Journal articles on the topic 'Glycotransferase'

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1

Borges, Chad R., Douglas S. Rehder, and Paolo Boffetta. "Multiplexed Surrogate Analysis of Glycotransferase Activity in Whole Biospecimens." Analytical Chemistry 85, no. 5 (February 15, 2013): 2927–36. http://dx.doi.org/10.1021/ac3035579.

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2

Zhu, Zhongyu, Boopathy Ramakrishnan, Jinyu Li, Yanping Wang, Yang Feng, Ponraj Prabakaran, Simona Colantonio, Marzena A. Dyba, Pradman K. Qasba, and Dimiter S. Dimitrov. "Site-specific antibody-drug conjugation through an engineered glycotransferase and a chemically reactive sugar." mAbs 6, no. 5 (September 3, 2014): 1190–200. http://dx.doi.org/10.4161/mabs.29889.

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3

Rahman, A. K. M. Shofiqur, Naoyasu Sugitani, Masahiro Hatsu, and Kazuhiro Takamizawa. "A role of xylanase, α-L-arabinofuranosidase, and xylosidase in xylan degradation." Canadian Journal of Microbiology 49, no. 1 (January 1, 2003): 58–64. http://dx.doi.org/10.1139/w02-114.

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Renewable natural resources such as xylans are abundant in many agricultural wastes. Penicillium sp. AHT-1 is a strong producer of xylanolytic enzymes. The sequential activities of its xylanase, α-L-arabinofuranosidase, and β-xylosidase on model hemicellulose oat–spelt xylan was investigated. Optimum production of the enzymes was found in culture containing oat–spelt xylan at 30°C and initial pH 7.0 after 6 days. The enzymes were partially purified by ammonium sulphate fractionation and anion-exchange chromatography on DEAE-Toyopearl 650 S. The apparent molecular mass was 21 kDa, and the protein displayed an "endo" mode of action. The xylanase exhibited glycotransferase activity. It synthesized higher oligosaccharides from the initial substrates, and xylotriose was the shortest unit of substrate transglycosylated. Xylanolytic enzymes (enzyme mixture) produced by this Penicillium sp. interacted cooperatively and sequentially in the hydrolysis of oat–spelt xylan in the following order: α-L-arabinofuranosidase [Formula: see text] xylanase [Formula: see text] β-xylosidase. All three enzymes exhibited optimal activity under the same conditions (temperature, pH, cultivation), indicating that they alone are sufficient to completely depolymerize the test xylan. Results indicate that the xylanolytic enzyme mixture of Penicillium sp. AHT-1 could be useful for bioconversion of xylan-rich plant wastes to value-added products.Key words: xylanase, enzyme purification, enzymatic hydrolysis, Penicillium sp. AHT-1.
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4

Alonso, Leocadio, Patrick Fox, María Calvo, and Javier Fontecha. "Effect of Beta Cyclodextrin on the Reduction of Cholesterol in Ewe’s Milk Manchego Cheese." Molecules 23, no. 7 (July 20, 2018): 1789. http://dx.doi.org/10.3390/molecules23071789.

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Beta-cyclodextrin (β-CD) is a cyclic oligosaccharide consisting of seven glucose units and is produced from starch using cyclodextrin glycotransferase enzymes to break the polysaccharide chain and forming a cyclic polysaccharide molecule. The use of β-CD in food research for reduction of cholesterol is increasing due to its affinity for non-polar molecules such as cholesterol. The aim of this study was to evaluate the feasibility of using β-CD in cholesterol removal from pasteurized ewe’s milk Manchego cheese and evaluate the effect on the main components of the milk, lipids, and flavor characteristics. Approximately 97.6% cholesterol reduction was observed in the cheese that was treated using β-CD. Physicochemical properties (fat, moisture and protein) were not changed by the β-CD treatment, except the soluble nitrogen and non-protein nitrogen that showed slight differences after the treatment. The amount of the different components of the lipid fraction (fatty acids, triglycerides and phospholipids) were similar in cheeses treated and not treated with β-CD. Flavor compound and short chain free fatty acids were not mostly significantly influenced by the effect of the β-CD. β-CD molecules are edible and nontoxic and as a result they can be used safely for cholesterol removal processing in cheese manufacturing. Therefore, the present study suggests that β-CD treatment is an effective process for cholesterol removal from Manchego cheese while preserving its properties.
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5

Glickman, J. Fraser, and Doug Auld. "Generic Glycotransferases Assays." Assay and Drug Development Technologies 2, no. 4 (August 1, 2004): 445. http://dx.doi.org/10.1089/1540658041850706.

