Enhancement of eosinophil effector function by soluble factors released by S. mansoni: role of proteases.
Open Access
- 1 July 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 131 (1) , 464-470
- https://doi.org/10.4049/jimmunol.131.1.464
Abstract
Schistosomulum-released products (SRP) have been shown to enhance both expression of rat and human eosinophil Fc receptors and IgG-dependent cytotoxicity. The present work provides additional evidence of the secretion of eosinophil-enhancing factors by schistosomula and other developmental stages of schistosomes, including adult worms. The heat lability, as well as the strong inhibition of the stimulating activity of SRP by the protease inhibitor Trasylol, suggest that thermolabile proteases secreted by the parasite are involved in this mechanism. The purification of the schistosome proteases by preparative isoelectric focusing and gel filtration demonstrated that neutral proteases able to hydrolyze the collagenase substrates Azocoll and Z-Gly-Pro-Leu-Gly-Pro are able to significantly enhance eosinophil effector functions. Purified Clostridium histolyticum collagenase was also able to mimic the enhancing effect of schistosome proteases, suggesting involvement of a collagenase-like activity of the enzymes in the eosinophil stimulation.This publication has 4 references indexed in Scilit:
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- Proteolytic cleavage of IgG bound to the Fc receptor of Schistosoma mansoni schistosomulaParasite Immunology, 1981
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- Eosinophil‐dependent cytotoxicity in rat schistosomiasis. Involvement of IgG2a antibody and role of mast cellsEuropean Journal of Immunology, 1978