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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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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...
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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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Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

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Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin,...
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Proteoglycans01:05

Proteoglycans

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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,...
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Studying Lactoferrin N-Glycosylation.

Sercan Karav1, J Bruce German2,3, Camille Rouquié4

  • 1Department of Molecular Biology and Genetics, Canakkale Onsekiz Mart University, 17100 Canakkale, Turkey. sercankarav@gmail.com.

International Journal of Molecular Sciences
|April 21, 2017
PubMed
Summary
This summary is machine-generated.

Lactoferrin, a milk protein, has diverse biological roles beyond iron binding. Its unique glycosylation patterns significantly influence these functions, impacting its use in medical foods and biotherapeutics.

Keywords:
N-glycansbioinfomatic librariesdeglycosylating enzymeslactoferrinmass spectrophotometrystructure-activity studies

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Mammalian Physiology

Background:

  • Lactoferrin is a multifunctional glycoprotein in mammalian milk, known for iron binding and roles in cell proliferation, differentiation, and antimicrobial activity.
  • While lactoferrin's iron-binding is well-studied, the impact of its glycosylation on biological functions remains largely unexplored.
  • Variations in glycosylation patterns among lactoferrin homologs may explain differences in their bioactivities.

Purpose of the Study:

  • To review the significance of lactoferrin glycosylation in its diverse biological functions.
  • To highlight the need for assessing glycan contributions to lactoferrin's bioactivity for biotherapeutic and medical food applications.

Main Methods:

  • Literature review focusing on lactoferrin structure-function relationships.
  • Analysis of studies investigating lactoferrin glycosylation patterns and their correlation with bioactivity.

Main Results:

  • Lactoferrin's glycan moieties are likely crucial contributors to its biological roles.
  • Unique glycosylation patterns exist across different mammalian lactoferrins, despite high amino acid sequence homology.
  • Understanding these patterns is key to explaining functional heterogeneity.

Conclusions:

  • Glycosylation is a critical, yet often overlooked, factor in determining lactoferrin's biological functionality.
  • Further research into lactoferrin glycosylation is essential for developing effective biotherapeutics and medical foods.
  • Assessing individual glycan contributions will enhance the application of lactoferrin in health and medicine.