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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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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...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Membrane Carbohydrates01:30

Membrane Carbohydrates

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The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
Membrane carbohydrates do not have any hydrophobic region and are exclusively located on the cell's outer surface. The addition of sugar molecules or glycosylation of proteins happens in...
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Related Experiment Video

Updated: Jun 14, 2025

Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan
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Identifying Cell Surface Markers of Primary Neural Stem and Progenitor Cells by Metabolic Labeling of Sialoglycan

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Deciphering the Cell Surface Sugar-Coating via Biochemical Pathways.

Pritam Ghosh1

  • 1Department of Chemistry, Humboldt-Universität zu Berlin, Brook-Taylor-Str. 2, 12489, Berlin, Germany.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|August 31, 2024
PubMed
Summary
This summary is machine-generated.

Glycans on cell surfaces are crucial for biological functions and disease biomarkers. New metabolic glycan labeling and boronic acid probes offer advanced methods for studying these cell surface sugars in situ.

Keywords:
AI-MLCopper click chemistryGlycanMetalloid boronTarget therapeutics

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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
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Area of Science:

  • Carbohydrate Chemistry
  • Cell Biology
  • Biochemistry

Background:

  • Cell surface glycans, forming the glycocalyx, are vital for cell structure, communication, and therapeutic targeting.
  • Glycans are complex, found as glycolipids, glycoproteins, and proteoglycans, posing challenges for study.
  • Understanding cellular glycosylation is essential for basic research and developing glycan-targeted therapies.

Purpose of the Study:

  • To review the significance of glycans as disease biomarkers.
  • To discuss the necessity of evaluating glycans in situ within their physiological environment.
  • To explore the prospects and potential applications of advanced glycan analysis techniques.

Main Methods:

  • Metabolic glycan labeling introduces unnatural modifications into cellular glycans via natural metabolic pathways.
  • Metabolic oligosaccharide engineering, pioneered by the Bertozzi group, utilizes glycan salvage pathways.
  • Boronic acid-based probes enable single-step carbohydrate recognition without surface modification.

Main Results:

  • Metabolic glycan labeling allows probes to integrate into cellular glycan structures, enabling detection via click chemistry.
  • Boronic acid probes offer a direct method for in situ carbohydrate detection.
  • The review highlights the importance of glycans as biomarkers and the need for in situ evaluation.

Conclusions:

  • Advanced glycan analysis techniques like metabolic labeling and boronic acid probes are crucial for fundamental research and therapeutic development.
  • Glycans hold significant potential as biomarkers for various diseases.
  • In situ evaluation of glycans in their physiological context is vital for understanding their roles and applications.