017: Glycobiology
Kyle J Bednar, Elena Shanina, Romain Ballet, Edward P Connors, Shiteng Duan, Joana Juan, Britni M Arlian, Michael D Kulis, Eugene C Butcher, Wai-Ping Fung-Leung, Tadimeti S Rao, James C Paulson, Matthew S Macauley
CD22, a sialic acid-binding Ig-type lectin (Siglec) family member, is an inhibitory coreceptor of the BCR with established roles in health and disease. The restricted expression pattern of CD22 on B cells and most B cell lymphomas has made CD22 a therapeutic target for B cell-mediated diseases. Models to better understand how in vivo targeting of CD22 translates to human disease are needed. In this article, we report the development of a transgenic mouse expressing human CD22 (hCD22) in B cells and assess its ability to functionally substitute for murine CD22 (mCD22) for regulation of BCR signaling, Ab responses, homing, and tolerance...
September 29, 2017: Journal of Immunology: Official Journal of the American Association of Immunologists
June Ereño-Orbea, Taylor Sicard, Hong Cui, Mohammad T Mazhab-Jafari, Samir Benlekbir, Alba Guarné, John L Rubinstein, Jean-Philippe Julien
CD22 maintains a baseline level of B-cell inhibition to keep humoral immunity in check. As a B-cell-restricted antigen, CD22 is targeted in therapies against dysregulated B cells that cause autoimmune diseases and blood cancers. Here we report the crystal structure of human CD22 at 2.1 Å resolution, which reveals that specificity for α2-6 sialic acid ligands is dictated by a pre-formed β-hairpin as a unique mode of recognition across sialic acid-binding immunoglobulin-type lectins. The CD22 ectodomain adopts an extended conformation that facilitates concomitant CD22 nanocluster formation on B cells and binding to trans ligands to avert autoimmunity in mammals...
October 2, 2017: Nature Communications
John Baeten, Alexander Johnson, Sumsum Sunny, Amritha Suresh, Praveen Birur, K Uma, Deepak Kademani
BACKGROUND: Aberrant sialylation is accepted as a carcinogenic biomarker. In previous work, fluorescently labeled wheat germ agglutinin (WGA) distinguished between cancerous and normal oral biopsies. The purpose of this study was to investigate WGA-fluorescein isothiocyanate (FITC) as a point-of-care tool for detecting oral malignant and dysplastic lesions in vivo. METHODS: Subject recruitment was divided into two groups: (1) the clinically normal oral mucosa group; or (2) the presence of clinically suspicious oral lesion(s) group...
September 30, 2017: Head & Neck
Carolyn J P Jones, W R Twink Allen, Sandra Wilsher
INTRODUCTION: In this study, we compare glycosylation at the fetomaternal interface in 3 equine species: horse, donkey and zebra, all of which can interbreed to produce hybrids, to assess their glycan similarities and differences. METHODS: Sections cut from 3 specimens of horse (Equus caballus) placenta (50, 200 and 280 days gestation), one donkey (Equus asinus) placenta (65 cm crown-rump length) and 5 specimens of zebra (Equus quagga) placentae (81-239 days gestation) were stained with a panel of 24 biotinylated lectins using an avidin-peroxidase revealing system...
October 2017: Placenta
Wanqing Li, An Xiao, Yanhong Li, Hai Yu, Xi Chen
O-Acetylation of sialic acid (Sia) modulates its recognition by sialic acid-binding proteins and plays an important role in biological and pathological processes. 9-O-Acetylation is the most common modification of sialic acid in human. However, study of O-acetylated sialoglycans is hampered due to the instability of O-acetyl group towards pH changes and sensitivity to esterases. Our previous studies demonstrated a chemical biology method to this problem by replacing the oxygen atom in the C9 ester group of sialic acid by a nitrogen to form an amide...
September 18, 2017: Carbohydrate Research
Takahiko Aoki
Human red blood cells (RBC), which are the cells most commonly used in the study of biological membranes, have some glycoproteins in their cell membrane. These membrane proteins are band 3 and glycophorins A-D, and some substoichiometric glycoproteins (e.g., CD44, CD47, Lu, Kell, Duffy). The oligosaccharide that band 3 contains has one N-linked oligosaccharide, and glycophorins possess mostly O-linked oligosaccharides. The end of the O-linked oligosaccharide is linked to sialic acid. In humans, this sialic acid is N-acetylneuraminic acid (NeuAc)...
September 29, 2017: Membranes
Lan Xu, Zhenqing Zhang, Xue Sun, Jingjing Wang, Wei Xu, Lv Shi, Jiaojiao Lu, Juan Tang, Jingjing Liu, Xiong Su
The highly glycosylated bone sialoprotein (BSP) is an abundant non-collagenous phosphoprotein in bone which enhances osteoblast differentiation and new bone deposition in vitro and in vivo. However, the structural details of its different glycosylation linkages have not been well studied and their functions in bone homeostasis are not clear. Previous studies suggested that the O-glycans, but not the N-glycans on BSP, are highly sialylated. Herein, we employed tandem mass spectrometry (MS/MS) to demonstrate that the N-glycanson the recombinant human integrin binding sialoprotein (rhiBSP) are also enriched in sialic acids (SAs) at their termini...
September 25, 2017: Experimental Cell Research
Marc-Olivier Montjovent, Linglong Zou, Heinrich Faust, Afsaneh Abdolzade-Bavil, Patrick M Liu, Petra Struwe
AIM: Recombinant glycoprotein produced in nonhuman mammalian cell lines can be modified with the immunogenic nonhuman sialic N-glycolylneuraminic acid (Neu5Gc). We describe here a validated method for detection of antidrug antibodies against both protein and Neu5Gc-containing glycan epitopes. RESULTS: An electrochemiluminescent method was established with drug conjugates as capture and detection reagents. Rabbit antidrug polyclonal antibodies were used as the positive control for protein moiety-specific antibodies, while chicken anti-Neu5Gc polyclonal antibodies were used as the positive control for antibodies against Neu5Gc glycan epitope...
September 2017: Bioanalysis
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