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Kunitz-type peptides of the sea anemone Heteractis crispa: Potential anti-inflammatory compounds

Abstract

Antihistamine activity of recombinant peptides, Kunitz-type serine protease inhibitors of the sea anemone Heteractis crispa, was studied. It was shown that the peptides rHCGS1.19 and rHCGS1.36 at a concentration 10 μM inhibit an increase in the calcium ion concentration in macrophages elicited by histamine at 62.2 and 84.0%, respectively. The anti-inflammatory effect can be seen as the result of mediated reactions between peptides and proteases involved in these processes, as with the histamine H1-type receptor blocking.

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Abbreviations

BPTI:

bovine pancreatic trypsin inhibitor

TNF-α:

tumor necrosis factor alpha

LPS:

lipopolysaccharide

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Correspondence to E. V. Leychenko.

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Original Russian Text © O.V. Sintsova, E.A. Pislyagin, I.N. Gladkikh, M.M. Monastyrnaya, E.S. Menchinskaya, E.V. Leychenko, D.L. Aminin, E.P. Kozlovskaya, 2017, published in Bioorganicheskaya Khimiya, 2017, Vol. 43, No. 1, pp. 105–112.

The paper is based on the materials of the “Chemical Biology 2016” conference; Novosibirsk, Russia, July 24–29, 2016.

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Sintsova, O.V., Pislyagin, E.A., Gladkikh, I.N. et al. Kunitz-type peptides of the sea anemone Heteractis crispa: Potential anti-inflammatory compounds. Russ J Bioorg Chem 43, 91–97 (2017). https://doi.org/10.1134/S1068162016060121

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  • DOI: https://doi.org/10.1134/S1068162016060121

Keywords

  • sea anemone
  • Kunitz-type protease inhibitors
  • antihistamine activity