4.0 Article

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

Journal

RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
Volume 41, Issue 6, Pages 590-596

Publisher

MAIK NAUKA/INTERPERIODICA/SPRINGER
DOI: 10.1134/S106816201506014X

Keywords

sea anemones; the Kunitz-type protease inhibitors; antihistamine activity; anti-inflammatory activity

Funding

  1. Russian Scientific Foundation [14-25-00037]

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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.

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