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Related Concept Videos

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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Glycosaminoglycans01:23

Glycosaminoglycans

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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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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Structure of Cadherins01:25

Structure of Cadherins

4.2K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Fibril-associated Collagen01:11

Fibril-associated Collagen

3.0K
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.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Updated: Nov 21, 2025

Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface
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Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface

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Organ-specific heparan sulfate structural phenotypes.

Xiaofeng Shi1, Joseph Zaia

  • 1Department of Biochemistry, Boston University School of Medicine, Boston, Massachusetts 02118, USA.

The Journal of Biological Chemistry
|February 27, 2009
PubMed
Summary
This summary is machine-generated.

Heparan sulfate (HS) structural variations were analyzed in rat organs. We found a common disaccharide with an unsubstituted amino group present in mammalian tissues, offering new insights into GAG biochemistry.

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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
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Detection of Glycosaminoglycans by Polyacrylamide Gel Electrophoresis and Silver Staining
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Area of Science:

  • Biochemistry
  • Glycobiology
  • Molecular Biology

Background:

  • Heparan sulfate (HS) is a glycosaminoglycan (GAG) crucial for protein interactions and biological functions.
  • HS exhibits significant structural diversity in chain length, sulfation, and acetylation, impacting its biological roles.
  • Understanding GAG biochemistry requires detailed structural information across biological systems.

Purpose of the Study:

  • To develop procedures for extracting GAGs from rat organ tissues.
  • To analyze and compare HS expression levels and structural variations using liquid chromatography/mass spectrometry.
  • To investigate HS GAG chain variations concerning organ location, length, composition, and specific structural epitopes.

Main Methods:

  • Extraction of GAGs from various rat organ tissues.
  • Analysis of HS expression levels and structural features using liquid chromatography/mass spectrometry (LC/MS).
  • Characterization of HS GAG chain variations, including average length, disaccharide composition, and low-abundance epitopes.

Main Results:

  • Detailed variations in HS GAG chains were observed as a function of organ location.
  • Significant structural heterogeneity in HS chains was identified, including average length and disaccharide composition.
  • A disaccharide with an unsubstituted amino group was found to be endogenous and widely expressed in mammalian organ tissues.

Conclusions:

  • HS structural heterogeneity is organ-specific and contributes to diverse biological functions.
  • The identification of a widely expressed unsubstituted amino group-containing disaccharide provides a new perspective on HS structure.
  • These findings advance the understanding of GAG biochemistry and the structural basis of HS-protein interactions.