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Related Concept Videos

Proteoglycans01:05

Proteoglycans

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,...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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...
Glycosaminoglycans01:23

Glycosaminoglycans

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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Characterization of Intra-Cartilage Transport Properties of Cationic Peptide Carriers
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Published on: August 10, 2020

Studies of proteoglycan involvement in CPP-mediated delivery.

Anders Wittrup1, Si-He Zhang, Mattias Belting

  • 1Department of Clinical Sciences, Section of Oncology, Lund University, Lund, Sweden.

Methods in Molecular Biology (Clifton, N.J.)
|November 6, 2010
PubMed
Summary

This chapter details methods to investigate if cell-penetrating peptides (CPPs) require heparan sulfate proteoglycans (HSPGs) for cellular entry. It provides protocols for studying HSPG involvement in CPP uptake and specificity.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Medicine

Background:

  • Cell-penetrating peptides (CPPs) are crucial for delivering macromolecules into cells.
  • Cellular uptake of many CPPs is known to depend on cell surface heparan sulfate proteoglycans (HSPGs).

Purpose of the Study:

  • To provide methodologies for assessing the role of proteoglycans (PGs) in CPP uptake.
  • To enable researchers to determine if a specific CPP's entry is PG-dependent.

Main Methods:

  • Protocols for purifying PGs using anion-exchange chromatography.
  • Methods for characterizing HSPG core protein composition in cell lines.
  • Techniques for modulating HSPG core protein expression to assess specificity.

Main Results:

  • The chapter outlines how to establish PG dependence for CPP uptake.
  • Detailed procedures are provided for PG purification and characterization.
  • Methods allow for the investigation of specific HSPG core protein roles in CPP delivery.

Conclusions:

  • The described methods facilitate the study of proteoglycan involvement in CPP cellular entry.
  • Researchers can now systematically investigate the role of specific HSPGs in CPP-mediated delivery.
  • This work aids in understanding and optimizing CPP-based drug delivery systems.