Relevant bibliographies by topics / Glycoproteome

Academic literature on the topic 'Glycoproteome'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Glycoproteome"

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Schulze, Stefan, Friedhelm Pfeiffer, Benjamin A. Garcia, and Mechthild Pohlschroder. "Comprehensive glycoproteomics shines new light on the complexity and extent of glycosylation in archaea." PLOS Biology 19, no. 6 (June 17, 2021): e3001277. http://dx.doi.org/10.1371/journal.pbio.3001277.

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Glycosylation is one of the most complex posttranslational protein modifications. Its importance has been established not only for eukaryotes but also for a variety of prokaryotic cellular processes, such as biofilm formation, motility, and mating. However, comprehensive glycoproteomic analyses are largely missing in prokaryotes. Here, we extend the phenotypic characterization of N-glycosylation pathway mutants in Haloferax volcanii and provide a detailed glycoproteome for this model archaeon through the mass spectrometric analysis of intact glycopeptides. Using in-depth glycoproteomic datasets generated for the wild-type (WT) and mutant strains as well as a reanalysis of datasets within the Archaeal Proteome Project (ArcPP), we identify the largest archaeal glycoproteome described so far. We further show that different N-glycosylation pathways can modify the same glycosites under the same culture conditions. The extent and complexity of the Hfx. volcanii N-glycoproteome revealed here provide new insights into the roles of N-glycosylation in archaeal cell biology.
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Yang, Lijun, Jie Liu, Hua Li, Yilian Liu, An He, Peiwu Huang, Weina Gao, Hua Cao, Ruilian Xu, and Ruijun Tian. "A fully integrated sample preparation strategy for highly sensitive intact glycoproteomics." Analyst 147, no. 5 (2022): 794–98. http://dx.doi.org/10.1039/d1an02166d.

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A fully integrated spintip-based glycoproteomic technology, termed Intact GlycoSISPROT, was developed for highly sensitive intact glycoproteome analysis with low microgram to nanogram level protein samples.
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Lu, Haojie, Ying Zhang, and Pengyuan Yang. "Advancements in mass spectrometry-based glycoproteomics and glycomics." National Science Review 3, no. 3 (April 21, 2016): 345–64. http://dx.doi.org/10.1093/nsr/nww019.

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Abstract Protein N-glycosylation plays a crucial role in a considerable number of important biological processes. Research studies on glycoproteomes and glycomes have already characterized many glycoproteins and glycans associated with cell development, life cycle, and disease progression. Mass spectrometry (MS) is the most powerful tool for identifying biomolecules including glycoproteins and glycans, however, utilizing MS-based approaches to identify glycoproteomes and glycomes is challenging due to the technical difficulties associated with glycosylation analysis. In this review, we summarize the most recent developments in MS-based glycoproteomics and glycomics, including a discussion on the development of analytical methodologies and strategies used to explore the glycoproteome and glycome, as well as noteworthy biological discoveries made in glycoproteome and glycome research. This review places special emphasis on China, where scientists have made sizeable contributions to the literature, as advancements in glycoproteomics and glycomincs are occurring quite rapidly.
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Mertz, Joseph L., Shisheng Sun, Bojiao Yin, Yingwei Hu, Rahul Bhattacharya, Michael J. Bettenbaugh, Kevin J. Yarema, and Hui Zhang. "Comparison of Three Glycoproteomic Methods for the Analysis of the Secretome of CHO Cells Treated with 1,3,4-O-Bu3ManNAc." Bioengineering 7, no. 4 (November 10, 2020): 144. http://dx.doi.org/10.3390/bioengineering7040144.

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Comprehensive analysis of the glycoproteome is critical due to the importance of glycosylation to many aspects of protein function. The tremendous complexity of this post-translational modification, however, makes it difficult to adequately characterize the glycoproteome using any single method. To overcome this pitfall, in this report we compared three glycoproteomic analysis methods; first the recently developed N-linked glycans and glycosite-containing peptides (NGAG) chemoenzymatic method, second, solid-phase extraction of N-linked glycoproteins (SPEG), and third, hydrophilic interaction liquid chromatography (HILIC) by characterizing N-linked glycosites in the secretome of Chinese hamster ovary (CHO) cells. Interestingly, the glycosites identified by SPEG and HILIC overlapped considerably whereas NGAG identified many glycosites not observed in the other two methods. Further, utilizing enhanced intact glycopeptide identification afforded by the NGAG workflow, we found that the sugar analog 1,3,4-O-Bu3ManNAc, a “high flux” metabolic precursor for sialic acid biosynthesis, increased sialylation of secreted proteins including recombinant human erythropoietin (rhEPO).
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Vivekanandan-Giri, Anuradha, Jessica L. Slocum, Carolyn L. Buller, Venkatesha Basrur, Wenjun Ju, Rodica Pop-Busui, David M. Lubman, Matthias Kretzler, and Subramaniam Pennathur. "Urine Glycoprotein Profile Reveals Novel Markers for Chronic Kidney Disease." International Journal of Proteomics 2011 (October 10, 2011): 1–18. http://dx.doi.org/10.1155/2011/214715.

