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Studies on cathepsin B in human articular cartilage
The Biochemical Journal
|April 1, 1978
Summary
Cathepsin B activity is elevated in osteoarthrotic human cartilage and varies with age and depth. This thiol proteinase plays a role in cartilage degradation.
Area of Science:
- Biochemistry
- Enzymology
- Orthopedics
Background:
- Cathepsin B (EC 3.4.22.1) is a thiol proteinase implicated in tissue remodeling.
- Understanding its role in human articular cartilage is crucial for osteoarthritis research.
Purpose of the Study:
- To assay cathepsin B activity in human articular cartilage.
- To investigate the relationship between cathepsin B activity, osteoarthritis, age, and cartilage depth.
Main Methods:
- Assay of cathepsin B using the synthetic substrate alpha-N-benzoyl-DL-arginine 2-naphthylamide.
- Enzyme activation by cysteine and EDTA; inhibition by iodoacetamide, HgCl2, and human serum.
Main Results:
- Human osteoarthrotic cartilage showed increased cathepsin B activity compared to normal cartilage.
- Normal cartilage cathepsin B activity was age-dependent, higher in juveniles and lower in adults.
- Both cathepsin B and D displayed zonal variation, with higher activity in superficial cartilage cells.
Conclusions:
- Cathepsin B activity is altered in osteoarthritis and influenced by age and cartilage location.
- These findings suggest cathepsin B's involvement in the pathogenesis of osteoarthritis.