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6

ZHU, Jing, Itaru WATANABE, Amanda POHOLEK, Matthew KOSS, Barbara GOMEZ, Chaowen YAN, Esperanza RECIO-PINTO, and William B. THORNHILL. "Allowed N-glycosylation sites on the Kv1.2 potassium channel S1–S2 linker: implications for linker secondary structure and the glycosylation effect on channel function." Biochemical Journal 375, no. 3 (November 1, 2003): 769–75. http://dx.doi.org/10.1042/bj20030517.

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N-glycosylation is a post-translational modification that plays a role in the trafficking and/or function of some membrane proteins. We have shown previously that N-glycosylation affected the function of some Kv1 voltage-gated potassium (K+) channels [Watanabe, Wang, Sutachan, Zhu, Recio-Pinto and Thornhill (2003) J. Physiol. (Cambridge, U.K.) 550, 51–66]. Kv1 channel S1–S2 linkers vary in length but their N-glycosylation sites are at similar relative positions from the S1 or S2 membrane domains. In the present study, by a scanning mutagenesis approach, we determined the allowed N-glycosylation sites on the Kv1.2 S1–S2 linker, which has 39 amino acids, by engineering N-glycosylation sites and assaying for glycosylation, using their sensitivity to glycosidases. The middle section of the linker (54% of linker) was glycosylated at every position, whereas both end sections (46% of linker) near the S1 or S2 membrane domains were not. These findings suggested that the middle section of the S1–S2 linker was accessible to the endoplasmic reticulum glycotransferase at every position and was in the extracellular aqueous phase, and presumably in a flexible conformation. We speculate that the S1–S2 linker is mostly a coiled-loop structure and that the strict relative position of native glycosylation sites on these linkers may be involved in the mechanism underlying the functional effects of glycosylation on some Kv1 K+ channels. The S3–S4 linker, with 16 amino acids and no N-glycosylation site, was not glycosylated when an N-glycosylation site was added. However, an extended linker, with an added N-linked site, was glycosylated, which suggested that the native linker was not glycosylated due to its short length. Thus other ion channels or membrane proteins may also have a high glycosylation potential on a linker but yet have similarly positioned native N-glycosylation sites among isoforms. This may imply that the native position of the N-glycosylation site may be important if the carbohydrate tree plays a role in the folding, stability, trafficking and/or function of the protein.
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7

Pejenaute-Ochoa, María Dolores, Carlos Santana-Molina, Damien P. Devos, José Ignacio Ibeas, and Alfonso Fernández-Álvarez. "Structural, Evolutionary, and Functional Analysis of the Protein O-Mannosyltransferase Family in Pathogenic Fungi." Journal of Fungi 7, no. 5 (April 23, 2021): 328. http://dx.doi.org/10.3390/jof7050328.

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Protein O-mannosyltransferases (Pmts) comprise a group of proteins that add mannoses to substrate proteins at the endoplasmic reticulum. This post-translational modification is important for the faithful transfer of nascent glycoproteins throughout the secretory pathway. Most fungi genomes encode three O-mannosyltransferases, usually named Pmt1, Pmt2, and Pmt4. In pathogenic fungi, Pmts, especially Pmt4, are key factors for virulence. Although the importance of Pmts for fungal pathogenesis is well established in a wide range of pathogens, questions remain regarding certain features of Pmts. For example, why does the single deletion of each pmt gene have an asymmetrical impact on host colonization? Here, we analyse the origin of Pmts in fungi and review the most important phenotypes associated with Pmt mutants in pathogenic fungi. Hence, we highlight the enormous relevance of these glycotransferases for fungal pathogenic development.
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8

Dejgaard, Selma Yilmaz, Ayesha Murshid, Kristina M. Dee, and John F. Presley. "Confocal Microscopy-based Linescan Methodologies for Intra-Golgi Localization of Proteins." Journal of Histochemistry & Cytochemistry 55, no. 7 (March 19, 2007): 709–19. http://dx.doi.org/10.1369/jhc.6a7090.2007.

