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Cells
Special Issues
Glycoproteomics and Protein Glycosylation in Cell Biology and Diseases
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Glycoproteomics and Protein Glycosylation in Cell Biology and Diseases

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Metabolism".

Deadline for manuscript submissions: closed (30 April 2024) | Viewed by 6335

Special Issue Editor

Dr. Sheng Pan

E-Mail Website
Guest Editor
The Brown Foundation Institute of Molecular Medicine, The University of Texas Health Science Center at Houston, Houston, TX, USA
Interests: proteomics; glycoproteomics; PTM characterization; mass spectrometry; pancreatic cancer
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Most secretory and membrane-bound proteins produced by mammalian cells contain covalently linked glycans with diverse structures. They play a pivotal role in many biological processes, such as protein folding, cell adhesion and trafficking, cell signaling, pathogen recognition, and immune response. Glycan synthesis is not template bound but involves the concerted action of glycosidases, glycosyltransferases, and glycan-modifying enzymes. Environmental factors and immune pressure can lead to genetic and epigenetic modification of these enzymes and result in altered glycan biosynthesis and protein glycosylation, leading to abnormal biological conditions and various diseases, including cancer. Many disease biomarkers are glycoproteins or glycosylation assays. With the recent advances in glycoproteomics and other glyco-technology, studies ranging from interrogation of molecular mechanisms at cellular, organelle, and other subcellular levels to characterization of various clinical specimens for biomarker discovery have been driving many new discoveries and hypotheses in glycobiology and disease study. In this Special Issue, we welcome submissions of original research or review articles aiming at the broad field of glycobiology and glycoproteomics in studying the implication of protein glycosylation in cell biology and diseases.

Dr. Sheng Pan
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • glycosylation 
  • glycoproteomics 
  • proteomics 
  • mass spectrometry 
  • glycobiology 
  • glycan 
  • glycomics 
  • lectin

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Published Papers (2 papers)

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Research

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22 pages, 3017 KiB  
Article
Glycation Interferes with the Expression of Sialyltransferases and Leads to Increased Polysialylation in Glioblastoma Cells
by Paola Schildhauer, Philipp Selke, Martin S. Staege, Anja Harder, Christian Scheller, Christian Strauss, Rüdiger Horstkorte, Maximilian Scheer and Sandra Leisz
Cells 2023, 12(23), 2758; https://doi.org/10.3390/cells12232758 - 2 Dec 2023
Cited by 2 | Viewed by 2049
Abstract
Glioblastoma (GBM) is a highly aggressive brain tumor that often utilizes aerobic glycolysis for energy production (Warburg effect), resulting in increased methylglyoxal (MGO) production. MGO, a reactive dicarbonyl compound, causes protein alterations and cellular dysfunction via glycation. In this study, we investigated the [...] Read more.
Glioblastoma (GBM) is a highly aggressive brain tumor that often utilizes aerobic glycolysis for energy production (Warburg effect), resulting in increased methylglyoxal (MGO) production. MGO, a reactive dicarbonyl compound, causes protein alterations and cellular dysfunction via glycation. In this study, we investigated the effect of glycation on sialylation, a common post-translational modification implicated in cancer. Our experiments using glioma cell lines, human astrocytes (hA), and primary glioma samples revealed different gene expressions of sialyltransferases among cells, highlighting the complexity of the system. Glycation has a differential effect on sialyltransferase expression, upregulating ST8SIA4 in the LN229 and U251 cell lines and decreasing the expression in normal hA. Subsequently, polysialylation increased in the LN229 and U251 cell lines and decreased in hA. This increase in polysialylation could lead to a more aggressive phenotype due to its involvement in cancer hallmark processes such as immune evasion, resistance to apoptosis, and enhancing invasion. Our findings provide insights into the mechanisms underlying GBM aggressiveness and suggest that targeting glycation and sialylation could be a potential therapeutic strategy. Full article
(This article belongs to the Special Issue Glycoproteomics and Protein Glycosylation in Cell Biology and Diseases)
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Review

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33 pages, 3802 KiB  
Review
O-GlcNAc Dynamics: The Sweet Side of Protein Trafficking Regulation in Mammalian Cells
by Awatef Ben Ahmed, Quentin Lemaire, Jodie Scache, Christophe Mariller, Tony Lefebvre and Anne-Sophie Vercoutter-Edouart
Cells 2023, 12(10), 1396; https://doi.org/10.3390/cells12101396 - 15 May 2023
Cited by 5 | Viewed by 3843
Abstract
The transport of proteins between the different cellular compartments and the cell surface is governed by the secretory pathway. Alternatively, unconventional secretion pathways have been described in mammalian cells, especially through multivesicular bodies and exosomes. These highly sophisticated biological processes rely on a [...] Read more.
The transport of proteins between the different cellular compartments and the cell surface is governed by the secretory pathway. Alternatively, unconventional secretion pathways have been described in mammalian cells, especially through multivesicular bodies and exosomes. These highly sophisticated biological processes rely on a wide variety of signaling and regulatory proteins that act sequentially and in a well-orchestrated manner to ensure the proper delivery of cargoes to their final destination. By modifying numerous proteins involved in the regulation of vesicular trafficking, post-translational modifications (PTMs) participate in the tight regulation of cargo transport in response to extracellular stimuli such as nutrient availability and stress. Among the PTMs, O-GlcNAcylation is the reversible addition of a single N-acetylglucosamine monosaccharide (GlcNAc) on serine or threonine residues of cytosolic, nuclear, and mitochondrial proteins. O-GlcNAc cycling is mediated by a single couple of enzymes: the O-GlcNAc transferase (OGT) which catalyzes the addition of O-GlcNAc onto proteins, and the O-GlcNAcase (OGA) which hydrolyses it. Here, we review the current knowledge on the emerging role of O-GlcNAc modification in the regulation of protein trafficking in mammalian cells, in classical and unconventional secretory pathways. Full article
(This article belongs to the Special Issue Glycoproteomics and Protein Glycosylation in Cell Biology and Diseases)
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