Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Biosynthesis of Polysaccharides01:26

Biosynthesis of Polysaccharides

733
Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
733
Protein Glycosylation01:25

Protein Glycosylation

9.9K
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...
9.9K
Proteoglycans01:05

Proteoglycans

5.0K
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,...
5.0K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.7K
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...
3.7K
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

9.3K
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.
9.3K
Glycosaminoglycans01:23

Glycosaminoglycans

7.3K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
7.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Unraveling the GM<sub>1</sub> Specificity of Galectin‑1 Binding to Lipid Membranes.

ACS bio & med chem Au·2025
Same author

Cysteine Oxidation in Human Galectin-1 Occurs Sequentially via a Folded Intermediate to a Fully Oxidized Unfolded Form.

International journal of molecular sciences·2024
Same author

Altering the Modular Architecture of Galectins Affects its Binding with Synthetic α-Dystroglycan O-Mannosylated Core M1 Glycoconjugates In situ.

Chembiochem : a European journal of chemical biology·2023
Same author

Targeting osteoarthritis-associated galectins and an induced effector class by a ditopic bifunctional reagent: Impact of its glycan part on binding measured in the tissue context.

Bioorganic & medicinal chemistry·2022
Same author

Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan.

Scientific reports·2022
Same author

Structure of Galectin-3 bound to a model membrane containing ganglioside GM1.

Biophysical journal·2022

Related Experiment Video

Updated: Feb 20, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

4.1K

The sugar code: Why glycans are so important.

Hans-Joachim Gabius1

  • 1Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstraße 13, 80539 Munich, Germany.

Bio Systems
|July 16, 2017
PubMed
Summary
This summary is machine-generated.

Sugars, the third alphabet of life, form complex carbohydrates (glycans) that act as cell surface signals. These glycans, akin to fingerprints, are crucial for intercellular communication and have broad physiological significance.

Keywords:
AgglutininGlycolipidGlycoproteinGlycosylationGlycosyltransferaseLectinSugar code

More Related Videos

Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

11.2K
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

37.5K

Related Experiment Videos

Last Updated: Feb 20, 2026

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
11:21

Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

Published on: January 20, 2022

4.1K
Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

11.2K
Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

37.5K

Area of Science:

  • Carbohydrate Chemistry
  • Glycobiology
  • Cellular Communication

Background:

  • Cell surfaces mediate intercellular communication via biochemical signals.
  • These signals must dynamically respond to internal/external factors.
  • Information density requires biomolecules forming many oligomers from few building blocks.

Purpose of the Study:

  • To explore the 'sugar code' concept for cellular communication.
  • To compare biocompounds as information carriers.
  • To highlight the role of complex carbohydrates (glycans) in cell signaling.

Main Methods:

  • Comparative analysis of biocompound properties (nucleotides, amino acids, sugars).
  • Examination of enzymatic machinery for sugar chain biosynthesis.
  • Review of glycan conjugates (glycoproteins, glycolipids) and their functions.

Main Results:

  • Sugars are identified as superior building blocks for information-rich oligomers compared to nucleotides and amino acids.
  • Enzymatic synthesis allows for an vast number of unique glycan structures (oligo- and polysaccharides).
  • Cellular glycomes function as unique molecular fingerprints, with glycans conjugated to proteins and lipids.

Conclusions:

  • The 'sugar code,' based on complex carbohydrates, represents a fundamental mechanism for cellular information processing.
  • Glycans play a critical role in intercellular communication, with broad implications in physiology and pathology.
  • Understanding the 'sugar code' involves studying the synthesis, modification, and recognition of these complex carbohydrate structures.