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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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Matrix Proteoglycans and Glycoproteins01:21

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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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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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The Extracellular Matrix01:29

The Extracellular Matrix

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In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
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The Extracellular Matrix01:42

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Connective Tissue Fibers and Ground Substance01:17

Connective Tissue Fibers and Ground Substance

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One of the significant functions of connective tissue is connecting tissues and organs. Unlike epithelial tissue that is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. The matrix usually includes a large amount of extracellular material produced by the connective tissue cells that are embedded within it. It plays a significant role in the functioning of this tissue. The major component of the matrix is a...
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Glycoproteomics of the Extracellular Matrix: A Method for Intact Glycopeptide Analysis Using Mass Spectrometry
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A personal voyage through the proteoglycan field.

Ulf Lindahl1

  • 1Department of Medical Biochemistry and Microbiology, Uppsala University, Box 582, SE-751 23 Uppsala, Sweden.

Matrix Biology : Journal of the International Society for Matrix Biology
|January 28, 2014
PubMed
Summary

Proteoglycans, key extracellular matrix components, are now understood as distinct molecules with unique core proteins and glycosaminoglycan (GAG) chains. Genomics has advanced this field, yet GAG biosynthesis regulation and GAG-protein interactions remain areas for further research.

Keywords:
Chondroitin sulfateCore proteinsGAGosomeGlycosaminoglycan biosynthesisGlycosaminoglycan chainGlycosaminoglycan–protein interactionsHeparan sulfate

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Extracellular Matrix Research

Background:

  • Proteoglycans were conceptualized as distinct molecules approximately 40 years ago, evolving from earlier, less defined ideas about the extracellular matrix.
  • Recognition of core proteins as unique molecular entities, varying in glycosaminoglycan (GAG) chain substitution and biological function, marked a significant advancement.

Purpose of the Study:

  • To survey the historical development and current understanding of proteoglycans as discrete molecular entities.
  • To highlight the impact of genomics on proteoglycan research.
  • To identify outstanding unresolved issues in the field, including GAG biosynthesis regulation and GAG-protein interaction specificity.

Main Methods:

  • Review of historical data and conceptual evolution in proteoglycan research.
  • Outline of methodological approaches used to study proteoglycans.
  • Integration of genomic data to assess its impact on the field.

Main Results:

  • Proteoglycans are now recognized as distinct molecules with specific core proteins and GAG chains, influencing their location and function.
  • Genomics has significantly impacted the study of proteoglycans, providing new insights into their diversity and function.
  • Methodological advancements have enabled a clearer understanding of proteoglycan structure, biosynthesis, and function.

Conclusions:

  • The field has progressed from muddled notions of the extracellular matrix to a clear understanding of proteoglycans as distinct molecular entities.
  • Genomics has been instrumental in advancing proteoglycan research, but key questions regarding GAG biosynthesis and GAG-protein interactions persist.
  • Further research is needed to fully elucidate the regulatory mechanisms of GAG biosynthesis and the specificities governing GAG-protein interactions.