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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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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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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Dually modified transmembrane proteoglycans in development and disease.

Laura M Jenkins1, Ben Horst1, Carly L Lancaster1

  • 1Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC, 29208, USA.

Cytokine & Growth Factor Reviews
|January 3, 2018
PubMed
Summary

Dually modified transmembrane proteoglycans (DMTPs) regulate cell signaling pathways crucial for development and disease, including cancer. Understanding their roles in growth factor availability and receptor interaction is vital for therapeutic strategies.

Keywords:
BetaglycanCancerCell signalingGlycosaminoglycanProteoglycanSyndecan

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Aberrant cell signaling drives diseases like cancer.
  • Growth factor availability and receptor interactions are key regulatory mechanisms.
  • Dually modified transmembrane proteoglycans (DMTPs) are cell surface macromolecules regulating these interactions.

Purpose of the Study:

  • To review the functions of betaglycan and syndecan-1 (SDC1) DMTPs.
  • To compare the roles of heparan sulfate (HS) and chondroitin sulfate (CS) modifications in DMTPs.
  • To elucidate how DMTPs control cell signaling in development and disease.

Main Methods:

  • Literature review of current research on DMTPs.
  • Comparative analysis of betaglycan and SDC1 functions.
  • Focus on HS and CS glycosaminoglycan (GAG) chain modifications.

Main Results:

  • Betaglycan and SDC1 modulate Wnt, TGF-β, and FGF signaling pathways.
  • DMTPs regulate ligand availability and receptor internalization.
  • HS and CS GAG chains are mutually dependent on core proteins for function.

Conclusions:

  • DMTPs are critical regulators of cell signaling pathways.
  • Understanding DMTPs offers insights into cancer progression and development.
  • Targeting DMTPs may present novel therapeutic avenues.