Related Experiment Video
Updated: Jul 2, 2026
11:02
Induction of Invasive Transitional Cell Bladder Carcinoma in Immune Intact Human MUC1 Transgenic Mice: A Model for Immunotherapy Development
Published on: October 30, 2013
Glycosylation in bladder cancer.
1Department of Urology, Hirosaki University Graduate School of Medicine, 5 Zaifucho, Hirosaki, Japan. coyama@cc.hirosaki-u.ac.jp
International Journal of Clinical Oncology
|August 16, 2008
Summary
Aberrant glycosylation, involving complex carbohydrates like blood type antigens, significantly impacts bladder cancer development and progression. Understanding these changes offers new diagnostic and therapeutic possibilities in glycobiology.
Area of Science:
- Glycobiology
- Cancer Biology
- Biochemistry
Background:
- Complex carbohydrates (glycoproteins, proteoglycans, glycosphingolipids) are vital for cell membrane functions and interactions.
- Aberrant glycosylation, a change in carbohydrate profiles, is a hallmark of malignant transformation in cancer.
- Blood type antigens and other complex carbohydrates are implicated in bladder cancer pathogenesis.
Purpose of the Study:
- To review the role of aberrant glycosylation and specific carbohydrate structures in bladder cancer.
- To highlight the diagnostic and therapeutic potential of targeting these glycans and their associated molecules.
Main Methods:
- Review of literature on carbohydrate expression in normal and tumor tissues.
- Immunohistochemical staining and monoclonal antibody-based detection of carbohydrate antigens.
- Analysis of studies investigating specific glycans (e.g., Lewis X, GM3, hyaluronic acid) and their ligands (selectins, galectins) in bladder cancer.
Main Results:
- Distinct differences in carbohydrate profiles exist between normal and bladder tumor tissues.
- Aberrant glycosylation, including altered expression of blood type antigens like Lewis X, is associated with bladder cancer.
- Specific glycans (e.g., GM3, hyaluronic acid) and their ligands influence cancer cell apoptosis, invasion, and metastasis.
Conclusions:
- Complex carbohydrates, their aberrant expression, and associated ligands play critical roles in bladder cancer progression.
- Targeting glycans and their interactions presents a promising avenue for novel diagnostic and therapeutic strategies in bladder cancer treatment.
Related Concept Videos
01:05Proteoglycans
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,...
01:24Oligosaccharide 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...
Multiple sugar molecules that may or may...
01:25Protein 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...
Glycosylation occurs in...