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Localization of resident Golgi proteins to earlier ( cis) or later ( trans) Golgi compartments has traditionally required quantitative immunocytochemistry and electron microscopy, which are inaccessible to many researchers. For this reason, light microscopy has often been used, initially for localization of Golgi glycotransferases and, more recently, for other Golgi proteins (e.g., Arf1, GBF1, Rab6). Quantitation of light microscopic intra-Golgi localization can be problematic. We describe here a novel quantitative light microscopic methodology using linescans crossing the Golgi ribbon. Our method determines a localization for the unknown protein in a one-dimensional coordinate system in which 0.0 corresponds to localization of a cis marker and 1.0 to localization of a trans marker. We also describe a variant of this methodology in which Golgi morphology is simplified by nocodazole-induced dispersal into ministacks, allowing a fully automated analysis. In our assay, β1,4-galactosyltransferase-YFP and Golgin97 localize similarly to trans markers, whereas p115, GBF1, and p58-YFP are similarly near other cis markers. The medial Golgi protein α1,3–1,6-mannosidase II gives an intermediate localization in this assay. These methodologies may prove useful in instances where electron microscopy is technically difficult as well as when rapid analysis of large numbers of samples is required.
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9

Urun, Yuksel, Kathryn M. Wilson, Irene M. Shui, Edward L. Giovannucci, Brian M. Wolpin, Paul Linh Nguyen, Lorelei A. Mucci, and Toni K. Choueiri. "ABO blood group and risk of lethal prostate cancer." Journal of Clinical Oncology 32, no. 4_suppl (February 1, 2014): 69. http://dx.doi.org/10.1200/jco.2014.32.4_suppl.69.

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69 Background: An individual’s blood group is defined by variability in glycotransferases expressed on red blood cell surface; these ABO antigens are also highly expressed on epithelial cells. Previous studies have suggested associations between ABO blood group and increased risk of epithelial cancers including gastric, pancreatic, and ovarian; however, its relationship with risk of prostate carcinoma, and its aggressiveness remains unclear. Methods: We prospectively evaluated the association between ABO blood group and risk of lethal prostate cancer in the Health Professionals Follow-up Study (HPFS) from 1996 to 2008. Hazard ratios (HRs) and 95% confidence intervals (CIs) were calculated using Cox proportional hazards models with adjustment for other risk factors and prostate-specific antigen testing. Results: During 12 years of follow-up of 26,602 men, 2,703 cases of incident prostate cancer were documented, including 289 lethal cases (prostate cancer death or distant metastases). The frequency of ABO blood type was similar between men who developed prostate cancer (37% A, 7% AB, 13% B, and 43% O) and other participants (37% A, 8% AB, 12% B, and 43% O). On multivariate analysis, blood type was not associated with overall prostate cancer incidence. However, compared to men with blood group O, those with blood group AB were significantly less likely to develop lethal prostate cancer (multivariate-adjusted HR = 0.39 [95% confidence interval {CI} = 0.18-0.85]). There was no association between type B or A compared to O with lethal disease. ABO blood type was not significantly associated with the risk of advanced stage or high-grade cancers (Gleason score 8 to 10). Conclusions: Blood group AB was associated with a lower risk of lethal prostate cancer compared to blood group O. Further studies are needed to replicate these findings and to clarify possible biological mechanisms underlying this association.
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10

Tatlow, Dean. "Miglustat: A glycotransferase inhibitor for Covid-19 treatment." Qeios, January 21, 2021. http://dx.doi.org/10.32388/pe4tsq.

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11

Tatlow, Dean. "Miglustat: A glycotransferase inhibitor for Covid-19 treatment." Qeios, January 30, 2021. http://dx.doi.org/10.32388/pe4tsq.2.

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12

Tatlow, Dean. "Miglustat: A glycotransferase inhibitor for Covid-19 treatment." Qeios, February 14, 2021. http://dx.doi.org/10.32388/pe4tsq.4.

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13

Tatlow, Dean. "Miglustat: A glycotransferase inhibitor for Covid-19 treatment." Qeios, February 3, 2021. http://dx.doi.org/10.32388/pe4tsq.3.

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14

Lili, Qi, Lu Xiaohui, Mao Haiguang, and Wang Jinbo. "Clostridium butyricum Induces the Production and Glycosylation of Mucins in HT-29 Cells." Frontiers in Cellular and Infection Microbiology 11 (June 17, 2021). http://dx.doi.org/10.3389/fcimb.2021.668766.

