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Relationship between α1-antitrypsin inactivation and tumor necrosis factor α concentration in the synovial fluid of patients with rheumatoid arthritis

✍ Scribed by Keith Chidwick; Catherine E. Whichelow; Zhi Zhang; Kevin Fairburn; John A. Sachs; David R. Blake; Paul G. Winyard

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
429 KB
Volume
37
Category
Article
ISSN
0004-3591

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✦ Synopsis

Objective. To examine the relationship between qantitrypsin (a,AT) specific activity and tumor necrosis factor a (TNFa) concentration in synovial fluid from 48 patients with rheumatoid arthritis.

Methods.The specific activity of alAT was calculated from the measurement of a,AT concentration (by rocket immunoelectrophoresis) and elastase inhibitory capacity. TNFa was detected by enzyme-linked immunosorbent assay.

Results. TNFa concentrations correlated with the extent of a,AT inactivation.

Conclusion. Our findings are consistent with a role of elastase in TNFa release within the inflamed joint.

The plasma protein a,-antitrypsin (a,AT) is the principal physiologic inhibitor of neutrophil elastase and has been shown to be substantially inactivated (2650%) in the synovial fluid (SF) of patients with rheumatoid arthritis (RA) (see refs. 1 and 2 and references therein), although the extent of this inactivation is influenced by exercise-induced hypoxic-reperfusion injury (2). Active a,AT, which has the capacity to form a 1: 1 complex with neutrophil elastase, is inacti-

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