Abstract

Mast cells contain large amounts of fully active proteases, i.e. chymase, tryptase and carboxypeptidase A (CPA3), that are stored together with serglycin (a proteoglycan with heparin side chains) in secretory granules. Hence, mast cell proteases are massively released upon degranulation and they may have a large impact on the local inflammatory reaction, e.g. by degrading various bioactive proteins. The objective of this study was to investigate the possibility if mast cells could regulate the levels of IL-6, a cytokine with a wide variety of biological functions. We found that cultured peritoneal mast cells from wild type mice can efficiently degrade IL-6 upon degranulation, whereas MCs from serglycin-deficient mice totally lacked this ability. Moreover, the addition of a serine protease inhibitor significantly reduced the proteolytic degradation of IL-6. Our data suggest that degradation of IL-6 by mast cells is mediated by serglycin-dependent serine proteases.

Published in

Book title: Abstract book

Conference

EMBRN-COST International Mast cell and Basophil Meeting 2013

Authors' information