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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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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...
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Fibril-associated Collagen01:11

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
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Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
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Type IV Collagen of Basal Lamina01:05

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Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
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Cofactors and Coenzymes01:27

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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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Related Experiment Video

Updated: Jan 28, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
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Analysis of SCAP N-glycosylation and Trafficking in Human Cells

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Collagen glycosylation.

Thierry Hennet1

  • 1Institute of Physiology, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.

Current Opinion in Structural Biology
|March 2, 2019
PubMed
Summary

This study explores the widespread hydroxylysine glycosylation in collagens, a process initiated by specific enzymes. Discoveries suggest diverse glycosylation forms may exist across various species.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Glycobiology

Background:

  • Collagens are abundant proteins in animals, yet the biology of hydroxylysine-bound disaccharides (Glc(α1-2)Gal(β1-O)) remains largely unknown.
  • Collagen glycosylation extent varies, with type IV collagen being more glycosylated than fibrillar collagens.
  • Glycosylated hydroxylysine is also found in non-collagenous proteins like complement protein 1Q and adiponectin.

Purpose of the Study:

  • To investigate the biological significance and variations of hydroxylysine glycosylation in collagens.
  • To identify the enzymes responsible for initiating collagen glycosylation.
  • To explore the implications of mutations in collagen glycosylation pathways.

Main Methods:

  • Literature review and comparative analysis of collagen structures and functions.

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Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
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  • Identification of key enzymes involved in the glycosylation pathway (COLGALT1 and COLGALT2).
  • Analysis of genetic mutations affecting collagen glycosylation and associated phenotypes.

    • Main Results:

    • The disaccharide Glc(α1-2)Gal(β1-O) is conserved across collagens from sponges to mammals.
    • Collagen O-glycosylation is initiated by galactosyltransferases COLGALT1 and COLGALT2 in the endoplasmic reticulum.
    • Mutations in COLGALT1 lead to cerebral small vessel abnormalities and porencephaly, linked to collagen type IV deficiency.

    Conclusions:

    • Hydroxylysine glycosylation is a fundamental post-translational modification in collagens with conserved and variable features.
    • COLGALT1 and COLGALT2 are crucial for initiating this glycosylation process.
    • Further research may uncover additional forms of collagen glycosylation in diverse organisms.