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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,...

Glucose Transporters

Glucose Transporters

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Glycosaminoglycans

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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.
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Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

Updated: Jun 8, 2026

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Published on: April 16, 2013

Glucosylceramide in humans.

Maria C Messner¹, Myles C Cabot

¹John Wayne Cancer Institute, 2200 Santa Monica Blvd, Santa Monica, California 90404, USA.

Advances in Experimental Medicine and Biology

|October 6, 2010

Summary

Glucosylceramide plays a dual role in cells, offering protection at normal levels but causing harm when excessively abundant, as seen in Gaucher disease.

Area of Science:

Biochemistry
Cell Biology
Glycosphingolipid Metabolism

Background:

Glucosylceramide is a key precursor in glycosphingolipid synthesis.
Its production is regulated by glucosylceramide synthase.
Aberrant levels are linked to various diseases.

Purpose of the Study:

To elucidate the multifaceted role of glucosylceramide in mammalian cells.
To understand the implications of glucosylceramide level alterations in disease.

Main Methods:

Analysis of glucosylceramide levels in cellular and tissue contexts.
Investigating the enzymatic activation of glucosylceramide synthase.
Correlating glucosylceramide abundance with disease states.

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Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis

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Published on: April 27, 2021

Related Experiment Videos

Last Updated: Jun 8, 2026

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Mass Spectrometric Analysis of Glycosphingolipid Antigens

Published on: April 16, 2013

Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis

Preparation of Human Tissues Embedded in Optimal Cutting Temperature Compound for Mass Spectrometry Analysis

Published on: April 27, 2021

Main Results:

Glucosylceramide upregulation can confer cellular protection and promote proliferation.
Sustained overabundance of glucosylceramide is detrimental.
Specific diseases like Gaucher disease are associated with glucosylceramide accumulation.

Conclusions:

Glucosylceramide's function is context-dependent, balancing protective and detrimental effects.
Modulating glucosylceramide levels may be a therapeutic target for related disorders.
Further research is needed to fully understand its complex cellular roles.