Relevant bibliographies by topics / Sialyltransferases

Academic literature on the topic 'Sialyltransferases'

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Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "Sialyltransferases"

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Rosenstock, Philip, Kaya Bork, Chiara Massa, Philipp Selke, Barbara Seliger, and Rüdiger Horstkorte. "Sialylation of Human Natural Killer (NK) Cells Is Regulated by IL-2." Journal of Clinical Medicine 9, no. 6 (June 11, 2020): 1816. http://dx.doi.org/10.3390/jcm9061816.

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Sialic acids are terminal sugars on the cell surface that are found on all cell types including immune cells like natural killer (NK) cells. The attachment of sialic acids to different glycan structures is catalyzed by sialyltransferases in the Golgi. However, the expression pattern of sialyltransferases in NK cells and their expression after activation has not yet been analyzed. Therefore, the present study determines which sialyltransferases are expressed in human NK cells and if activation with IL-2 changes the sialylation of NK cells. The expression of sialyltransferases was analyzed in the three human NK cell lines NK-92, NKL, KHYG-1 and primary NK cells. NK-92 cells were cultured in the absence or presence of IL-2, and changes in the sialyltransferase expression were measured by qPCR. Furthermore, specific sialylation was investigated by flow cytometry. In addition, polySia and NCAM were measured by Western blot analyses. IL-2 leads to a reduced expression of ST8SIA1, ST6GAL1 and ST3GAL1. α-2,3-Sialylation remained unchanged, while α-2,6-sialylation was increased after IL-2 stimulation. Moreover, an increase in the amount of NCAM and polySia was observed in IL-2-activated NK cells, whereas GD3 ganglioside was decreased. In this study, all sialyltransferases that were expressed in NK cells could be identified. IL-2 regulates the expression of some sialyltransferases and leads to changes in the sialylation of NK cells.
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Janesch, Bettina, Hirak Saxena, Lyann Sim, and Warren W. Wakarchuk. "Comparison of α2,6-sialyltransferases for sialylation of therapeutic proteins." Glycobiology 29, no. 10 (July 8, 2019): 735–47. http://dx.doi.org/10.1093/glycob/cwz050.

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AbstractThe development of therapeutic proteins for the treatment of numerous diseases is one of the fastest growing areas of biotechnology. Therapeutic efficacy and serum half-life are particularly important, and these properties rely heavily on the glycosylation state of the protein. Expression systems to produce authentically fully glycosylated therapeutic proteins with appropriate terminal sialic acids are not yet perfected. The in vitro modification of therapeutic proteins by recombinant sialyltransferases offers a promising and elegant strategy to overcome this problem. Thus, the detailed expression and characterization of sialyltransferases for completion of the glycan chains is of great interest to the community. We identified a novel α2,6-sialyltransferase from Helicobacter cetorum and compared it to the human ST6Gal1 and a Photobacterium sp. sialyltransferase using glycoprotein substrates in a 96-well microtiter-plate-based assay. We demonstrated that the recombinant α2,6-sialyltransferase from H. cetorum is an excellent catalyst for modification of N-linked glycans of different therapeutic proteins.
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Czuchry, Diana, Paul Desormeaux, Melissa Stuart, Donald L. Jarvis, Khushi L. Matta, Walter A. Szarek, and Inka Brockhausen. "Identification and Biochemical Characterization of the Novel α2,3-Sialyltransferase WbwA from Pathogenic Escherichia coli Serotype O104." Journal of Bacteriology 197, no. 24 (September 21, 2015): 3760–68. http://dx.doi.org/10.1128/jb.00521-15.

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ABSTRACTThe sialyl-T antigen sialylα2-3Galβ1-3GalNAc is a common O-glycan structure in human glycoproteins and is synthesized by sialyltransferase ST3Gal1. The enterohemorrhagicEscherichia coliserotype O104 has the rare ability to synthesize a sialyl-T antigen mimic. We showed here that thewbwAgene of theE. coliO104 antigen synthesis gene cluster encodes an α2,3-sialyltransferase WbwA that transfers sialic acid from CMP-sialic acid to Galβ1-3GalNAcα-diphosphate-lipid acceptor. Nuclear magnetic resonance (NMR) analysis of purified WbwA enzyme reaction product indicated that the sialyl-T antigen sialylα2-3Galβ1-3GalNAcα-diphosphate-lipid was synthesized. We showed that the conserved His-Pro (HP) motif and Glu/Asp residues of two EDG motifs in WbwA are important for the activity. The characterization studies showed that WbwA fromE. coliO104 is a monofunctional α2,3-sialyltransferase and is distinct from human ST3Gal1 as well as all other known sialyltransferases due to its unique acceptor specificity. This work contributes to knowledge of the biosynthesis of bacterial virulence factors.IMPORTANCEThis is the first characterization of a sialyltransferase involved in the synthesis of an O antigen inE. coli. The enzyme contributes to the mimicry of human sialyl-T antigen and has unique substrate specificity but very little sequence identity to other sialyltransferases. Thus, the bacterial sialyltransferase is related to the human counterpart only by the similarity of biochemical activity.
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Yang, Rui, Mengge Gong, Siming Jiao, Juntian Han, Cui Feng, Meishan Pei, Zhongkai Zhou, Yuguang Du, and Jianjun Li. "Protein Engineering of Pasteurella multocida α2,3-Sialyltransferase with Reduced α2,3-Sialidase Activity and Application in Synthesis of 3′-Sialyllactose." Catalysts 12, no. 6 (May 25, 2022): 579. http://dx.doi.org/10.3390/catal12060579.

