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Doxycycline in the protection of serum alpha-1-antitrypsin from human neutrophil collagenase and gelatinase.

By T Sorsa, O Lindy, Y T Konttinen, K Suomalainen, T Ingman, H Saari, S Halinen, H M Lee, L M Golub and J Hall

Abstract

The concentration of doxycycline required to inhibit 50% (50% inhibitory concentration for serpinase activity) of alpha-1-antitrypsin degradation by purified neutrophil collagenase was found to be approximately 20 microM, a value similar to the 50% inhibitory concentration of doxycycline required to inhibit collagen degradation by neutrophil collagenase. Doxycycline also efficiently inhibited phorbol myristate acetate-triggered neutrophil-mediated degradation of alpha-1-antitrypsin. This suggests that doxycycline can protect alpha-1-antitrypsin from collagenase and gelatinase in the presence of other proteases and biologically active molecules that are released by triggered neutrophils. The protection of a body's alpha-1-antitrypsin shield from serpinolytic activity of collagenase and matrix metallproteinases can result in inhibition of serine proteases such as neutrophil elastase. Tetracyclines may thus protect matrix constituents from a wider spectrum of neutral proteases than previously recognized, not just from the matrix metalloproteinases collagenase and gelatinase

Topics: Research Article
Year: 1993
OAI identifier: oai:pubmedcentral.nih.gov:187711
Provided by: PubMed Central
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