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Kunitz-type peptides of the sea anemone Heteractis crispa: Potential anti-inflammatory compounds
- Source :
- Russian Journal of Bioorganic Chemistry. 43:91-97
- Publication Year :
- 2017
- Publisher :
- Pleiades Publishing Ltd, 2017.
-
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.
- Subjects :
- 0301 basic medicine
Proteases
030102 biochemistry & molecular biology
medicine.drug_class
medicine.medical_treatment
Organic Chemistry
chemistry.chemical_element
Biology
Sea anemone
Calcium
biology.organism_classification
Biochemistry
Anti-inflammatory
law.invention
03 medical and health sciences
chemistry.chemical_compound
030104 developmental biology
chemistry
law
medicine
Recombinant DNA
Antihistamine
Receptor
Histamine
Subjects
Details
- ISSN :
- 1608330X and 10681620
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- Russian Journal of Bioorganic Chemistry
- Accession number :
- edsair.doi...........9aea26b78e01f1b21d9cf59cbd5657ee
- Full Text :
- https://doi.org/10.1134/s1068162016060121