Related Experiment Video
Updated: Mar 21, 2026

06:53
Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells
Published on: June 2, 2022
3.9K
Exploring human glycosylation for better therapies
Larissa Krasnova1, Chi-Huey Wong2
1Department of Chemistry, The Scripps Research Institute, La Jolla, California, USA.
Molecular Aspects of Medicine
|May 15, 2016
Summary
Glycosylation, the process of adding sugars to proteins and lipids, is complex and influenced by many factors. Understanding it requires diverse methods to develop new therapies like cancer vaccines.
Area of Science:
- Biochemistry
- Glycobiology
- Proteomics
- Immunology
Background:
- Protein and lipid glycosylation is not directly gene-encoded, making it highly variable.
- Glycosylation patterns differ based on cell type, enzymes, substrates, and environmental factors.
- Cellular heterogeneity in glycoforms leads to diverse biological activities and disease states.
Purpose of the Study:
- To review recent advancements in understanding and manipulating glycosylation.
- To highlight the importance of a multidisciplinary approach in glycosylation research.
- To demonstrate how structure-defined carbohydrates can drive therapeutic innovation.
Main Methods:
- Multidisciplinary strategies including genetic manipulation and pathway engineering.
- Structural and functional proteomic analysis.
- Chemical and enzymatic synthesis of glycans.
- Development of glycosylation probes and glycan microarrays.
Main Results:
- Recent progress enables a deeper understanding of complex glycosylation.
- Structure-defined oligosaccharides are crucial for developing novel therapeutics.
- Advancements facilitate the creation of homogeneous therapeutic antibodies.
Conclusions:
- Glycosylation research necessitates an integrated approach combining various scientific disciplines.
- The development of structure-defined carbohydrates is key to advancing medical treatments.
- This field holds promise for novel carbohydrate-based vaccines, particularly for cancer.
More Related Videos
Related Concept Videos
Protein Glycosylation
10.3K
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...
10.3K
Oligosaccharide Assembly
3.8K
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...
3.8K
Proteoglycans
5.1K
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,...
5.1K
Hypoglycemia and Glucagon
1.2K
Without prolonged fasting, healthy individuals maintain blood glucose levels above 3.5 mM due to a well-adapted neuroendocrine counterregulatory system that effectively prevents acute hypoglycemia, a potentially life-threatening condition. The primary clinical scenarios for hypoglycemia encompass diabetes treatment, inappropriate production of endogenous insulin or insulin-like substances by tumors, and the use of glucose-lowering agents in non-diabetic individuals. Notably, hypoglycemia in the...
1.2K
Site-Targeted Drug Delivery Systems: Polymeric Carriers
85
Polymeric carriers enhance targeted drug delivery by increasing efficacy while minimizing off-target effects. These carriers comprise a biodegradable polymeric backbone integrated with functional elements that enable targeting, improve physicochemical properties, and regulate drug release.Targeting MechanismsThe targeting ability of polymeric carriers is mediated by a homing device, which is a molecular recognition component designed to selectively bind to specific tissues or cells. Monoclonal...
85
Oral Hypoglycemic Agents: α-Glucosidase Inhibitors
837
α-glucosidase inhibitors, including acarbose (Precose), miglitol (Glyset), and voglibose (Voglib) (primarily available in Asia), are drugs that control blood sugar levels by delaying the digestion of starch and disaccharides. They achieve this by inhibiting α-glucosidase enzymes in the intestine, which slow the absorption of carbohydrates in the intestine, which in turn leads to a prolonged release of the glucoregulatory hormone GLP-1 from intestinal L-cells.
Acarbose and miglitol are...
Acarbose and miglitol are...
837

