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

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...

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,...

Fibronectins Connect Cells with ECM

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...

Matrix Proteoglycans and Glycoproteins

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...

Glycocalyx and its Functions

Glycocalyx and its Functions

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.
Components of...

You might also read

Related Articles

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

Sort by

Same author

Posttraumatic stress and youth violence perpetration: A population-based cross-sectional study.

European psychiatry : the journal of the Association of European Psychiatrists·2016

Same author

[Inherited thrombopathia in Simmental cattle].

Schweizer Archiv fur Tierheilkunde·2016

Same author

A case-control study to estimate the effects of acute clinical infection with the Schmallenberg virus on milk yield, fertility and veterinary costs in Swiss dairy herds.

Preventive veterinary medicine·2016

Same author

Subaxial cervical spine.

Surgical technology international·2015

Same author

How to be a good reviewer.

European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society·2014

Same author

Isolation of the TRP2 and the TRP3 genes of Saccharomyces cerevisiae by functional complementation in yeast.

Current genetics·2013

Search research articles

Related Experiment Video

Updated: Jun 29, 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 28, 2010

Intracellular functions of N-linked glycans.

A Helenius¹, M Aebi

¹Institute of Biochemistry, Eidgenössische Technische Hochschule Zürich, Universitätstrasse 16, CH-8092 Zürich, Switzerland.

Science (New York, N.Y.)

|March 28, 2001

Summary

N-linked oligosaccharides are crucial for glycoprotein processing in the endoplasmic reticulum (ER) and Golgi complex. These sugar chains act as essential tags, guiding protein folding, quality control, and transport throughout the cell.

Area of Science:

Cell Biology
Biochemistry
Glycoscience

Background:

N-linked oligosaccharides are synthesized as 14-sugar blocks added to polypeptides during translation in the endoplasmic reticulum (ER).
These glycans undergo significant modifications as glycoproteins mature and traffic through the secretory pathway (ER and Golgi complex).
In the early secretory pathway, N-glycans function as critical tags for protein folding, quality control, sorting, and transport.

Purpose of the Study:

To elucidate the multifaceted roles of N-linked oligosaccharides in glycoprotein processing.
To highlight the distinct functions of N-glycans in the ER versus the Golgi complex.
To emphasize the evolutionary significance of compartmentalizing glycan synthesis and modification.

Main Methods:

More Related Videos

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H⁺

Published on: June 25, 2018

Related Experiment Videos

Last Updated: Jun 29, 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 28, 2010

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H+

Analysis of N-glycans from Raphanus sativus Cultivars Using PNGase H⁺

Published on: June 25, 2018

The study is primarily a review and synthesis of existing knowledge on N-linked glycosylation.

It analyzes the structural and functional aspects of N-glycans at different stages of glycoprotein maturation.

Comparative analysis of glycan roles in the ER and Golgi complex.

Main Results:

N-glycans serve as universal tags recognized by lectins and enzymes, facilitating order in glycoprotein maturation.
In the ER, N-glycans are vital for initial protein folding, quality control, and trafficking.
In the Golgi complex, N-glycans are further elaborated into complex structures with new functional roles.

Conclusions:

The sequential processing of N-linked oligosaccharides in the ER and Golgi complex is an evolutionary adaptation for efficient glycan function.
N-glycans play indispensable roles in protein homeostasis and cellular communication.
Understanding N-glycan dynamics is key to deciphering complex cellular processes.