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      Recombinant bovine S100A8 and A9 enhance IL-1β secretion of interferon-gamma primed monocytes.

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          Abstract

          Calgranulin A (S100A8) and B (S100A9) are found at high levels in inflamed tissue and have been associated with acute and chronic inflammatory disorders. Calgranulins are discussed as damage-associated molecular patterns (DAMPs). To analyze the role of calgranulins for inflammatory responses, bovine S100A8 and S100A9 were cloned, successfully expressed and FPLC-purified. Both molecules did not induce NF-κB activation in boTLR4-transfected HEK293 cells and stimulation of bovine monocytes with both proteins did not result in interleukin 1β (IL-1β) secretion or an upregulated mRNA expression of selected genes (IL1B, TNF, CXCL8, IL10, IL12). However, Interferon γ (IFN-γ) primed bovine monocytes released significantly higher amounts of IL-1β after stimulation with S100A8, S100A9, and co-stimulation with adenosine triphosphate (ATP). In IL-4/IL-13-primed monocytes, the IL-1β release was completely abrogated. The results imply that TLR4/MyD88/NF-κB-independent S100A8/A9-mediated activation of the inflammasome in cattle is favored in a Th1 environment and that S100A8 and S100A9 act as a DAMP in cattle.

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          Author and article information

          Journal
          Vet. Immunol. Immunopathol.
          Veterinary immunology and immunopathology
          1873-2534
          0165-2427
          Sep 15 2013
          : 155
          : 3
          Affiliations
          [1 ] Immunology Unit, University of Veterinary Medicine Hannover, Bischofsholer Damm 15, D-30173 Hannover, Germany.
          Article
          S0165-2427(13)00204-3
          10.1016/j.vetimm.2013.07.002
          23890724
          Copyright © 2013 Elsevier B.V. All rights reserved.

          Cattle, DAMP, Inflammasome, S100

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