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Chronic kidney disease (CKD) is a significant public health problem, and progression to end-stage renal disease leads to dramatic increases in morbidity and mortality. The mechanisms underlying progression of disease are poorly defined, and current noninvasive markers incompletely correlate with disease progression. Therefore, there is a great need for discovering novel markers for CKD. We utilized a glycoproteomic profiling approach to test the hypothesis that the urinary glycoproteome profile from subjects with CKD would be distinct from healthy controls. N-linked glycoproteins were isolated and enriched from the urine of healthy controls and subjects with CKD. This strategy identified several differentially expressed proteins in CKD, including a diverse array of proteins with endopeptidase inhibitor activity, protein binding functions, and acute-phase/immune-stress response activity supporting the proposal that inflammation may play a central role in CKD. Additionally, several of these proteins have been previously linked to kidney disease implicating a mechanistic role in disease pathogenesis. Collectively, our observations suggest that the human urinary glycoproteome may serve as a discovery source for novel mechanism-based biomarkers of CKD.
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Sharma, Ashok, James Cox, Joshua Glass, Tae Jin Lee, Sai Karthik Kodeboyina, Wenbo Zhi, Lane Ulrich, Zachary Lukowski, and Shruti Sharma. "Serum Glycoproteomic Alterations in Patients with Diabetic Retinopathy." Proteomes 8, no. 3 (September 13, 2020): 25. http://dx.doi.org/10.3390/proteomes8030025.

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The precise molecular mechanisms of diabetic retinopathy (DR) pathogenesis are unclear, and treatment options are limited. There is an urgent need to discover and develop novel therapeutic targets for the treatment of this disease. Glycosylation is a post-translational modification that plays a critical role in determining protein structure, function, and stability. Recent studies have found that serum glycoproteomic changes are associated with the presence or progression of several inflammatory diseases. However, very little is known about the glycoproteomic changes associated with DR. In this study, glycoproteomic profiling of the serum of diabetic patients with and without DR was performed. A total of 15 glycopeptides from 11 glycoproteins were found to be significantly altered (5 upregulated and 10 downregulated) within the serum glycoproteome of DR patients. These glycoproteins are known to be involved in the maintenance of the extracellular matrix and complement system through peptidolytic activity or regulation.
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Nilsson, Jonas, Adnan Halim, Ammi Grahn, and Göran Larson. "Targeting the glycoproteome." Glycoconjugate Journal 30, no. 2 (August 11, 2012): 119–36. http://dx.doi.org/10.1007/s10719-012-9438-6.

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Phung, Toan K., Cassandra L. Pegg, and Benjamin L. Schulz. "GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis." Beilstein Journal of Organic Chemistry 16 (September 1, 2020): 2127–35. http://dx.doi.org/10.3762/bjoc.16.180.

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Mass spectrometry glycoproteomics is rapidly maturing, allowing unprecedented insights into the diversity and functions of protein glycosylation. However, quantitative glycoproteomics remains challenging. We developed GlypNirO, an automated software pipeline which integrates the complementary outputs of Byonic and Proteome Discoverer to allow high-throughput automated quantitative glycoproteomic data analysis. The output of GlypNirO is clearly structured, allowing manual interrogation, and is also appropriate for input into diverse statistical workflows. We used GlypNirO to analyse a published plasma glycoproteome dataset and identified changes in site-specific N- and O-glycosylation occupancy and structure associated with hepatocellular carcinoma as putative biomarkers of disease.
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Chernykh, Anastasia, Rebeca Kawahara, and Morten Thaysen-Andersen. "Towards structure-focused glycoproteomics." Biochemical Society Transactions 49, no. 1 (January 13, 2021): 161–86. http://dx.doi.org/10.1042/bst20200222.

