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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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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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Structures of Solids

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
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Structure of Lipids03:38

Structure of Lipids

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Lipids include a diverse group of compounds that are largely nonpolar in nature. This is because they are hydrocarbons that include mostly nonpolar carbon-carbon or carbon-hydrogen bonds. Non-polar molecules are hydrophobic (“water fearing”), or insoluble in water. Lipids perform many different functions in a cell. Cells store energy for long-term use in the form of fats. Lipids also provide insulation from the environment for plants and animals. For example, they help keep aquatic...
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Viral Structure00:56

Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Updated: Feb 1, 2026

A Structured Rehabilitation Protocol for Improved Multifunctional Prosthetic Control: A Case Study
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Structural deciphering of the NG2/CSPG4 proteoglycan multifunctionality.

Elisa Tamburini1, Alice Dallatomasina2, Jade Quartararo1

  • 1Centre for Molecular and Translational Oncology (COMT), University of Parma, Parma, Italy.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|December 15, 2018
PubMed
Summary

Chondroitin sulfate proteoglycan 4 (CSPG4) is a complex cell surface protein involved in numerous cellular functions and signaling pathways. Understanding its structure-function relationship can reveal new therapeutic strategies for various diseases.

Keywords:
extracellular matrixmacromolecular interactionssignal transductionstructure-function relationship

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The chondroitin sulfate proteoglycan 4 (CSPG4) gene encodes a large, complex transmembrane proteoglycan central to the human surfaceome.
  • CSPG4 exhibits extensive evolutionary conservation and produces diverse glycoforms with distinct functional potentials.
  • Its structure facilitates interactions with over 40 ligands, involving both ectodomain and cytoplasmic tail.

Purpose of the Study:

  • To elucidate the structural-functional basis of CSPG4's multifaceted roles in cellular processes.
  • To explore how CSPG4's unique molecular interplays and signaling capabilities impact cell behavior.
  • To highlight the potential of targeting CSPG4's multivalency for disease intervention.

Main Methods:

  • Analysis of CSPG4's evolutionary conservation and transcript processing.
  • Investigation of CSPG4's interactions with ligands and its role in signal transduction.
  • Examination of CSPG4's association with the cytoskeleton and its membrane dynamics.

Main Results:

  • CSPG4 mediates complex molecular events through ligand interactions and dual signaling.
  • Its functional connection with the cytoskeleton and regulators enables signal transduction.
  • CSPG4's mobility and endocytic trafficking influence its signaling potential.
  • Differential phosphorylation of its intracellular domain affects numerous cellular phenomena.

Conclusions:

  • CSPG4's structural complexity and multivalency allow it to profoundly influence cell behavior.
  • Its involvement in diverse cellular pathways suggests a significant role in both normal physiology and pathology.
  • Targeting CSPG4 interactions offers a promising avenue for therapeutic strategies against various diseases.