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Impaired Activity of Protease Inhibitors Towards Neutrophil Elastase Bound to Human Articular Cartilage

Impaired Activity of Protease Inhibitors Towards Neutrophil Elastase Bound to Human Articular Cartilage

K Kawabata, A R Moore, D A Willoughby

Ann Rheum Dis. 1996 Apr;55(4):248-52.

PMID: 8733442

Abstract:

Objective:
To investigate the effects of protease inhibitors on the ability of free and cartilage bound neutrophil elastase to degrade cartilage proteoglycan in vitro.
Methods:
Cryostat sections of human articular cartilage were used as substrate, and proteoglycan loss induced by free or cartilage bound elastase was quantified by alcian blue staining, followed by scanning and integrating microdensitometry.
Results:
High molecular mass protease inhibitors (alpha 1 protease inhibitor, alpha 2 macroglobulin, and soya bean trypsin inhibitor) and synovial fluid from patients with rheumatoid arthritis were effective in blocking proteoglycan loss from sections treated with free elastase, but their activity towards cartilage bound elastase was much reduced. In contrast, low molecular mass elastase inhibitors (N-methoxysuccinyl-Ala-Ala-Pro-Val chloromethyl ketone and ONO-5046 (N-[2-[4-(2,2-dimethylpropionyloxy) phenylsulphonylamino]benzoyl] amino-acetic acid) were effective against free and cartilage bound elastase.
Conclusion:
The binding of elastase to cartilage appears to be a mechanism whereby the enzyme can remain active in the presence of high molecular mass protease inhibitors.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP65144345	N-(Methoxysuccinyl)-Ala-Ala-Pro-Val-chloromethyl ketone		65144-34-5	Price

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