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Facilitated by advances in the separation sciences, mass spectrometry and informatics, glycoproteomics, the analysis of intact glycopeptides at scale, has recently matured enabling new insights into the complex glycoproteome. While diverse quantitative glycoproteomics strategies capable of mapping monosaccharide compositions of N- and O-linked glycans to discrete sites of proteins within complex biological mixtures with considerable sensitivity, quantitative accuracy and coverage have become available, developments supporting the advancement of structure-focused glycoproteomics, a recognised frontier in the field, have emerged. Technologies capable of providing site-specific information of the glycan fine structures in a glycoproteome-wide context are indeed necessary to address many pending questions in glycobiology. In this review, we firstly survey the latest glycoproteomics studies published in 2018–2020, their approaches and their findings, and then summarise important technological innovations in structure-focused glycoproteomics. Our review illustrates that while the O-glycoproteome remains comparably under-explored despite the emergence of new O-glycan-selective mucinases and other innovative tools aiding O-glycoproteome profiling, quantitative glycoproteomics is increasingly used to profile the N-glycoproteome to tackle diverse biological questions. Excitingly, new strategies compatible with structure-focused glycoproteomics including novel chemoenzymatic labelling, enrichment, separation, and mass spectrometry-based detection methods are rapidly emerging revealing glycan fine structural details including bisecting GlcNAcylation, core and antenna fucosylation, and sialyl-linkage information with protein site resolution. Glycoproteomics has clearly become a mainstay within the glycosciences that continues to reach a broader community. It transpires that structure-focused glycoproteomics holds a considerable potential to aid our understanding of systems glycobiology and unlock secrets of the glycoproteome in the immediate future.
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Liu, Jing, Fangjun Wang, Hui Lin, Jun Zhu, Yangyang Bian, Kai Cheng, and Hanfa Zou. "Monolithic Capillary Column Based Glycoproteomic Reactor for High-Sensitive Analysis of N-Glycoproteome." Analytical Chemistry 85, no. 5 (February 20, 2013): 2847–52. http://dx.doi.org/10.1021/ac400315n.

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Dissertations / Theses on the topic "Glycoproteome"

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Zielinska, Dorota. "Unveiling the eukaryotic N-glycoproteome." Diss., Ludwig-Maximilians-Universität München, 2011. http://nbn-resolving.de/urn:nbn:de:bvb:19-166063.

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Zielinska, Dorota [Verfasser], and Matthias [Akademischer Betreuer] Mann. "Unveiling the eukaryotic N-glycoproteome / Dorota Zielinska. Betreuer: Matthias Mann." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2011. http://d-nb.info/1047543605/34.

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Huang, Peiwu. "Method development and application for spatial proteome and glycoproteome profiling." HKBU Institutional Repository, 2020. https://repository.hkbu.edu.hk/etd_oa/788.