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Sialyltransferases are key enzymes for the production of sialosides. The versatility of Pasteurella multocida α2,3-sialyltransferase 1 (PmST1) causes difficulties in the efficient synthesis of α2,3-linked sialylatetd compounds, especial its α2,3-sialidase activity. In the current study, the α2,3-sialidase activity of PmST1 was further reduced by rational design-based protein engineering. Three double mutants PMG1 (M144D/R313Y), PMG2 (M144D/R313H) and PMG3 (M144D/R313N) were designed and constructed using M144D as the template and kinetically investigated. In comparison with M144D, the α2,3-sialyltransferase activity of PMG2 was enhanced by 1.4-fold, while its α2,3-sialidase activity was reduced by 4-fold. Two PMG2-based triple mutants PMG2-1 (M144D/R313H/T265S) and PMG2-2 (M144D/R313H/E271F) were then designed, generated and characterized. Compared with PMG2, triple mutants showed slightly improved α2,3-sialyltransferase activity, but their α2,3-sialidase activities were increased by 2.1–2.9 fold. In summary, PMG2 was used for preparative-scale production of 3′-SL (3′-sialyllactose) with a yield of >95%. These new PmST1 mutants could be potentially utilized for efficient synthesis of α2,3-linked sialosides. This work provides a guide to designing and constructing efficient sialyltransferases.
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Sticher, U., H. J. Gross, and R. Brossmer. "Purification of α 2,6-sialyltransferase from rat liver by dye chromatography." Biochemical Journal 253, no. 2 (July 15, 1988): 577–80. http://dx.doi.org/10.1042/bj2530577.

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We describe a simple three-step purification for Gal-beta 1,4-GlcNAc-alpha 2,6-sialyltransferase (EC 2.4.99.1) from rat liver which uses chromatography on Cibacron Blue F3GA and f.p.l.c. It gives a highly purified (11,000-fold) enzyme in 19% yield, which is free of other sialyltransferases, CMP-NeuAc hydrolase, sialidases and proteinases.
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Lee, Ki-Young, Hyung Gu Kim, Mi Ran Hwang, Jung Il Chae, Jai Myung Yang, Young Choon Lee, Young Kug Choo, Young Ik Lee, Sang-Soo Lee, and Su-Il Do. "The Hexapeptide Inhibitor of Galβ1,3GalNAc-specific α2,3-Sialyltransferase as a Generic Inhibitor of Sialyltransferases." Journal of Biological Chemistry 277, no. 51 (October 11, 2002): 49341–51. http://dx.doi.org/10.1074/jbc.m209618200.

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The mammalian Galβ1,3GalNAc-specific α2,3-sialyltransferase (ST3Gal I) was expressed as a secreted glycoprotein in High FiveTM(Trichoplusia ni) cells. Using this recombinant ST3Gal I, we screened the synthetic hexapeptide combinatorial library to explore a sialyltransferase inhibitor. We found that the hexapeptide, NH2-GNWWWW, exhibited the most strong inhibition of ST3Gal I among five different hexapeptides that were finally selected. The kinetic analysis of ST3Gal I inhibition demonstrated that this hexapeptide could act as a competitive inhibitor (Ki= 1.1 μm) on CMP-NeuAc binding to the enzyme. Moreover, the hexapeptide was shown to strongly inhibit bothN-glycan-specific α2,3- and α2,6-sialyltranferasein vitro, suggesting that this peptide may inhibit the broad range of sialyltransferases regardless of their linkage specificity. The inhibitory activityin vivowas investigated by RCA-I lectin blot analyses and by metabolicd-[6-3H]GlcNH2radiolabeling analyses ofN- andO-linked oligosaccharides in Chines hamster ovary cells. Our results demonstrate that the hexapeptide can act as a generic inhibitor of theN- andO-glycan-specific sialyltransferases in mammalian cells, which results in the significantly reduced NeuAc expression on cellular glycoproteinsin vivo.
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Pietrobono, Silvia, and Barbara Stecca. "Aberrant Sialylation in Cancer: Biomarker and Potential Target for Therapeutic Intervention?" Cancers 13, no. 9 (April 22, 2021): 2014. http://dx.doi.org/10.3390/cancers13092014.

