Key result
An acid metalloproteinase purified from human articular cartilage was found to be elevated approximately 3-fold in osteoarthritic cartilage compared to normal levels.
Population
Human articular cartilage samples (20-g) and 26 cartilage extracts (including osteoarthritic cartilage)
Design
Preclinical
Authors
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May suggest role in cartilage degradation but should not change practice; leaves open its value as a therapeutic target.
The study identifies and characterizes a novel acid metalloproteinase from human articular cartilage that is elevated in osteoarthritis, suggesting a potential role in cartilage degradation.
Azzo et al. (1986) studied Osteoarthritis (n=26). Acid metalloproteinase purification and characterization was evaluated on Enzyme activity and characteristics. An acid metalloproteinase purified from human articular cartilage was found to be elevated approximately 3-fold in osteoarthritic cartilage compared to normal levels.
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