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Tissues are heterogeneous ecosystems comprised of various cell types. For example, in tumor tissues, malignant cancer cells are surround by various non-malignant stromal cells. Proteins, especially N-linked glycoproteins, are key players in tumor microenvironment and respond to many extracellular stimuli for involving and regulating intercellular signaling. Understanding the human proteome and glycoproteome in heterogeneous tissues with spatial resolution are meaningful for exploring intercellular signaling networks and discovering protein biomarkers for various diseases, such as cancer. In this study, we aimed to develop new liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based analytical methods for spatially-resolved proteome and glycoproteome profiling in tissue samples, and apply them for profiling potential biomarkers for pancreatic cancer. We first systematically and synchronously optimized the LC-MS parameters to increase peptide sequencing efficiency in data dependent proteomics. Taking advantage of its hybrid instrument design with various mass analyzer and fragmentation strageties, the Orbitrap Fusion mass spectrometer was used for systematically comparing the popular high-high approach by using orbitrap for both MS1 and MS2 scans and high-low approach by using orbitrap for MS1 scan and ion trap for MS2 scans. High-high approach outperformed high-low approach in terms of better saturation of the scan cycle and higher MS2 identification rate. We then systematically optimized various MS parameters for high-high approach. We investigated the influence of isolation window and injection time on scan speed and MS2 identification rate. We then explored how to properly set dynamic exclusion time according to the chromatography peak width. Furthermore, we found that the orbitrap analyzer, rather than the analytical column, was easily saturated with higher peptide loading amount, thus limited the dynamic range of MS1-based quantification. Finally, by using the optimized LC-MS parameters, more than 9000 proteins and 110,000 unique peptides were identified by using 10 hours of effective LC gradient time. The study therefore illustrated the importance of synchronizing LC-MS precursor targeting and high-resolution fragment detection for high-efficient data dependent proteomics. Understanding the tumor heterogeneity through spatially resolved proteome profiling is meaningful for biomedical research. Laser capture microdissection (LCM) is a powerful technology for exploring local cell populations without losing spatial information. Here, we designed an immunohistochemistry (IHC)-based workflow for cell type-resolved proteome analysis of tissue samples. Firstly, targeted cell type was stained by IHC using antibody targeting cell-type specific marker to improve accuracy and efficiency of LCM. Secondly, to increase protein recovery from chemically crosslinked IHC tissues, we optimized a decrosslinking procedure to seamlessly combine with the integrated spintip-based sample preparation technology SISPROT. This newly developed approach, termed IHC-SISPROT, has comparable performance with traditional H&E staining-based proteomic analysis. High sensitivity and reproducibility of IHC-SISPROT was achieved by combining with data independent proteomic analysis. This IHC-SISPROT workflow was successfully applied for identifying 6660 and 6052 protein groups from cancer cells and cancer- associated fibroblasts (CAFs) by using only 5 mm 2 and 12 μm thickness of hepatocellular carcinoma tissue section. Bioinformatic analysis revealed the enrichment of cell type-specific ligands and receptors and potentially new communications between cancer cells and CAFs by these signaling proteins. Therefore, IHC-SISPROT is sensitive and accurate proteomic approach for spatial profiling of cell type-specific proteome from tissues. N-linked glycoproteins are promising candidates for diagnostic and prognostic biomarkers and therapeutic targets. They often locate at plasma membrane and extracellular space with distinct cell type distribution in tissue microenvironment. Due to access to only low microgram of proteins and low abundance of glycoproteins in tissue sections harvested by LCM, region- and cell type-resolved glycoproteome analysis of tissue sections remains challenging. Here we designed a fully integrated spintip-based glycoproteomic approach (FISGlyco) which achieved all the steps for glycoprotein enrichment, digestion, deglycosylation and desalting in a single spintip device. Sample loss is significantly reduced and the total processing time is reduced to 4 hours, while detection sensitivity and label-free quantification precision is greatly improved. 607 N-glycosylation sites were successfully identified and quantified from only 5 μg of mouse brain proteins. By seamlessly combining with LCM, the first region-resolved N-glycoproteome profiling of four mouse brain regions, including isocortex, hippocampus, thalamus, and hypothalamus, was achieved, with 1,875, 1,794, 1,801, and 1,417 N-glycosites identified, respectively. Our approach could be a generic approach for region and even cell type specific glycoproteome analysis of tissue sections. Pancreatic ductal adenocarcinoma (PDAC) is a devastating disease with five year survival rate of around 8%. No effective biomarkers and targeted therapy are one of the major reasons for this urgent clinical situation. To explore potential protein biomarkers and drug targets located at intercellular space of pancreatic tumor microenvironment, we established chemical proteomic approach for deep glycoproteome profiling of PDAC clinical tissue samples based on the above- mentioned new proteomic methods. Taking advantage of a long chain biotin- hydrazide probe with less space hindrance, the new method outperformed traditional hydrazide chemistry method in terms of sensitivity, time efficiency and glycoproteome coverage. The method was successfully applied to enrich and validate LIF and its receptors as potential biomarkers for PDAC. In addition, to explore the full map of pancreatic tumor microenvironment glycoproteome with diagnostic and therapeutic values, we collected 114 pancreatic tissues, including 30 PDAC tumor tissues, 30 adjacent non-tumor (NT) tissues, 32 chronic pancreatitis tissues and 22 normal pancreatic tissues, and systematically profiled their glycoprotein expression pattern by using the developed glycoproteomic strategy. The deepest glycoproteome of PDAC was achieved, which covered the majority of previously reported glycoprotein biomarkers and drug targets for PDAC. Importantly, we discovered many new glycoproteins with differential expression in PDAC and normal tissue types. Moreover, LCM-based cell-type proteome profiling was achieved for 13 PDAC tissue samples, which covered more than 8000 proteins for both pancreatic stromal cells and pancreatic cancer cells in each sample. We therefore provided a valuable resource for screening novel and cancer specific glycoprotein biomarkers for pancreatic cancer with spatial resolution
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Murrey, Heather Elizabeth Dougherty Dennis A. Hsieh-Wilson Linda C. "Identification and characterization of the plasticity-relevant fucose-alpha(1-2)galactose glycoproteome from mouse brain /." Diss., Pasadena, Calif. : Caltech, 2009. http://resolver.caltech.edu/CaltechETD:etd-12182008-145714.