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Sialylation is an integral part of cellular function, governing many biological processes including cellular recognition, adhesion, molecular trafficking, signal transduction and endocytosis. Sialylation is controlled by the levels and the activities of sialyltransferases on glycoproteins and lipids. Altered gene expression of these enzymes in cancer yields to cancer-specific alterations of glycoprotein sialylation. Mounting evidence indicate that hypersialylation is closely associated with cancer progression and metastatic spread, and can be of prognostic significance in human cancer. Aberrant sialylation is not only a result of cancer, but also a driver of malignant phenotype, directly impacting key processes such as tumor cell dissociation and invasion, cell-cell and cell-matrix interactions, angiogenesis, resistance to apoptosis, and evasion of immune destruction. In this review we provide insights on the impact of sialylation in tumor progression, and outline the possible application of sialyltransferases as cancer biomarkers. We also summarize the most promising findings on the development of sialyltransferase inhibitors as potential anti-cancer treatments.
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Harduin-Lepers, Anne, Rosella Mollicone, Philippe Delannoy, and Rafael Oriol. "The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach." Glycobiology 15, no. 8 (April 20, 2005): 805–17. http://dx.doi.org/10.1093/glycob/cwi063.

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Yamamoto, Takeshi, Yoshimitsu Takakura, and Hiroshi Tsukamoto. "Bacterial Sialyltransferases." Trends in Glycoscience and Glycotechnology 18, no. 102 (2006): 253–65. http://dx.doi.org/10.4052/tigg.18.253.

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Ratnam, Shobhitha, Arun Nagpurkar, and Sailen Mookerjea. "Characterization of serum, liver, and intestinal sialyltransferases from rats treated with colchicine." Biochemistry and Cell Biology 65, no. 3 (March 1, 1987): 183–87. http://dx.doi.org/10.1139/o87-023.

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A modified high pressure liquid chromatographic method using lactose (Galβ1 → 4G1c) as an exogenous acceptor has been used to characterize the sialyltransferases known to increase in the serum of colchicine-treated rats. The results show a 10-fold increase of Galβ1 → 4GlcNAc α2 → 6sialytransferase (α2 → 6 ST), whereas the Galβ1 → 3GlcNAc α2 → 3sialyltransferase showed only 1.6-fold increase in the serum after 17 h of colchicine treatment. The sialyltransferase activity in serum using exogenous desialylated, α1-acid glycoprotein as acceptor also showed an eightfold increase. In liver homogenate and Golgi membrane, the sialyltransferase activity when assayed with desialylated α1-acid glycoprotein as acceptor showed a slight decrease after 4 h, but returned to normal level after 17 h. A similar trend was seen when the two transferases were assayed with lactose as acceptor. The antiserum to rat α2 → 6 ST inhibited the sialyltransferase activity in serum, liver, and jejunal incubation medium. Jejunal sections from rats treated with colchicine for 4 h in presence of heated serum showed a decrease of sialyltransferase, with consequent increase of the α2 → 6 ST enzyme activity in the medium. This result suggests that intestinal tissue could be a source of increased serum enzyme activity in colchicine treatment.
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Dissertations / Theses on the topic "Sialyltransferases"

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Chiu, Cecilia P. C. "Crystallographic studies of bacterial sialyltransferases." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31274.

