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Glycosylation Modulates the Structure and Functions of Collagen: A Review
1Institute of Chemistry, Slovak Academy of Sciences, 845 38 Bratislava, Slovakia.
Molecules (Basel, Switzerland)
|April 13, 2024
Summary
Collagen glycosylation, a key post-translational modification, impacts protein function and human diseases. Understanding collagen glycosyltransferases offers therapeutic potential for novel agents.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Collagens are essential extracellular matrix proteins crucial for tissue structure and function.
- Collagen biosynthesis involves intricate post-translational modifications, including specific glycosylation.
- Aberrant collagen glycosylation is linked to various human diseases.
Purpose of the Study:
- To review current knowledge on collagen glycosylation.
- To survey glycosyltransferases involved in collagen modification, their structures, and mechanisms.
- To discuss the role of collagen glycosylation in biological functions and diseases.
Main Methods:
- Literature review of collagen glycosylation.
- Analysis of glycosyltransferase structures and catalytic mechanisms.
- Discussion of disease associations and therapeutic implications.
Main Results:
- Collagens undergo specific glycosylation with disaccharides linked to hydroxylysine.
- Several glycosyltransferases (e.g., COLGALT1, COLGALT2, LH3) are implicated in this process.
- Collagen glycosylation influences secretion, fibril alignment, function, and disease pathogenesis.
Conclusions:
- Collagen glycosylation is critical for collagen homeostasis and function.
- Detailed understanding of collagen glycosyltransferases and their mechanisms is advancing.
- Targeting collagen glycosylation presents therapeutic opportunities for disease treatment.
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