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Kalxdorf, Mathias [Verfasser]. "Mass spectrometric methods for measuring dynamic processes, drug-induced effects and target engagement on the cell surface glycoproteome / Mathias Kalxdorf." Halle, 2018. http://d-nb.info/1166140695/34.

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Ji, Yanlong [Verfasser], Volker [Gutachter] Dötsch, and Thomas [Gutachter] Oellerich. "Quantitative N-glycoproteome, phosphoproteome and ubiquitinome analyses for studying B-cell receptor signaling in B-cell lymphoma / Yanlong Ji ; Gutachter: Volker Dötsch, Thomas Oellerich." Frankfurt am Main : Universitätsbibliothek Johann Christian Senckenberg, 2021. http://d-nb.info/1234680874/34.

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Weaver, Danielle. "N-linked glycosylation in Campylobacter jejuni and Campylobacter fetus and N-linked glycans as targets for antibody-based detection." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/nlinked-glycosylation-in-campylobacter-jejuni-and-campylobacter-fetus-and-nlinked-glycans-as-targets-for-antibodybased-detection(2b739b0d-84a3-47cc-af7a-d915b4caf37c).html.

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Campylobacter spp., especially C. jejuni and C. coli, are the leading cause of bacterial gastroenteritis in Europe. There is a recognised need to develop detection tools which can be performed on farms to facilitate reducing the presence of Campylobacter in poultry. A similar application could be beneficial for detection of C. fetus, a veterinary pathogen which causes significant economic loss in the cattle industry. Campylobacter species perform protein N-linked glycosylation and in C. jejuni at least 150 proteins, many of which are surface-exposed, may be modified. Therefore, the first portion of this thesis investigated the feasibility of using N-linked glycans as targets for antibody-based detection of Campylobacter species. To do this, a His-tagged N-glycoprotein was expressed and purified from C. fetus and used as immunogen to raise an antiserum termed CfNgp. The Campylobacter N-glycan reactivity of this antiserum was characterised and it was shown to react with N-glycoproteins and cells of C. fetus and other emerging Campylobacter species such as C. concisus. Immunoblotting techniques and flow cytometry were used to characterise an antiserum (CjNgp) raised against a C. jejuni N-linked glycoprotein and demonstrated that it can specifically detect cells of C. jejuni, C. coli and other emerging Campylobacter species found in poulty. This thesis also describes the investigation of the relatively uncharacterised C. fetus N-linked glycosylation system. Functional analysis of C. fetus predicted glycosyltransferases was acheived by developing glycocompetent E. coli containing a hybrid C. jejuni/C. fetus pgl system. The N-glycan structures biosynthesised were analysed using mass spectrometry and this novel approach discovered the activity of two C. fetus glycosyltransferase enzymes. Finally, this work used a bioinformatics pipeline to produce a C. fetus predicted N-linked glycoproteome and experimentally verified a newly identified N-linked glycoprotein. This pipeline was also applied to investigate the putative conservation of N-linked glycoproteins throughout the Campylobacter genus and highlighted ‘core’ N-linked glycoproteins which are key targets for experimental investigation. Overall, this work demonstrates that Campylobacter N-linked glycans are attractive targets for antibody-based detection, expands our knowledge of C. fetus N-linked glycosylation and contributes to the broader understanding of this intriguing aspect of Campylobacter biology.
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Wu, Gang. "Glycomic and glycoproteomic studies of immune disorders." Thesis, Imperial College London, 2014. http://hdl.handle.net/10044/1/42776.

