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Hyaluronate-binding proteins of murine brain
M S Marks1, G Chi-Rosso, B P Toole
1Department of Anatomy and Cellular Biology, Tufts University Health Sciences Center, Boston, Massachusetts 02111.
Journal of Neurochemistry
|January 1, 1990
Summary
Adult mouse brain contains multiple hyaluronate-binding proteins. Two forms resemble cartilage proteoglycan aggregates, while a third is distinct, revealing complex brain extracellular matrix components.
Area of Science:
- Neuroscience
- Biochemistry
- Extracellular Matrix Biology
Background:
- Hyaluronate-binding proteins are crucial components of the extracellular matrix, influencing tissue structure and cell behavior.
- The presence and characteristics of these proteins in the adult mouse brain are not fully understood.
Purpose of the Study:
- To identify and characterize hyaluronate-binding macromolecules in the adult mouse brain.
- To compare brain hyaluronate-binding proteins with known cartilage proteoglycan aggregates.
Main Methods:
- Fractionation of adult mouse brain into soluble and membrane components.
- Characterization using affinity chromatography (Sepharose CL-4B/CL-6B, diethylaminoethyl-cellulose), antibody cross-reactivity, and binding affinity measurements (KD).
Main Results:
- Approximately 60% of hyaluronate-binding activity was in the soluble fraction, 33% in membrane fractions, exhibiting high affinity and specificity.
- A significant portion of soluble activity contained chondroitin sulfate chains and reacted with antibodies against cartilage link protein and proteoglycan core protein, resembling cartilage proteoglycan aggregates.
- Another class of hyaluronate-binding material lacked chondroitin sulfate and did not react with cartilage-specific antibodies, indicating a distinct glycoprotein nature.
Conclusions:
- Adult mouse brain contains at least three distinct hyaluronate-binding macromolecules.
- Two of these share properties with cartilage proteoglycan aggregates, suggesting similar functional roles in the brain.
- A third distinct hyaluronate-binding glycoprotein was identified, highlighting the molecular diversity of brain extracellular matrix components.