Cell Surface Glycosylation
Cell Surface Glycosylation - Related Videos
11:27
Analysis of SCAP N-glycosylation and Trafficking in Human Cells
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Cited by 17 •
2016
We describe a modified method for membrane fraction isolation from human cells and sample preparation for the detection of SCAP N-glycosylation and total protein by using western blot. We further introduce a GFP-labeling method to monitor SCAP trafficking using confocal microscopy. This protocol can be used in regular biology laboratories.
01:25
Protein Glycosylation
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2023
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded. Glycosylation occurs in...
09:54
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Cited by 31 •
2011
Using specific glycosidases to remove sugars from glycoproteins followed by SDS-PAGE is a valuable method to detect glycan modifications on protein samples and is a good choice for initial glycobiology studies. Changes following deglycosylation can be detected as shifts in gel mobility or by staining with glycan sensitive reagents.
10:11
Glycopeptide Capture for Cell Surface Proteomics
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Cited by 8 •
2014
Cell surface proteins are biologically important and widely glycosylated. We introduce here a glycopeptide-capture approach to solubilize, enrich, and deglycosylate these proteins for facile LC-MS based proteomic analyses.
08:49
Cell Surface Receptor Identification Using Genome-Scale CRISPR/Cas9 Genetic Screens
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Cited by 8 •
2020
This manuscript describes a genome-scale cell-based screening approach to identify extracellular receptor-ligand interactions.
FAQs
During passage through the endoplasmic reticulum and Golgi apparatus, glycosyltransferases add sugar units while glycosidases remove or remodel them. The resulting sequence of enzymatic changes gives proteins and lipids distinct surface carbohydrate patterns. Those patterns create functional differences in how cells are recognized, adhere, signal, and engage with immune processes.
Movement through these organelles is important because glycan modification occurs while membrane proteins and lipids are being processed for the cell surface. Enzyme-driven addition and remodeling can therefore produce different exposed patterns rather than a uniform coating. This organization helps explain why surface carbohydrates vary among cell types and support specialized cell interactions.
Cell surface glycosylation affects several forms of cellular communication at once. Its carbohydrate patterns can participate in cell recognition and adhesion, while also influencing signaling and immune interactions. Consequently, a change in the surface pattern may alter how a cell contacts neighboring cells, responds to its surroundings, or is engaged by immune processes.
Examining these surface patterns can connect molecular changes with cell behavior and disease-related biology. In particular, research can ask how glycosylation differences contribute to infection, inflammation, development, or cancer progression. The topic therefore provides a way to relate enzymatic remodeling at the membrane to broader changes in cellular communication and interaction.
Cell-type-specific patterns are valuable because they distinguish the molecular surfaces presented by different cells. These differences can help researchers investigate recognition, adhesion, signaling, and immune interactions in their proper biological context. Comparing such patterns may also clarify how normal cellular communication differs from glycosylation-associated changes linked to disease processes.
Because altered glycosylation is associated with infection, inflammation, development, and cancer progression, its surface features can serve as clues to disease mechanisms. Researchers can use this knowledge in biomarker research to identify informative molecular patterns and in therapeutic strategy development aimed at addressing glycosylation-related cellular changes. The emphasis is on linking surface chemistry with outcomes.