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C. butyricum is a common gut commensal bacterium, which has many positive functions in human intestine. In this study, we investigated the effects of monosaccharide and its derivatives on the adhesion of C. butyricum to the mucus of HT-29 cells. RNA interference was performed to assess the roles of MUC2 and glycan in the adhesion of C. butyricum to HT-29 cells. The effects of C. butyricum on the glycosylation of mucins were assayed with fluorescence microscope. The expression levels of mucins and glycotransferases were also determined. The results showed that C. butyricum could adhere to the mucins secreted by HT-29 cells. Several kinds of monosaccharides inhibited the adhesion of C. butyricum to HT-29 cells, which suggested that the mucus glycan was the attaching sites of this bacterium. Knockdown of MUC2, FUT2 or GALNT7 significantly decreased the numbers of the bacteria adhering to HT-29 cells. When colonizing on the surface of HT-29 cells, C. butyricum could increase the production of mucins, promote the expression of glycotransferase, and induce the glycosylation of mucins. These results demonstrated that the glycan of mucus played important roles in the adhesion of C. butyricum to HT-29 cells. This study indicates for the first time that C. butyricum possesses the ability to modulate the glycosylation profile of mucus secreted by HT-29 cells. These findings contribute to understanding the mechanism of interaction between colonic epithelial cells and commensal bacteria.
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15

Mamsa, Hafsa, Rachelle L. Stark, Kara M. Shin, Aaron M. Beedle, and Rachelle H. Crosbie. "Sarcospan increases laminin binding capacity of α-dystroglycan to ameliorate DMD independent of Galgt2." Human Molecular Genetics, September 28, 2021. http://dx.doi.org/10.1093/hmg/ddab276.

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Abstract In Duchenne muscular dystrophy (DMD), mutations in dystrophin result in a loss of the dystrophin-glycoprotein complex at the myofiber membrane, which functions to connect the extracellular matrix with the intracellular actin cytoskeleton. The dystroglycan subcomplex interacts with dystrophin and spans the sarcolemma where its extensive carbohydrates (matriglycan and CT2 glycan) directly interact with the extracellular matrix. In the current manuscript, we show that sarcospan overexpression enhances the laminin-binding capacity of dystroglycan in DMD muscle by increasing matriglycan glycosylation of α-dystroglycan. Furthermore, we find that this modification is not affected by loss of Galgt2, a glycotransferase which catalyzes the CT2 glycan. Our findings reveal that the matriglycan carbohydrates, and not the CT2 glycan, are necessary for sarcospan-mediated amelioration of DMD. Overexpression of Galgt2 in the DMD mdx murine model prevents muscle pathology by increasing CT2 modified α-dystroglycan. Galgt2 also increases expression of utrophin, which compensates for the loss of dystrophin in DMD muscle. We found that combined loss of Galgt2 and dystrophin reduced utrophin expression; however, it did not interfere with sarcospan rescue of disease. These data reveal a partial dependence of sarcospan on Galgt2 for utrophin upregulation. In addition, sarcospan alters the cross-talk between the adhesion complexes by decreasing the association of integrin β1D with dystroglycan complexes. In conclusion, sarcospan functions to re-wire the cell to matrix connections by strengthening the cellular adhesion and signaling which, in turn, increases the resilience of the myofiber membrane.
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16

Singh, Jugpreet, Jack Fabrizio, Elsa Desnoues, Julliany Pereira Silva, Wolfgang Busch, and Awais Khan. "Root system traits impact early fire blight susceptibility in apple (Malus × domestica)." BMC Plant Biology 19, no. 1 (December 2019). http://dx.doi.org/10.1186/s12870-019-2202-3.

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Abstract Background Although it is known that resistant rootstocks facilitate management of fire blight disease, incited by Erwinia amylovora, the role of rootstock root traits in providing systemic defense against E. amylovora is unclear. In this study, the hypothesis that rootstocks of higher root vigor provide higher tolerance to fire blight infection in apples is tested. Several apple scion genotypes grafted onto a single rootstock genotype and non-grafted ‘M.7’ rootstocks of varying root vigor are used to assess phenotypic and molecular relationships between root traits of rootstocks and fire blight susceptibility of apple scion cultivars. Results It is observed that different root traits display significant (p < 0.05) negative correlations with fire blight susceptibility. In fact, root surface area partially dictates differential levels of fire blight susceptibility of ‘M.7’ rootstocks. Furthermore, contrasting changes in gene expression patterns of diverse molecular pathways accompany observed differences in levels of root-driven fire blight susceptibility. It is noted that a singular co-expression gene network consisting of genes from defense, carbohydrate metabolism, protein kinase activity, oxidation-reduction, and stress response pathways modulates root-dependent fire blight susceptibility in apple. In particular, WRKY75 and UDP-glycotransferase are singled-out as hub genes deserving of further detailed analysis. Conclusions It is proposed that low root mass may incite resource-limiting conditions to activate carbohydrate metabolic pathways, which reciprocally interact with plant immune system genes to elicit differential levels of fire blight susceptibility.
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17