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Sugar oligomers which are linked to proteins and lipids play important roles in a large number of biological processes. These sugars are referred to as glycans. In the immune system, almost all key proteins are glycosylated. Glycans regulate the migration, recognition, activation, and apoptosis of immune cells, as well as the activities of antibodies. Owing to glycan complexity, the study of glycosylation is challenging. Mass spectrometry (MS) is a state-of-the-art technology which is ideally suited to investigating glycosylation, because of its ultra-high sensitivity and resolution, as well as its ability to analyze individual molecules in a complex, heterogeneous mixture. In this thesis, mass spectrometry was used to investigate the abnormal glycosylation of two newly discovered immune disorders: a hyper IgE syndrome and a congenital disorder of glycosylation (CDG). In the hyper IgE syndrome, a total set of glycans on leukocytes was analysed (glycomic studies). A reduction in tri- and tetra-antennary glycans was observed in the patients. In addition, substantially increased levels of hybrid glycans were detected in a patient with more severe symptoms, and decreased fucosylation was found on their neutrophils. Site specific glycosylation analysis (glycoproteomic studies) was done on IgE, and 6 of 7 potential N-glycosylation sites on this antibody were mapped, which did not show significant glycosylation changes. In the CDG, tri-glucosylated high mannose glycans were observed, which helped the identification of an ER glucosidase I defect. Mass spectrometry was also used to investigate engineered antibodies which are designed to treat immune disorders. A dramatic increase in sialylation was observd in an IgG1 after introducing point mutations in the Fc region, and a considerable amount of high mannose glycans were detected in an IgG1 hexamer.
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Cotton, Sofia Ribeiro. "Glycoproteomic characterization of advanced bladder cancer towards novel therapies." Master's thesis, Universidade de Aveiro, 2016. http://hdl.handle.net/10773/17366.

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Mestrado em Biologia Molecular e Celular
A heterogenidade da natureza molecular dos tumores de bexiga tem dificultado o estabelecimento de abordagens no campo da medicina de precisão, revelando-se a necessidade de terapias mais eficientes e novas ferramentas de detecção não-invasivas. Contudo, têm-se denotado um desenvolvimento no estudo da carcinogénese de bexiga e na progressão do tumor, acompanhado de profundas alterações na glicosilação de proteínas que, dada a sua superfície celular e a natureza secretada, apresenta um potencial elevado na melhoria da gestão da doença. Segundo esta abordagem foi efectuado um estudo sobre tumores de bexiga de diferentes naturezas clinicopatológicas para O-glicanos de cadeia curta, regularmente encontrados na maioria dos tumores sólidos, recorrendo-se à imunohistoquímica. O estudo incluiu os antígenos Tn e T e os seus homólogos sialilados sialil-Tn (STn) e sialil-T (ST), geralmente associados com um mau prognóstico. Explorou-se ainda a sialilação da natureza dos antigénios T, especificamente as sialoformas sialil-3-T (S3T) e sialil-6-T (S6T), com base em combinações de tratamentos enzimáticos. Observou-se uma predominância de sialoglicanos, em comparação com as glicoformas neutras (antígenos Tn e T) em tumores de bexiga. Em particular, o antigénio STn foi associado ao estado avançado da doença e invasão muscular. Os antígenos S3T e S6T foram detectados pela primeira vez em tumores de bexiga, estando ausentes no urotélio normal, permitindo destacar a natureza específica em tumores. Verificou-se também a sobreexpressão dos glicanos em lesões avançadas, especialmente nos casos com invasão muscular.As análises glicoproteómicas dos tumores avançados de bexiga permitiram identificar diversas glicoproteínas-chave associadas ao cancro (MUC16, CD44, integrinas), denotando uma glicosilação alterada.As glicoformas da MUC16 STN positivas, características do cancro de ovário, encontram-se num subconjunto de tumores de bexiga em estado avançado, com um pior prognóstico. Em suma, os tumores de bexiga apresentam severas alterações no O-glicoma e no Oglicoproteoma devendo ser abordados de forma abrangente com o objectivo de desenvolver ferramentas de diagnóstico não invasivas e terapias dirigidas. As glicoformas aberrantes de MUC16 apresentam potencial como biomarcadores de mau prognóstico. Este trabalho estabeleceu um guia para a descoberta de glicobiomarcadores no cancro de bexiga, que pode ser utilizado para a estratificação dos pacientes e, por fim, levar à descoberta de novos alvos terapêuticos.
The heterogeneous molecular nature of bladder tumours has hampered the establishment of precision medicine approaches, more efficient therapeutics and novel non-invasive detection tools. Still, it has been long described that bladder carcinogenesis and tumour progression is accompanied by profound alterations in protein glycosylation which, given its cell surface and secreted nature, holds tremendous potential for disease management improvement. Therefore, we have screened series of bladder tumours of different clinicopathological natures for short-chain O-glycans, found in most solid tumours, by immunohistochemistry. These included the Tn and T antigens and their sialylated counterparts sialyl-Tn (STn) and sialyl-T(ST), generally associated with poor prognosis. We have also explored the nature of T antigens sialylation, namely the sialyl-3-T(S3T) and sialyl-6-T(S6T) sialoforms, based on combinations of enzymatic treatments. We observed a predominance of sialoglycans over neutral glycoforms (Tn and T antigens) in bladder tumours. In particular, the STn antigen was associated with high-grade disease and muscle invasion, in accordance with our previous observations.The S3T and S6T antigens were detected for the first time in bladder tumours, but not in healthy urothelia, highlighting their cancer-specific nature. These glycans were also overexpressed in advanced lesions, especially in cases showing muscle invasion. Glycoproteomic analyses of advanced bladder tumours identified several key cancer-associated glycoproteins (MUC16, CD44, integrins) carrying altered glycosylation. Particular interest was devoted to MUC16 STn+-glycoforms, characteristic of ovarian cancers, which were found in a subset of advanced stage bladder tumours facing worst prognosis. In summary, bladder tumours present severe O-glycome and O-glycoproteome alterations that should be comprehensively addressed envisaging novel non-invasive diagnostic tools and targeted therapeutics. Furthermore, abnormal MUC16 glycoforms holds potential as surrogate biomarkers of poor prognosis. Finally, this work established a roadmap for glycobiomarker discovery in bladder cancer, which may be used for patient stratification and ultimately lead to novel therapeutic targets.
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Estrella, Ruby Poblete Graduate School of Biomedical Engineering Faculty of Engineering UNSW. "A glycoproteomic approach to the structural characterization of acidic glycoproteins." Publisher:University of New South Wales. Graduate School of Biomedical Engineering, 2009. http://handle.unsw.edu.au/1959.4/43562.