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Sialic acids terminate oligosaccharide chains on the surfaces of mammalian cells and many microbial species, often playing critical biological roles in recognition and adherence. The enzymes which transfer the sialic acid moiety to these key terminal positions are known as sialyltransferases. Despite their important biological roles very little is understood about the mechanism of action or molecular structure of these enzymes. Campylobacter jejuni, a highly prevalent food-borne pathogen that causes acute gastroenteritis in humans, contains two versions of a sialyltransferase: a monofunctional α-2,3-sialyltransferase Cst-I and a bifunctional α-2,3/8-sialyltransferase Cst-II. Both of these enzymes are responsible for lipooligosaccharides (LOS) sialylation to camouflage the bacterial surface from the host, and thus evade the immune system. In addition, sialylated-glycoconjugates on C. jejuni often mimic human gangliosides, contributing to the molecular basis of Guillain-Barré syndrome, an autoimmune disease of the peripheral nervous system that often develops post-infection. The sialyltransferase reaction is believed to proceed through an inversion mechanism, catalyzing the transfer of sialic acid from CMP-N-acetylneuraminic acid onto different acceptors. This thesis is to understand through high-resolution structural characterization, site specific mutagenesis and kinetic analysis, the mechanism of the glycosyl transfer(s) in both monofunctional and bifunctional Csts. Crystals of Cst-II were obtained and the complex structures with bound CMP, inert donor sugar analogue CMP-3-fluoro-N-acetylneuraminic acid (CMP-3FNeu5Ac) and inhibitor CDP were solved using MAD phasing from incorporated selenomethionines. Work within this study represents the first known structure of a sialyltransferase. Based on the position of the substrates, the active site of Cst-II has been elucidated. Site-directed mutagenesis of conserved residues in the active site was performed and mutants were characterized using enzyme kinetics. A reaction mechanism was proposed based on the kinetic assay. A directed evolution methodology was designed for glycosyltransferases using Cst-II as the model system. A single mutation, F91Y was found to substantially increase the reaction rate of the enzyme with a fluorescent-coupled acceptor, bodipy-lactose. The crystal structure of this Cst-II F91Y mutant was solved and it revealed an unexpected flip of the tyrosine side chain of Y91 from the core of the enzyme into the solvent region, exposing a hydrophobic pocket which seems to be capable of accommodating the bodipy ring structure. Together with kinetic analyses, the crystallographic study was able to explain the observed increase in the catalytic rate for this novel sugar acceptor. A monofunctional variant of Cst, Cst-I, also isolated from Campylobacter jejuni, was characterized crystallographically and kinetically. The conservation of active site residues supports the proposed mechanism for GT-42 sialyltransferases. The complex structure of the Cst-I enzyme with the donor analogue CMP-3FNeu5Ac provides a platform for molecular modeling of various acceptors into the active sites of Cst-I and Cst-II. The modeling shed lights upon the understanding of differences in substrate specificity. The structures of these complexes will be used as templates to design therapeutic inhibitors against this common human pathogen.
Medicine, Faculty of
Biochemistry and Molecular Biology, Department of
Graduate
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Sievi, Eeva. "Fate of mammalian golgi sialyltransferases in yeast." Helsinki : University of Helsinki, 2002. http://ethesis.helsinki.fi/julkaisut/eri/biote/vk/sievi/.

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Toivonen, Suvi. "Acceptor specificity studies of fucosyl- and sialyltransferases." Helsinki : University of Helsinki, 2002. http://ethesis.helsinki.fi/julkaisut/eri/biote/vk/toivonen/.

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Burke, Erin E. "Heavy atom and hydrogen kinetic isotope effect studies on recombinant, mammalian sialyltransferases." [Gainesville, Fla.] : University of Florida, 2005. http://purl.fcla.edu/fcla/etd/UFE0011586.

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MALTA, Tiago Barros Santos. "Imunodetecção de sialiltransferase e histoquímica de ácidos siálicos no câncer de mama e sua possível aplicação em diagnóstico, prognóstico e terapia." Universidade Federal de Pernambuco, 2016. https://repositorio.ufpe.br/handle/123456789/18431.

