Related Experiment Video
Updated: Apr 12, 2026
11:25
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
7.2K
Tissue-Specific Glycosylation at the Glycopeptide Level
Katalin F Medzihradszky1, Krista Kaasik2, Robert J Chalkley2
1From the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517 folkl@cgl.ucsf.edu.
Molecular & Cellular Proteomics : MCP
|May 22, 2015
Summary
This study reveals site-specific glycosylation differences in mouse liver proteins, highlighting variations based on cellular location and tissue type. Glycopeptide analysis showed distinct N- and O-linked glycan patterns between liver and brain tissues.
Area of Science:
- Biochemistry
- Proteomics
- Glycomics
Background:
- Glycosylation is a crucial post-translational modification affecting protein function.
- Understanding site-specific glycosylation patterns is essential for deciphering protein roles.
- Comparative glycomics studies are needed to reveal tissue-specific modifications.
Purpose of the Study:
- To characterize site-specific N- and O-glycosylation in mouse liver.
- To investigate the impact of cellular location on N-glycan structures.
- To compare glycosylation patterns between mouse liver and brain tissues.
Main Methods:
- Enrichment and mass spectrometric analysis of intact glycopeptides.
- Utilized both collisional activation (CA) and electron transfer dissociation (ETD) for glycopeptide analysis.
- Compared N-glycan structures of proteins from different cellular compartments (lysosomal, ER, secreted, transmembrane).
Main Results:
- Site-specific N- and O-glycosylation data were obtained for approximately 130 mouse liver proteins.
- Observed incorporation of diverse sialic acid variants in both N- and O-linked glycans.
- Protein N-glycosylation varied significantly depending on cellular location.
- Tissue-specific glycosylation differences were identified between mouse liver and brain, even at the same protein sites.
Conclusions:
- Cellular location influences N-glycosylation patterns in mouse liver.
- Significant tissue-specific differences exist in protein glycosylation between mouse liver and brain.
- Comparative glycopeptide analysis provides insights into tissue-specific glycan heterogeneity.
Related Concept Videos
01:25Protein Glycosylation
10.6K
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...
Glycosylation occurs in...
10.6K
01:05Proteoglycans
5.3K
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,...
5.3K
01:24Oligosaccharide Assembly
3.9K
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...
Multiple sugar molecules that may or may...
3.9K
01:29Protein Folding Quality Check in the RER
5.7K
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...
5.7K
01:21Matrix Proteoglycans and Glycoproteins
5.7K
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...
5.7K
01:14Glycocalyx and its Functions
10.6K
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.
10.6K