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Glycoproteins, and their subset proteoglycans, are an important group of molecules in joint tissues, providing crucial functions such as cartilage structural integrity and lubrication at cartilage surfaces. The functionality of these glycoproteins is attributable to their oligosaccharide components, however surprisingly little is known about their fine structural details. With the use of glycoproteomic methods, this thesis presents the development and incorporation of mass spectrometric, biochemical and immunological methods to elucidate glycoprotein structures in synovial fluids, chondrocytes and synoviocytes in order to provide insight into how their structures may contribute to their functions. Initially, anion exchange chromatography was used to extract the acidic fraction containing glycoproteins and proteoglycans in arthritic synovial fluid (SF) samples, followed by proteomic analysis to identify the main glycoproteins in 1D-SDS-PAGE gels. To complement these findings, an in-gel enzymatic digest method for glycosaminoglycan (GAG) and oligosaccharide analysis was developed for analysis of glycoproteins by graphitised carbon liquid chromatography mass spectrometry (LC-MS). Further characterization of the major glycoprotein, lubricin, was pursued by investigating its interactions with the surrounding extracellular matrix (ECM) from its cellular sources and characterising the secreted lubricin with Western blot and proteomic analysis. Finally, the graphitised carbon LC-MS method was applied to analyse the overall glycosylation profiles of lubricin. The major glycoprotein found in arthritic synovial fluid was lubricin, as identified by peptide LC-MS and Western blot. Graphitised carbon LC-MS identified the major chondroitin sulfate (CS) repeat region disaccharides and linkage region oligosaccharides of aggrecan with confirmation through tandem mass spectra and Western blots using CS linkage region stub antibodies. Application of this method to lubricin led to the discovery of O-linked oligosaccharide structures which were previously undescribed for lubricin. A higher proportion of sialylated oligosaccharide structures were detected in the rheumatoid arthritis (RA) samples compared to the osteoarthritic (OA) samples, which signifies a diagnostic difference between these diseases. Sulfated oligosaccharide structures were also detected on synovial fluid lubricin, correlated with Western blot reactivity with the MECA-79 antibody, thus suggesting a role for lubricin in inflammation. Overall the results demonstrated that glycosylation structure indicates additional functional properties for the glycoproteins such as lubricin.
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Book chapters on the topic "Glycoproteome"

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Hanisch, Franz-Georg, and Stefan Müller. "Approaches to the O-Glycoproteome." In The Proteomics Protocols Handbook, 439–57. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1385/1-59259-890-0:439.

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Pan, Sheng. "Quantitative Glycoproteomics for N-Glycoproteome Profiling." In Shotgun Proteomics, 379–88. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0685-7_25.