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CAPES, CNPQ, FACEPE
O câncer de mama feminino é o segundo tipo de câncer mais frequente no mundo, com aumento de incidência de 22% a cada ano. Estudos nas últimas décadas revelaram que a transformação maligna está associada a uma variedade de células com padrões de glicosilação alterados, como por exemplo a sialilação. Os ácidos siálicos tem sido relacionados à iniciação e progressão do câncer, tendo assim implicações potenciais na prevenção, diagnóstico e tratamento da doença. Este trabalho avaliou a expressão fenotípica de ST3Gal-I, através da imunohistoquímica, e o perfil de ácido siálico, através da histoquímica com lectinas usando Maackia Amurensis agglutinin II (MAA), em tecidos mamários diagnosticados com fibroadenoma (n=59), carcinoma ductal in situ (CDIS, n=40), carcinoma ductal invasivo (CDI, n=50) e carcinoma lobular (CL, n=42). Todos os tipos de lesões de mama apresentaram alta imunopositividade à ST3Gal-I, sendo observada uma expressão em 93,2% dos casos de Fibroadenoma, 92,5% de CDIS, 96% dos casos CDI e 85,2% de CL. As células apresentaram um padrão de marcação citoplasmático e perinuclear com relação à ST3Gal-I. Diferentes distribuições de resíduos de ácido siálico ⍺2,3-ligados, com um padrão de marcação predominantemente citoplasmático e membranar, foram observados nas lesões de mama estudadas. Os casos de fibroadenoma apresentaram o menor percentual de sialilação entre as lesões analisadas (47,5%), enquanto os de CDI o maior pecentual (98%). Embora este estudo não tenha mostrado diferença significativa na expressão de ST3Gal-I entre as lesões de mama, alterações representativas na presença de ácidos siálicos entre fibroadenoma e lesões malignas (p<0,0001), e também entre CDIS e CDI (p = 0.037) foram notadas. Não foram encontradas correlações significativas entre as expressões de ST3Gal-I e MAA, os marcadores de rotina e as características clinico-histopatológicas dos pacientes. Os resultados indicam uma distribuição particular de ácidos siálicos ⍺2,3-ligados nas células mamárias entre as lesões estudadas sugerindo seu envolvimento na progressão/manutenção do câncer de mama.
The female breast cancer is the second most common type of cancer in the world, with increased incidence of 22% every year. Recent studies in recent decades have revealed that the malignant transformation is associated with a variety of cells with altered glycosylation patterns such as sialylation. Sialic acids have been demonstrated to participate in cancer initiation and progression, thus has potential implications for cancer prevention, diagnosis and treatment. This study evaluated the phenotype expression of ST3Gal-I using immunohistochemistry and the sialic acid residues profile by histochemistry with Maackia amurensis agglutinin II (MAA) in mammary tissues diagnosed as fibroadenoma (n=59), ductal carcinoma in situ (DCIS, n=40), invasive ductal carcinoma (IDC, n=50) and lobular carcinoma (LC, n=42). All types of breast lesions showed high ST3Gal-I immunopositivity, its expression was observed in 93.2% cases of Fibroadenoma, 92.5% of DCIS, 96% of IDC and 85.2% cases of LC. The cells ST3Gal-I staining pattern was mainly cytoplasmatic and perinuclear. The MAA staining in breast lesions showed a diffuse cytoplasmatic and membrane pattern with different distribution of ⍺2,3-linked sialic acids among the lesions studied, fibroadenoma cases showed the lowest percentage among the analyzed lesions (47.5%) while IDC showed the highest (98%). Although this study did not show a significant difference in expression of ST3Gal-I among all lesions, representative alterations in sialic acid content between fibroadenoma and malignant lesions (p<0.0001), and also between CDIS and CDI (p=0.037) were observed. No significant correlations were found between the expressions of ST3Gal-I and MAA, routine markers and clinical-histopathological characteristics of the patients. Results indicate different distribution of ⍺2,3-linked sialic acids on the cells of the studied lesions which seems to be involved in breast cancer progression and/or maintenance.
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Pérez, Garay Marta. "Role of alpha 2,3-sialyltransferases ST3Gal III and ST3Gal IV in pancreatic ductal adenocarcinoma." Doctoral thesis, Universitat de Girona, 2011. http://hdl.handle.net/10803/7644.

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Este trabajo demuestra que los genes que codifican para los enzimas beta-galactosido alfa-2,3-sialiltransferasa 3 (ST3Gal III), y en menor medida beta-galactosido alfa-2,3-sialiltransferasa 4 (ST3Gal IV), están directamente implicados en etapas clave de la progresión tumoral como la adhesión, la migración y la formación de metástasis en las líneas de adenocarcinoma pancreático humano Capan-1 y MDAPanc-28. También, que las Especies Reactivas del Oxígeno (ROS) generadas durante los procesos de proliferación y diferenciación celular o debido a estímulos oxidantes externos, desempeñan un importante papel en el control de la síntesis de ST3Gal III y SLex, y por lo tanto en la regulación del fenotipo metastático. Además, junto al papel pro-adhesivo de la E-Selectina, este trabajo ha descrito efectos prometastáticos adicionales para esta molécula como inductora de la migración y de la secreción de VEGF a través de un mecanismo E-Selectina-SLex dependiente.
This work shows that genes that codifying for the enzymes beta-galactoside alpha-2,3-sialyltransferase 3 (ST3Gal III), and in a lower extent beta-galactoside alpha-2,3-sialyltransferase 4 (ST3Gal IV) , are directly implicated in key steps of tumour progression such as adhesion, migration and metastasis formation in the pancreatic adenocarcinoma cell lines Capan-1 and MDAPanc-28. Moreover, Reactive Oxygen Species (ROS) generated in these cell lines during cell proliferation-differentiation processes or by external oxidant stimuli, play a role in the control of ST3Gal III and SLex levels and in the acquisition of a more aggressive phenotype. And, together with the pro-adhesive role of E-Selectin for circulating cells, this work uncovers sE-Selectin dependent migration and VEGF secretion through a SLex depending mechanism, supporting additional pro-metastatic effects for sE-Selectin-SLex interaction.
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Preidl, Johannes Jonas [Verfasser]. "Entwicklung von Fluoreszenzpolarisations-Sonden und affinitätsbasierten Photomarkierern für Sialyltransferasen sowie HT-Screening einer Sialyltransferase / Johannes Preidl." Berlin : Freie Universität Berlin, 2011. http://d-nb.info/1026358213/34.

