Jove
Visualize
Contact Us

Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Proteoglycans01:05

Proteoglycans

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,...
Protein Glycosylation01:25

Protein Glycosylation

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...
Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Inhibition of CDK Activity02:34

Inhibition of CDK Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Feedback Inhibition00:46

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!

You might also read

Related Articles

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

Sort by
Same author

Case reports and technical notes; anterior sacral meningocele.

Journal of neurosurgery·2010
Same author

The etiology and surgical treatment of intestinal obstruction.

Journal. Iowa State Medical Society·2010
Same author

Inhibition of N-linked glycosylation.

Current protocols in immunology·2008
Same author

Release of saccharides from glycoconjugates.

Current protocols in immunology·2008
Same author

Inhibition of N-linked glycosylation.

Current protocols in protein science·2008
Same author

Sialidases.

Current protocols in molecular biology·2008
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 Experiment Video

Updated: Jul 7, 2026

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

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

Published on: April 27, 2010

Inhibition of N-linked glycosylation.

L D Powell1

  • 1University of California San Diego, La Jolla, California, USA.

Current Protocols in Molecular Biology
|February 12, 2008
PubMed
Summary

Inhibiting N-linked glycosylation in cells produces glycoproteins with altered chains, aiding the study of oligosaccharide functions. This method helps understand the roles of these sugar chains on proteins and cells.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • N-linked oligosaccharides are crucial post-translational modifications on glycoproteins.
  • Understanding the functional roles of N-linked oligosaccharides is essential in cell biology.

Purpose of the Study:

  • To describe a method for preventing N-linked glycosylation in cultured cells using enzyme inhibitors.
  • To provide a framework for assessing the functional impact of altered N-linked glycosylation on specific proteins and cells.

Main Methods:

  • Determining the optimal non-toxic concentration of enzyme inhibitors by monitoring protein biosynthesis ([35S]methionine incorporation).
  • Assessing inhibitor efficacy in blocking oligosaccharide processing via [3H]mannose labeling, TCA precipitation, or endo H digestion.

More Related Videos

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Related Experiment Videos

Last Updated: Jul 7, 2026

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

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

Published on: April 27, 2010

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

  • Analyzing the effect of inhibitors on specific glycoproteins to evaluate N-linked oligosaccharide chain alterations.
  • Main Results:

    • Treatment with enzyme inhibitors leads to the production of glycoproteins with incomplete or modified N-linked oligosaccharide chains.
    • The described methods allow for the precise evaluation of inhibitor effects on glycosylation.

    Conclusions:

    • Inhibiting N-linked glycosylation is a viable strategy for investigating the functional significance of oligosaccharide chains.
    • This approach facilitates the study of protein function and cellular processes influenced by glycosylation patterns.