Cartilage proteoglycan aggregate formation. Role of link protein.
The Biochemical journal
confidence
Key findings
Optimal HA for proteoglycan aggregate formation ~1% of proteoglycan dry weight; link protein binds to HA-binding region of proteoglycan monomer.
View source on PubMed (PMID 7325976) ↗
- Sample size
- Not reported
- Population
- In vitro cartilage proteoglycan aggregates
- Dosing
- Hyaluronic acid ~1% of proteoglycan dry weight; link protein ~1.5% of proteoglycan dry weight
- Duration
- Not reported
- Route
- In vitro
- Blinding
- not_reported
- Controls
- none
- Drug class
- glycosaminoglycan
Full abstract
Cartilage proteoglycan aggregate formation was studied by zonal rate centrifugation in sucrose gradients. Proteoglycan aggregates, monomers and proteins could be resolved. It was shown that the optimal proportion of hyaluronic acid for proteoglycan aggregate formation was about 1% of proteoglycan dry weight. The reaggregation of dissociated proteoglycan aggregate A1 fraction was markedly concentration-dependent and even at 9 mg/ml only about 90% of the aggregates were reformed. The lowest proportion of link protein required for maximal formation of link-stabilized proteoglycan aggregates was 1.5% of proteoglycan dry weight. It was separately shown that link protein co-sedimented with the proteoglycan monomer. By competition with isolated hyaluronic acid-binding-region fragments, a proportion of the link proteins was removed from the proteoglycan monomers, indicating that the link protein binds to the hyaluronic acid-binding region of the proteoglycan monomer.