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Abu-Izneid, Tareq, and n/a. "The Synthesis and Evaluation of Functionalised Carbohydrates as Probes of Tumour Metastasis." Griffith University. Institute for Glycomics, 2005. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20061019.111424.

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Sialyltransferases, CMP-sialic acid synthetases and CMP-sialic acid transport proteins play a crucial role in the construction of cell surface glycoconjugates. These proteins also have a pivotal role to play in a number of diseases, including cancer. The sialyltransferase enzymes are responsible for transfering sialic acids from the donor substrate (CMP-sialic acid) to growing cell surface glycoconjugate chains within the Golgi apparatus. The CMP-sialic acid synthetase enzymes are responsible for the synthesis of the CMP-sialic acid, the donor substrate of the sialyltransferases in the nucleus, while the CMP-sialic acid transport proteins are responsible for transporting CMP-sialic acid from the Cytosol to the Golgi apparatus. When these proteins function in an abnormal way, hypersialylation results, leading to an increased level of sialylation on the cell surface. This increased level of sialylation aids in the detachment of primary tumour cells due to an increase in the level of overall negative charge, causing repulsion between the cancer cells. Therefore, the sialyltransferase enzymes, CMP-sialic acid synthetases and CMP-sialic acid transport proteins are intimately involved in the metastatic cascade associated with cancer. Chapter 1 provides a general introduction of cancer metastasis, discussing the roles of three target proteins (CMP-sialic acid synthetases, CMP-sialic acid transport proteins and sialyltransferases), as well as discussing their substrate specificities, with an emphasis on their involvements in cancer metastasis. The Chapter concludes with an overview of the types of compounds intended to be utilised as probes or inhibitors of these proteins. Chapter 2 describes the general approach towards the synthesis of CMP-Neu5Ac mimetics with a sulfur linkage in the presence of a phosphate group in the general structure 38. The precursor phosphoramidite derivative 45 was prepared and isolated in a good yield using Py.TFA. Unfortunately, the target compound 38 could not be prepared. Chapter 3 describes an alternative strategy wherein S-linked sialylnucleoside mimetics, of the general structure 39, with a sulfur linkage, but no phosphate group, between the sialylmimetic and the ribose moiety in the base is targeted. A series of these S-linked sialylnucleoside mimetics were successfully prepared. Cytidine, uridine, adenosine and 5-fluorouridine nucleosides were used to create a library of different nucleosides and with structural variability also present in the sialylmimetic portion. This small 'library' of 15 compounds was designed to shed light on the interaction of these compounds with the binding sites of the sialyltranferase, CMP-sialic acid synthetase and/or CM-sialic acid transport protein. Approaches towards the synthesis of O-linked sialylnucleoside mimetics of the general structure 40 are described in Chapter 4. Several methodologies are reported, as well as protecting group manipulations, for successful preparation of these sialylnucleoside mimetics. Cytidine and uridine were employed as the nucleosides, thus allowing a direct comparison between the O- and S-linked sialylnucleoside mimetics in biological evaluation. It appears from these synthetic investigations that gaining access into the O-linked series is not as straightforward as for the S-linked series, with alternative protecting group strategies required for the different nucleosides. The biological evaluation of some of the compounds reported in Chapters 3 and 4 is detailed in Chapter 5. The sialylnucleoside mimetics were evaluated, by 1H NMR spectroscopy, for their ability to inhibit CMP-KDN synthetase. In addition, an initial 1H NMR spectroscopic-based assay was investigated for inhibition studies of α(2,6)sialyltranferase in the absence of potential inhibitors. The final chapter (Chapter 6) brings together full experimental details in support of the compounds described in the preceding Chapters.
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Abu-Izneid, Tareq. "The Synthesis and Evaluation of Functionalised Carbohydrates as Probes of Tumour Metastasis." Thesis, Griffith University, 2005. http://hdl.handle.net/10072/367269.