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Campbell, Matthew P., Robyn A. Peterson, Elisabeth Gasteiger, Julien Mariethoz, Frederique Lisacek, and Nicolle H. Packer. "Navigating the Glycome Space and Connecting the Glycoproteome." In Protein Bioinformatics, 139–58. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6783-4_7.

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Cao, Qichen, Qing Zhao, Xiaohong Qian, and Wantao Ying. "Identification of Core-Fucosylated Glycoproteome in Human Plasma." In Methods in Molecular Biology, 127–37. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5_10.

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Santorelli, Lucia, Elisa Barigazzi, M. Pitto, and F. Raimondo. "Investigation of the N-Glycoproteome in the Urinary Exosomes: Technical Challenges." In Toxic Chemical and Biological Agents, 257–58. Dordrecht: Springer Netherlands, 2020. http://dx.doi.org/10.1007/978-94-024-2041-8_26.

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Kalxdorf, Mathias, Hans Christian Eberl, and Marcus Bantscheff. "Monitoring Dynamic Changes of the Cell Surface Glycoproteome by Quantitative Proteomics." In Methods in Molecular Biology, 47–59. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7201-2_3.

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Adav, Sunil S., and Siu Kwan Sze. "Simultaneous Enrichment of Plasma Extracellular Vesicles and Glycoproteome for Studying Disease Biomarkers." In Methods in Molecular Biology, 193–201. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7057-5_15.

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Krois, Daniel. "Glycokonjugate, Glycoproteine." In Organisch-chemische Methoden, 75–83. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-53013-9_5.

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Xiao, Haopeng, George X. Tang, Weixuan Chen, and Ronghu Wu. "A Boronic Acid-Based Enrichment for Site-Specific Identification of the N-glycoproteome Using MS-Based Proteomics." In Analysis of Post-Translational Modifications and Proteolysis in Neuroscience, 31–41. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/7657_2015_94.

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Hao, Piliang, Huoming Zhang, and Siu Kwan Sze. "Application of Electrostatic Repulsion Hydrophilic Interaction Chromatography to the Characterization of Proteome, Glycoproteome, and Phosphoproteome Using Nano LC–MS/MS." In Methods in Molecular Biology, 305–18. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-319-6_23.

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Conference papers on the topic "Glycoproteome"

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Flores, Ricardo J., Yiting Li, Serrine S. Lau, Eastwood Leung, Ching C. Lau, and Tsz-Kwong Man. "Abstract 5570: An affinity lectin chromatography approach to characterize N-linked glycoproteome in metastatic osteosarcoma." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5570.

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Arampatzidou, Maria, Majlinda Kullolli, and Sharon J. Pitteri. "Abstract 2489: Glycoproteomic analysis of breast cancer cell lines for biomarker discovery." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2489.

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Miyoshi, Eiji, Kanako Azuma, Shinji Takamatsu, Naoko Terao, Satoshi Serada, Tetsuji Naka, and Yoshihiro Kamada. "Abstract 1407: Identification of sialylated glycoproteins in doxorubicin-treated hepatoma cells with glycoproteomic analyses." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1407.

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Block, Timothy M. "Abstract CN01-02: Glycoproteomic discovery of liver cancer biomarkers: Be careful how you use it!" In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-cn01-02.

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Miyamoto, Suzanne, Ken Yoneda, Renee Ruhaak, Carol Stroble, Carlito B. Lebrilla, and David Gandara. "Abstract 4804: Glycoproteomic analysis of lung cancer malignant pleural effusions identify glycosylated proteins being produced by metastatic tumor cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4804.

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Lindpaintner, Klaus, Apoorva Srinivasan, Alan Mitchell, Apurva Dixit, Gege Xu, Xin Cong, and Daniel Serie. "158 A novel, highly accurate liquid biopsy-based glycoproteomic predictor of checkpoint inhibitor treatment benefit in advanced non-small cell lung cancer." In SITC 37th Annual Meeting (SITC 2022) Abstracts. BMJ Publishing Group Ltd, 2022. http://dx.doi.org/10.1136/jitc-2022-sitc2022.0158.

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Ueda, Koji, Hidewaki Nakagawa, Naomi Saichi, Masaru Katsumata, Taka-Aki Sato, and Yusuke Nakamura. "Abstract 5568: Development of serum glycoproteomic profiling technology for the identification of pancreatic cancer biomarkers: simultaneous identification of glycosylation sites and site-specific quantification of glycan structure changes." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5568.

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