Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Oligosaccharide Assembly

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...

Proteoglycans

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 Glycosylation

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 Activity

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 Activity

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 Inhibition

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 molecular biology·2008

Same author

Sialidases.

Current protocols in molecular biology·2008

Search research articles

Related Experiment Video

Updated: Jul 5, 2026

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

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 Protein Science

|April 23, 2008

Summary

Researchers used specific inhibitors in cultured cells to alter protein glycosylation, enabling the study of oligosaccharide functions. This method helps investigate how sugar chains impact protein roles in cells.

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

N-linked glycosylation is a crucial post-translational modification affecting protein structure and function.
Understanding the role of oligosaccharides in glycoproteins requires specific experimental approaches.
Current methods may lack precision in dissecting the functional impact of altered glycosylation patterns.

Purpose of the Study:

To describe a method for preventing N-linked glycosylation in cultured cells using inhibitors.
To enable the study of glycoproteins with modified or absent oligosaccharide chains.
To investigate the functional significance of oligosaccharides on specific proteins and intact cells.

Main Methods:

Determination of optimal non-toxic inhibitor concentration by monitoring [(35)S]methionine incorporation for protein biosynthesis.

More Related Videos

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

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

Published on: November 25, 2017

Related Experiment Videos

Last Updated: Jul 5, 2026

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

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

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

Published on: November 25, 2017

Assessment of inhibitor efficacy in blocking oligosaccharide processing using [(3)H]mannose labeling, TCA precipitation, or endo H digestion.

Protein concentration using acetone precipitation.

Main Results:

Successful prevention of N-linked glycosylation in cultured cells, yielding glycoproteins with altered oligosaccharide chains.
Established protocols for assessing inhibitor effectiveness and protein biosynthesis.
Validated methods for analyzing changes in protein glycosylation.

Conclusions:

Inhibitor-based modulation of N-linked glycosylation is a viable strategy for functional studies.
This approach allows for detailed examination of oligosaccharide roles in protein function.
The described methods provide a robust framework for investigating glycoprotein structure-function relationships.