High sensitivity glycomics in biomedicine

Lageveen-Kammeijer, Guinevere S. M.; Küster, Bernhard; Reusch, Dietmar; Wuhrer, Manfred

doi:10.1002/mas.21730

Cited by 13 publications

(7 citation statements)

References 196 publications

(265 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Yet, tissue heterogeneity poses a problem for glycomic and transcriptomic analysis as it masks cell specific signatures. Dissecting specific regions of the tissue by LCM, largely overcomes this issue and enables analysis of glycomic signatures from specific cells of interest 62 . We succeeded in the in-depth O -glycome analysis from a limited amount (20,000 - 25,000) of FFPE tissue-derived cells, which opens up the potential to use this workflow for future glyco-biomarker discovery in other types of tumors.…”

Section: Resultsmentioning

confidence: 99%

Specific (sialyl-)Lewis core 2 O-glycans differentiate colorectal cancer from healthy colon epithelium

et al. 2022

Self Cite

View full text Add to dashboard Cite

Cells are covered with a dense layer of carbohydrates, some of which are solely present on neoplastic cells. The so-called tumor-associated carbohydrate antigens (TACAs) are increasingly recognized as promising targets for immunotherapy. These carbohydrates differ from those of the surrounding non-cancerous tissues and contribute to the malignant phenotype of the cancer cells by promoting proliferation, metastasis, and immunosuppression. However, due to tumor tissue heterogeneity and technological limitations, TACAs are insufficiently explored. Methods: A workflow was established to decode the colorectal cancer (CRC)-associated O -linked glycans from approximately 20,000 cell extracts. Extracts were obtained through laser capture microdissection of formalin fixed paraffin embedded tissues of both primary tumors and metastatic sites, and compared to healthy colon mucosa from the same patients. The released O -glycans were analyzed by porous graphitized carbon liquid chromatography-tandem mass spectrometry in negative ion mode. Results: Distinctive O -glycosylation features were found in cancerous, stromal and normal colon mucosal regions. Over 100 O -linked glycans were detected in cancerous regions with absence in normal mucosa. From those, six core 2 O -glycans were exclusively found in more than 33% of the cancers, carrying the terminal (sialyl-)Lewis X/A antigen. Moreover, two O -glycans were present in 72% of the analyzed cancers and 94% of the investigated cancers expressed at least one of these two O -glycans. In contrast, normal colon mucosa predominantly expressed core 3 O -glycans, carrying α2-6-linked sialylation, (sulfo-)Lewis X/A and Sda antigens. Conclusion: In this study, we present a novel panel of highly specific TACAs, based upon differences in the glycomic profiles between CRC and healthy colon mucosa. These TACAs are promising new targets for development of innovative cancer immune target therapies and lay the foundation for the targeted treatment of CRC.

show abstract

Section: Resultsmentioning

confidence: 99%

Specific (sialyl-)Lewis core 2 O-glycans differentiate colorectal cancer from healthy colon epithelium

et al. 2022

Self Cite

View full text Add to dashboard Cite

show abstract

“…Glycosylation takes place in the individual cell, and the glycome by-and-large results directly from the organization of the metabolic glycosylation network in the cell. We cannot see the results of this process in a single cell using current structural analytics, and most of our understanding of the glycome stems from direct structural analysis of heterogeneous cell or tissue preparations, and thus informs us of an averaged snapshot of the glycan structures found in many cells ( Čaval et al., 2021 ; Khoo, 2019 ; Lageveen-Kammeijer et al., 2021 ; Levery et al., 2015 ; Thaysen-Andersen and Packer, 2014 ). An exception to this is the use of glycan-binding probes (lectins, antibodies, glycan-binding proteins) for binding to cells and tissues, and this approach, although limited by the number of specific probes to the majority of glycan structures ( Bojar et al., 2021 ), suggests that expression of select glycan structures can be highly regulated on cells during the cell cycle and during cellular maturation and differentiation ( Dabelsteen et al., 1991 ; Park et al., 2021 ; Thomas, 1971 ).…”

Section: Introductionmentioning

confidence: 99%

Applying transcriptomics to study glycosylation at the cell type level

2022

View full text Add to dashboard Cite

“…To capture the structural complexity and diversity of glycans, complementary techniques are often needed. In glycomic studies, glycans are released from glycoproteins (e.g., with peptide N‐glycosidase F for N‐glycans), usually derivatised and in general analysed by LC and MS methods for structural elucidation being accomplished by exoglycosidase sequencing and/or MS/MS analysis; while glycoproteomics is based on LC‐MS/MS methodologies (Chau et al., 2023; Chen et al., 2021; Kobeissy et al., 2022; Lageveen‐Kammeijer et al., 2022; Riley et al., 2021; Williams et al., 2018). Lectin‐based arrays (Saito et al., 2018; Williams et al., 2019; Yokose et al., 2020), lectin blotting and immunoblotting (Escrevente et al., 2011; Freitas et al., 2019; Gomes et al., 2015; Zhang et al., 2018) are also useful for characterising the EV glycome.…”

Section: Csf Ev Glycomic and Glycoproteomic Studiesmentioning

confidence: 99%

Recommendations for reproducibility of cerebrospinal fluid extracellular vesicle studies

Sandau,

Magaña,

Costa

et al. 2023

J of Extracellular Vesicle

View full text Add to dashboard Cite

Cerebrospinal fluid (CSF) is a clear, transparent fluid derived from blood plasma that protects the brain and spinal cord against mechanical shock, provides buoyancy, clears metabolic waste and transports extracellular components to remote sites in the brain. Given its contact with the brain and the spinal cord, CSF is the most informative biofluid for studies of the central nervous system (CNS). In addition to other components, CSF contains extracellular vesicles (EVs) that carry bioactive cargoes (e.g., lipids, nucleic acids, proteins), and that can have biological functions within and beyond the CNS. Thus, CSF EVs likely serve as both mediators of and contributors to communication in the CNS. Accordingly, their potential as biomarkers for CNS diseases has stimulated much excitement for and attention to CSF EV research. However, studies on CSF EVs present unique challenges relative to EV studies in other biofluids, including the invasive nature of CSF collection, limited CSF volumes and the low numbers of EVs in CSF as compared to plasma. Here, the objectives of the International Society for Extracellular Vesicles CSF Task Force are to promote the reproducibility of CSF EV studies by providing current reporting and best practices, and recommendations and reporting guidelines, for CSF EV studies. To accomplish this, we created and distributed a world‐wide survey to ISEV members to assess methods considered ‘best practices’ for CSF EVs, then performed a detailed literature review for CSF EV publications that was used to curate methods and resources. Based on responses to the survey and curated information from publications, the CSF Task Force herein provides recommendations and reporting guidelines to promote the reproducibility of CSF EV studies in seven domains: (i) CSF Collection, Processing, and Storage; (ii) CSF EV Separation/Concentration; (iii) CSF EV Size and Number Measurements; (iv) CSF EV Protein Studies; (v) CSF EV RNA Studies; (vi) CSF EV Omics Studies and (vii) CSF EV Functional Studies.

show abstract

High sensitivity glycomics in biomedicine

Cited by 13 publications

References 196 publications

Specific (sialyl-)Lewis core 2 O-glycans differentiate colorectal cancer from healthy colon epithelium

Specific (sialyl-)Lewis core 2 O-glycans differentiate colorectal cancer from healthy colon epithelium

Applying transcriptomics to study glycosylation at the cell type level

Recommendations for reproducibility of cerebrospinal fluid extracellular vesicle studies

Contact Info

Product

Resources

About