Duodenase activates rat peritoneal mast cells via protease-activated receptors of type 1 |
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Authors: | A M Makarova T S Zamolodchikova L D Rumsh S M Strukova |
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Institution: | (1) Faculty of Biology, Moscow State University, Vorob’evy gory, Moscow, 119899, Russia;(2) Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia |
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Abstract: | It was found that duodenase, a serine protease from the bovine duodenum, activates rat peritoneal mast cells (PMC) in vitro presumably via protease-activated receptors (PARs). Like thrombin (a serine protease from the blood coagulation system) and the PAR1 agonist peptide (PAR1-AP), duodenase was shown to accelerate the secretion of β-hexosaminidase (a marker of cell degranulation) by PMC in a dose-dependent manner. The blockage of the proteolytic activity of duodenase toward the substrate Tos-Gly-Pro-Lys-pNA by the soybean Bauman-Birk protease inhibitor substantially reduced (by 40%) the ability of duodenase to stimulate the secretory activity of PMC. Pretreatment of PMC with duodenase decreased the β-hexosaminidase secretion induced by thrombin and PAR1-AP by 35 and 41.7 %, respectively, and abolished the antiinflammatory effect of activated protein C. At the same time, pretreatment of PMC with duodenase did not affect the secretion of β-hexosaminidase induced by compound 48/80, a nonspecific degranulator of mast cells. Duodenase, unlike PAR1-AP (30–100 μM), in a broad concentration range (10–100 nM) did not induce aggregation of human platelets, but suppressed the platelet aggregation elicited by PAR1-AP. |
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Keywords: | duodenase inflammation mast cells PAR1 agonist peptide protease-activated receptors thrombin |
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