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Sialyltransferases, CMP-sialic acid synthetases and CMP-sialic acid transport proteins play a crucial role in the construction of cell surface glycoconjugates. These proteins also have a pivotal role to play in a number of diseases, including cancer. The sialyltransferase enzymes are responsible for transfering sialic acids from the donor substrate (CMP-sialic acid) to growing cell surface glycoconjugate chains within the Golgi apparatus. The CMP-sialic acid synthetase enzymes are responsible for the synthesis of the CMP-sialic acid, the donor substrate of the sialyltransferases in the nucleus, while the CMP-sialic acid transport proteins are responsible for transporting CMP-sialic acid from the Cytosol to the Golgi apparatus. When these proteins function in an abnormal way, hypersialylation results, leading to an increased level of sialylation on the cell surface. This increased level of sialylation aids in the detachment of primary tumour cells due to an increase in the level of overall negative charge, causing repulsion between the cancer cells. Therefore, the sialyltransferase enzymes, CMP-sialic acid synthetases and CMP-sialic acid transport proteins are intimately involved in the metastatic cascade associated with cancer. Chapter 1 provides a general introduction of cancer metastasis, discussing the roles of three target proteins (CMP-sialic acid synthetases, CMP-sialic acid transport proteins and sialyltransferases), as well as discussing their substrate specificities, with an emphasis on their involvements in cancer metastasis. The Chapter concludes with an overview of the types of compounds intended to be utilised as probes or inhibitors of these proteins. Chapter 2 describes the general approach towards the synthesis of CMP-Neu5Ac mimetics with a sulfur linkage in the presence of a phosphate group in the general structure 38. The precursor phosphoramidite derivative 45 was prepared and isolated in a good yield using Py.TFA. Unfortunately, the target compound 38 could not be prepared. Chapter 3 describes an alternative strategy wherein S-linked sialylnucleoside mimetics, of the general structure 39, with a sulfur linkage, but no phosphate group, between the sialylmimetic and the ribose moiety in the base is targeted. A series of these S-linked sialylnucleoside mimetics were successfully prepared. Cytidine, uridine, adenosine and 5-fluorouridine nucleosides were used to create a library of different nucleosides and with structural variability also present in the sialylmimetic portion. This small 'library' of 15 compounds was designed to shed light on the interaction of these compounds with the binding sites of the sialyltranferase, CMP-sialic acid synthetase and/or CM-sialic acid transport protein. Approaches towards the synthesis of O-linked sialylnucleoside mimetics of the general structure 40 are described in Chapter 4. Several methodologies are reported, as well as protecting group manipulations, for successful preparation of these sialylnucleoside mimetics. Cytidine and uridine were employed as the nucleosides, thus allowing a direct comparison between the O- and S-linked sialylnucleoside mimetics in biological evaluation. It appears from these synthetic investigations that gaining access into the O-linked series is not as straightforward as for the S-linked series, with alternative protecting group strategies required for the different nucleosides. The biological evaluation of some of the compounds reported in Chapters 3 and 4 is detailed in Chapter 5. The sialylnucleoside mimetics were evaluated, by 1H NMR spectroscopy, for their ability to inhibit CMP-KDN synthetase. In addition, an initial 1H NMR spectroscopic-based assay was investigated for inhibition studies of ?(2,6)sialyltranferase in the absence of potential inhibitors. The final chapter (Chapter 6) brings together full experimental details in support of the compounds described in the preceding Chapters.
Thesis (PhD Doctorate)
Doctor of Philosophy (PhD)
Institute for Glycomics
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Eggers, Katinka Caroline [Verfasser]. "Studies on the structural basis of NCAM functions and on the role of (poly)sialyltransferases and their biosynthetic products in onco- and neurodevelopment / Katinka Caroline Eggers." Hannover : Technische Informationsbibliothek und Universitätsbibliothek Hannover (TIB), 2012. http://d-nb.info/1024938425/34.

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Books on the topic "Sialyltransferases"

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Gherardini, Lisa. Sialyltransferase activity as a possible indicator of psychotic disorders. Dublin: University College Dublin, 1998.

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Bramley, Jennifer. Characterisation of a sialyltransferase-deficient mutant of Neisseria gonorrhoeae. Birmingham: University of Birmingham, 1997.

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Bruner, Michael John. Characterization of the reaction catalyzed by alpha (2-6) Sialyltransferase. 1999.

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Book chapters on the topic "Sialyltransferases"

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Basu, Subhash, Manju Basu, and Shib Sankar Basu. "Biological Specificity of Sialyltransferases." In Biology of the Sialic Acids, 69–94. Boston, MA: Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-9504-2_3.

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Yamamoto, Takeshi. "Sialyltransferases from marine environments." In Marine Glycobiology, 193–206. Taylor & Francis Group, 6000 Broken Sound Parkway NW, Suite 300, Boca Raton, FL 33487-2742: CRC Press, 2016. http://dx.doi.org/10.1201/9781315371399-15.

