JBC INTERFERin siRNA transfection reagent

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Volume 271, Number 45, Issue of November 8, 1996 pp. 28077-28081
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Cystatins Up-regulate Nitric Oxide Release from Interferon-gamma - activated Mouse Peritoneal Macrophages

(Received for publication, August 10, 1995, and in revised form, March 19, 1996)

Ludovic Verdot Dagger § , Gilles Lalmanach Dagger , Vincent Vercruysse § , Susanne Hartmann par , Richard Lucius par , Johan Hoebeke Dagger , Francis Gauthier Dagger and Bernard Vray §

From the § Laboratoire d'Immunologie Expérimentale (CP 615), Faculté de Médecine, Université Libre de Bruxelles, B1070 Brussels, Belgium, the Dagger  Laboratoire d'Enzymologie et de Chimie des Protéines, Université François Rabelais, F37032 Tours, France, and par  Molecular Parasitology (Institut of Biology), Humboldt-University Berlin, Berlin, Germany

Up-regulation of nitric oxide (NO) production by activated murine macrophages was observed during infection by Trypanosoma cruzi, the etiological agent of Chagas' disease. Cell infection by T. cruzi depends at least in part on cruzipain, a membrane-associated papain-related proteinase which is sensitive to inhibition by synthetic inhibitors of cysteine proteinases. Using the natural cysteine proteinase inhibitor chicken cystatin, a representative member of cystatin family 2, to investigate the effect of cruzipain on macrophage infection and NO release, we found that the inhibitor alone up-regulated NO release from interferon-gamma -activated macrophages. A 12-fold increase in NO production was observed in the presence of 1 µM chicken cystatin. This overproduction was concentration-dependent and could be detected at concentrations as low as 10 nM and remained in the presence of polymyxin B. Representative members of the other cystatin families, i.e. stefin B (family 1), T-kininogen, and its inhibitory domains (family 3), were also able to enhance NO production from interferon-gamma -activated macrophages. Neither E64, an irreversible inhibitor of cysteine proteinases, nor inhibitors of aspartyl and serine proteinases (aprotinin, pepstatin, and soybean trypsin inhibitor) enhanced NO production. Upon complexation with saturating amounts of reduced-alkylated papain, cystatins still remained active in increasing NO production, suggesting that the cystatin inhibitory site was not involved in the mechanism.

The results demonstrate that members of all 3 cystatin families share another common property unrelated to their function of cysteine proteinase inhibitors, i.e. up-regulation of NO production, which biological significance remains to be elucidated.


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