Abstract
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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Original Russian Text © O.V. Sintsova, M.M. Monastyrnaya, E.A. Pislyagin, E.S. Menchinskaya, E.V. Leychenko, D.L. Aminin, E.P. Kozlovskaya, 2015, published in Bioorganicheskaya Khimiya, 2015, Vol. 41, No. 6, pp. 657–663.
The article has been adapted from the report presented at the VIIth All-Russian symposium “Proteins and Peptides”, Novosibirsk, 12–17 July, 2015.
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Sintsova, O.V., Monastyrnaya, M.M., Pislyagin, E.A. et al. Anti-inflammatory activity of a polypeptide from the Heteractis crispa sea anemone. Russ J Bioorg Chem 41, 590–596 (2015). https://doi.org/10.1134/S106816201506014X
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DOI: https://doi.org/10.1134/S106816201506014X