Liu, Jiajia, Lijun Han, Guodong Li, Aili Zhang, Xiaoli Liu, and Mingzhi Zhao. "Transcriptome and metabolome profiling of the medicinal plant Veratrum mengtzeanum reveal key components of the alkaloid biosynthesis." Frontiers in Genetics 14 (January 20, 2023). http://dx.doi.org/10.3389/fgene.2023.1023433.

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Veratrum mengtzeanum is the main ingredient for Chinese folk medicine known as “Pimacao” due to its unique alkaloids. A diverse class of plant-specific metabolites having key pharmacological activities. There are limited studies on alkaloid synthesis and its metabolic pathways in plants. To elucidate the alkaloid pathway and identify novel biosynthetic enzymes and compounds in V. mengtzeanum, transcriptome and metabolome profiling has been conducted in leaves and roots. The transcriptome of V. mengtzeanum leaves and roots yielded 190,161 unigenes, of which 33,942 genes expressed differentially (DEGs) in both tissues. Three enriched regulatory pathways (isoquinoline alkaloid biosynthesis, indole alkaloid biosynthesis and tropane, piperidine and pyridine alkaloid biosynthesis) and a considerable number of genes such as AED3-like, A4U43, 21 kDa protein-like, 3-O-glycotransferase 2-like, AtDIR19, MST4, CASP-like protein 1D1 were discovered in association with the biosynthesis of alkaloids in leaves and roots. Some transcription factor families, i.e., AP2/ERF, GRAS, NAC, bHLH, MYB-related, C3H, FARI, WRKY, HB-HD-ZIP, C2H2, and bZIP were also found to have a prominent role in regulating the synthesis of alkaloids and steroidal alkaloids in the leaves and roots of V. mengtzeanum. The metabolome analysis revealed 74 significantly accumulated metabolites, with 55 differentially accumulated in leaves compared to root tissues. Out of 74 metabolites, 18 alkaloids were highly accumulated in the roots. A novel alkaloid compound viz; 3-Vanilloylygadenine was discovered in root samples. Conjoint analysis of transcriptome and metabolome studies has also highlighted potential genes involved in regulation and transport of alkaloid compounds. Here, we have presented a comprehensive metabolic and transcriptome profiling of V. mengtzeanum tissues. In earlier reports, only the roots were reported as a rich source of alkaloid biosynthesis, but the current findings revealed both leaves and roots as significant manufacturing factories for alkaloid biosynthesis.
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18

Guo, Zhongwu, and Qingjiang Li. "Enzymatic Synthesis of Glycosphingolipids: A Review." Synthesis, March 11, 2021. http://dx.doi.org/10.1055/a-1426-4451.

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AbstractGlycosphingolipids (GSLs) are the major vertebrate glycolipids, which contain two distinctive moieties, a glycan and a ceramide, stitched together by a β-glycosidic linkage. The hydrophobic lipid chains of ceramide can insert into the cell membrane to form ‘lipid rafts’ and anchor the hydrophilic glycan onto the cell surface to generate microdomains and function as signaling molecules. GSLs mediate signal transduction, cell interactions, and many other biological activities, and are also related to many diseases. To meet the need of biological studies, chemists have developed various synthetic methodologies to access GSLs. Among them, the application of enzymes to GSL synthesis has witnessed significant advancements in the past decades. This short review briefly summarizes the history and progress of enzymatic GSL synthesis.1 Introduction1.1 The Glycosphingolipid Structure1.2 GSL Biosynthesis1.3 Functions and Biological Significance1.4 Overview of GSL Synthesis1.5 Scope of the Review2 Glycotransferases for GSL Synthesis3 Glycosynthases for GSL Synthesis4 Enzymatic Synthesis of Ceramide5 Conclusion
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