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A brain extracellular matrix proteoglycan forms aggregates with hyaluronan

M Iwata1, T N Wight, S S Carlson

  • 1Department of Physiology and Biophysics, University of Washington, Seattle 98195.

The Journal of Biological Chemistry
|July 15, 1993
PubMed
Summary

The adult central nervous system extracellular matrix (ECM) contains a novel proteoglycan, pgT1, that binds hyaluronan. These pgT1/hyaluronan interactions form large aggregates, suggesting a key role in brain ECM structure.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Extracellular Matrix Biology

Background:

  • The adult central nervous system (CNS) extracellular matrix (ECM) composition is not well understood.
  • A previously identified brain proteoglycan, pgT1, exhibits properties of a general ECM component and is distinct from other known proteoglycans.

Purpose of the Study:

  • To investigate the interaction of pgT1 with hyaluronan.
  • To characterize the structure and properties of pgT1 aggregates.

Main Methods:

  • pgT1 binding affinity to hyaluronan was assessed.
  • pgT1 aggregation was induced and analyzed.
  • Electron microscopy was used to visualize aggregate structure.
  • Affinity coelectrophoresis determined the dissociation constant (Kd) for pgT1-hyaluronan interaction.

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Main Results:

  • pgT1 binds hyaluronan with high affinity (Kd = 0.9 +/- 0.2 nM).
  • pgT1 forms large aggregates in non-denaturing conditions, resembling cartilage proteoglycan aggregates.
  • Electron microscopy revealed aggregates composed of approximately 18 pgT1 subunits associated with a 350-nm filament.
  • Aggregation was dependent on the presence of hyaluronan and sensitive to Streptomyces hyaluronidase.

Conclusions:

  • pgT1 forms extensive aggregates with hyaluronan in the brain.
  • These pgT1/hyaluronan aggregates represent a significant structural component of the brain ECM network.
  • The findings suggest a broader role for pgT1 in CNS structure and function.