Disease-associated glycans on cell surface proteins

Area of Science:

• Biochemistry and Molecular Biology
• Cell Biology
• Glycoscience

Background:

• Glycoproteins and glycolipids are vital membrane molecules, with N-glycans on cell surface receptors significantly controlling cellular functions.
• Identifying the functional roles of glycans is essential for understanding cell signaling and physiological/pathological processes.

Purpose of the Study:

• This review focuses on glycosyltransferases involved in N-glycan modification.
• It examines their roles in target proteins like EGFR, ErbB3, TGF-β receptor, TCR, BACE1, GLUT2, E-cadherin, and α5β1 integrin.
• The review explores the connection between these modifications, diseases, and epithelial-mesenchymal transition (EMT).

Main Methods:

• Literature review of glycosyltransferases and their roles in N-glycan modification.
• Analysis of target proteins and their functional alterations due to glycosylation.
• Examination of the involvement of specific glycosyltransferases (GnT-III, GnT-IV, GnT-V, ST6GAL1, Fut8) in pathological signaling and EMT.

Main Results:

• Glycosyltransferases significantly modify N-glycans on key cell surface receptors and proteins.
• These modifications influence receptor function, cellular signaling pathways, and disease progression.
• Specific enzymes like GnT-V and Fut8 are highlighted for their roles in regulating receptor function in pathological contexts.

Conclusions:

• Glycosyltransferases are critical regulators of cell surface receptor function through N-glycan modification.
• Dysregulation of these enzymes is implicated in various diseases and the EMT process.
• Targeting specific glycosyltransferases presents a potential therapeutic strategy for diseases involving aberrant cell signaling.