Anti-inflammatory activity of a polypeptide from the Heteractis crispa sea anemone

The anti-inflammatory activity of the HCGS 1.20 recombinant polypeptide (a Kunitz-type serine protease inhibitor from the Heteractis crispa sea anemone) was investigated. The polypeptide was shown to inhibit the histamine-induced increase in the concentration of calcium ions and the lipopolysaccharidestimulated increase in the concentration of nitric oxide (II) in macrophages. A possible mechanism of this anti-inflammatory activity of the polypeptide was discussed.