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

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.8K
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...
2.8K
Protein Glycosylation01:25

Protein Glycosylation

6.9K
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...
6.9K
Selectins01:25

Selectins

3.3K
Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
3.3K

You might also read

Related Articles

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

Sort by
Same author

High-Resolution Spatial Transcriptomic Atlas of Mouse Soleus Muscle: Unveiling Single Cell and Subcellular Heterogeneity in Health and Denervation.

bioRxiv : the preprint server for biology·2024
Same author

Genotype-phenotype correlations in RHOBTB2-associated neurodevelopmental disorders.

Genetics in medicine : official journal of the American College of Medical Genetics·2023
Same author

Adjuvant chemotherapy following chemoradiotherapy as primary treatment for locally advanced cervical cancer versus chemoradiotherapy alone (OUTBACK): an international, open-label, randomised, phase 3 trial.

The Lancet. Oncology·2023
Same author

Radiation Therapy Techniques and Treatment-Related Toxicity in the PORTEC-3 Trial: Comparison of 3-Dimensional Conformal Radiation Therapy Versus Intensity-Modulated Radiation Therapy.

International journal of radiation oncology, biology, physics·2021
Same author

EIF3F-related neurodevelopmental disorder: refining the phenotypic and expanding the molecular spectrum.

Orphanet journal of rare diseases·2021
Same author

Long-Term Toxicity and Health-Related Quality of Life After Adjuvant Chemoradiation Therapy or Radiation Therapy Alone for High-Risk Endometrial Cancer in the Randomized PORTEC-3 Trial.

International journal of radiation oncology, biology, physics·2020

Related Experiment Video

Updated: Jul 4, 2025

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
05:19

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System

Published on: June 28, 2024

877

Lectins as versatile tools to explore cellular glycosylation.

Susan Brooks1

  • 1Oxford Brookes University, Oxford. sbrooks@brookes.ac.uk.

European Journal of Histochemistry : EJH
|January 29, 2024
PubMed
Summary
This summary is machine-generated.

Lectins, carbohydrate-binding proteins, are vital tools for studying cell glycosylation. Lectin histochemistry reveals crucial changes in cancer development and offers potential for early detection and prognosis.

More Related Videos

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

36.7K
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

3.4K

Related Experiment Videos

Last Updated: Jul 4, 2025

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
05:19

Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System

Published on: June 28, 2024

877
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

36.7K
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

3.4K

Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Lectins are naturally occurring proteins that bind carbohydrates with high selectivity.
  • They have been used since the late 1880s to explore glycosylation in cells and tissues.
  • Glycosylation plays critical roles in biological systems, development, health, and disease.

Purpose of the Study:

  • To highlight the utility of lectins and lectin histochemistry in understanding glycosylation.
  • To emphasize the role of lectins in cancer research, including biomarker discovery and understanding metastasis.
  • To discuss recent advancements in lectin technology and their impact on glycomic analysis.

Main Methods:

  • Lectin histochemistry for mapping tissue glycosylation.
  • Utilizing lectins to identify changes in cellular glycosylation during development, health, and disease.
  • Leveraging advancements in biotechnology for improved lectin binding partner characterization and engineered lectins.

Main Results:

  • Lectin histochemistry has revealed significant alterations in glycosylation associated with cancer development and metastasis.
  • Glycosylated biomarkers identified through lectin studies show potential for cancer prognosis, early detection, and screening.
  • Insights into the functional roles of glycosylation in both healthy and diseased states have been gained.

Conclusions:

  • Lectins and lectin histochemistry are indispensable tools for glycomic research.
  • Understanding glycosylation patterns through lectin analysis is crucial for advancing cancer diagnostics and therapeutics.
  • Emerging biotechnologies and high-throughput platforms promise more sophisticated glycomic mapping and deeper biological insights.