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Song, Kwon-Ho, and Cheorl-Ho Kim. "Screening for Xenoantigenic Determinants Formed by Sialyltransferases." In Sialo-Xenoantigenic Glycobiology, 43–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-34094-9_5.

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Hosoguchi, Kensaku, Takahiro Maeda, Jun-ichi Furukawa, Hiroshi Hinou, and Shin-Ichiro Nishimura. "An Efficient Strategy for the Exploration of Specific Inhibitors of Sialyltransferases." In Molecular Imaging for Integrated Medical Therapy and Drug Development, 294–301. Tokyo: Springer Japan, 2010. http://dx.doi.org/10.1007/978-4-431-98074-2_29.

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Alturfan, A. Ata, and Ebru Emekli-Alturfan. "Interaction of Sialyltransferases, Sialidases, and Sialic Acids in Liver Diseases and Applications to Biomarker Discovery." In Biomarkers in Disease: Methods, Discoveries and Applications, 247–64. Dordrecht: Springer Netherlands, 2017. http://dx.doi.org/10.1007/978-94-007-7675-3_19.

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Alturfan, A. Ata, and Ebru Emekli-Alturfan. "Interaction of Sialyltransferases, Sialidases and Sialic Acids in Liver Diseases and Applications to Biomarker Discovery." In Biomarkers in Disease: Methods, Discoveries and Applications, 1–18. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-007-7742-2_19-1.

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Schomburg, Dietmar, and Dörte Stephan. "Monosialoganglioside sialyltransferase." In Enzyme Handbook 12, 1129–32. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_244.

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Schomburg, Dietmar, and Dörte Stephan. "Galactosyldiacylglycerol alpha-2,3-sialyltransferase." In Enzyme Handbook 12, 1145–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_247.

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Schomburg, Dietmar, and Dörte Stephan. "Lactosylceramide alpha-2,3-sialyltransferase." In Enzyme Handbook 12, 1163–67. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_251.

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Schomburg, Dietmar, and Dörte Stephan. "Neolactotetraosylceramide alpha-2,3-sialyltransferase." In Enzyme Handbook 12, 1169–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-61117-9_252.

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Conference papers on the topic "Sialyltransferases"

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Drinnan, Nicholas B., Laurent Bornaghi, Alison Franks, Ylva Strandberg, and Judy Halliday. "RESIN BOUND ACCEPTORS FOR SIALYLTRANSFERASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.773.

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Lee, Ki-Young, Jung Il Chae, Kyung-Cheol Sohn, Jae-Eun Park, Yunjeong Kang, and Su-Il Do. "THE HEXAPEPTIDE INHIBITOR OF ST3Gal I SIALYLTRANSFERASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.663.

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Izume, Masayuki, Syunsuke Kaneko, Katsuhiro Wada, Hideya Yuasa, and Hironobu Hashimoto. "SYNTHESIS OF BISUBSTRATE ANALOGUES OF FUCOSYL- AND SIALYLTRANSFERASE." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.600.

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Galan, M. Carmen, Andre P. Venot, John Glushka, Anne Imberty, and GeertJan Boons. "ALPHA-(2,6)-SIALYLTRANSFERASE CATALYZED SIALYLATIONS OF CONFORMATIONALLY CONSTRAINED OLIGOSACCHARIDES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.455.

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Fan, Tan-chi, Wen-der Lin, Chih-hao Chang, Lan-yi Chang, Zhin-mei Chen, Kay-hooi Khoo, and Alice Yu. "Abstract 2305: Role of ST3Gal1 sialyltransferase in breast cancer cells." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2305.

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Skropeta, Danielle, and Richard R. Schmidt. "RAPID ACCESS TO CHIRAL, NON-RACEMIC SIALYLTRANSFERASE INHIBITORS BASED ON TRANSITION STATE ANALOGUES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.454.

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Schultz, Matthew J., Andrew T. Holdbrooks, Asmi Chakraborty, William E. Grizzle, Charles N. Landen, Donald J. Buchsbaum, Michael G. Conner, et al. "Abstract 3327: The tumor associated sialyltransferase ST6Gal-I promotes a cancer stem cell phenotype and upregulates stem-related transcription factors." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3327.

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Reports on the topic "Sialyltransferases"

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Lau, Joseph T. Sialyltransferase in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2001. http://dx.doi.org/10.21236/ada400483.

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Lau, Joseph T. Sialyltransferase in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada411655.

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Ivanov, Dimitar, and Katerina Todorova. Multiple Forms of Serum Sialyltransferase in Normal Rats and Rats Bearing Zajdela Hepatoma. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, September 2020. http://dx.doi.org/10.7546/crabs.2020.09.08.

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