Related Experiment Video
Updated: Sep 20, 2025
11:36
Glycan Node Analysis: A Bottom-up Approach to Glycomics
Published on: May 22, 2016
10.5K
Glycosylation in Cancer
Henrique Oliveira Duarte1,2, Celso Albuquerque Reis1,2,3, Veronique Blanchard4,5
1Instituto de Investigação e Inovação em Saúde, Universidade do Porto (i3S), Porto, Portugal.
Handbook of Experimental Pharmacology
|May 29, 2025
Summary
Cancer cells exhibit altered glycosylation, impacting tumor growth, immune response, and patient prognosis. These changes are crucial for cancer development and serve as biomarkers for diagnosis and therapy.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Aberrant glycosylation is a hallmark of all investigated malignancies in humans and animals.
- These alterations are integral to tumor initiation, progression, and metastasis.
Purpose of the Study:
- To provide an overview of cancer-associated glycosylation changes.
- To discuss the underlying genetic and biochemical mechanisms.
- To highlight the functional and clinical significance of these changes.
Main Methods:
- Biochemical characterization of glycan biosynthesis pathways.
- Genomic analysis of enzymatic machinery in cancer cells.
- Review of experimental and epidemiological findings.
Main Results:
- Tumor-associated glycans significantly influence invasive and metastatic growth.
- Glycosylation changes play a role in anti-tumor immunological defense.
- These alterations impact patient prognosis and clinical outcomes.
Conclusions:
- Cancer-associated glycosylation changes are critical for tumor progression and patient outcomes.
- Tumor-associated glycans are valuable biomarkers for cancer diagnosis and monitoring.
- These changes represent targets for novel therapeutic strategies.
Keywords:
Anti-cancer vaccinationCancerCell adhesionExtracellular matrixGlycan-specific receptorsGlycomeGlycosylationGlycosyltransferaseImmune evasionMetastasisTumour-associated glycanMore Related Videos
13:21Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Published on: May 4, 2012
15.8K
10:59Glycomics-Guided Glycoproteomics Facilitates Comprehensive Profiling of the Glycoproteome in Complex Tumor Microenvironments
Published on: February 7, 2025
1.3K
Related Concept Videos
01:25Protein Glycosylation
7.3K
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...
7.3K
02:53Adaptive Mechanisms in Cancer Cells
6.0K
Cancer cells accumulate genetic changes at an abnormally rapid rate due to the defects in the DNA repair mechanisms. From an evolutionary perspective, such genetic instability is advantageous for cancer development. Mutant cell lines accumulate a series of beneficial mutations that contribute to their progression into cancer.
Some of the advantages that cancer cells have on normal cells include - enhanced ability to divide without terminally differentiating, induce new blood vessel formation,...
Some of the advantages that cancer cells have on normal cells include - enhanced ability to divide without terminally differentiating, induce new blood vessel formation,...
6.0K
01:05Proteoglycans
4.0K
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,...
4.0K
01:24Oligosaccharide Assembly
3.0K
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...
3.0K
03:03mTOR Signaling and Cancer Progression
3.9K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
The mTOR pathway or the...
3.9K
02:18Cancer
49.9K
Cancers arise due to mutations in genes involved in the regulation of cell division, which leads to unrestricted cell proliferation. Modern science and medicine have made great strides in the understanding and treatment of cancer, including eradicating cancer in some patients. However, there is still no cure for cancer. This is largely due to the fact that cancer is a large group of many diseases.
49.9K