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• W2090515057 abstract "Abstract Protease‐activated receptors (PARs) mediate cell activation after proteolytic cleavage of their extracellular amino terminus. We have reported earlier that primary cultures of rat brain capillary endothelial (RBCE) cells express at least two receptors for thrombin: PAR‐1 and PAR‐3. In the present study we show that PAR‐2 activation by trypsin or by the PAR‐2 agonist peptide (SLIGRL) evokes [Ca 2+ ] i signal in RBCE cells. Taking advantage of RBCE cells expressing PAR‐1 and PAR‐2, we show that trypsin activates both receptors. The relative agonist activity of trypsin and thrombin on PARs of RBCE cells compared with that of SLIGRL were 112% and 48%, respectively, whereas the potency of trypsin was 10 5 ‐fold higher than that of SLIGRL. Because under pathological conditions other proteases such as plasmin or leukocyte elastase may reach the cells of the blood–brain barrier, we investigated the effect of these proteases on RBCE cells. Elastase evoked a small increase in [Ca 2+ ] i but preincubation of cells with elastase dose‐dependently reduced the trypsin‐induced [Ca 2+ ] i signal. Plasmin had a 30% inhibitory effect on the trypsin‐induced response, and reduced the SLIGRL signal by 20%. It is concluded that PAR‐2 is functional in brain capillary endothelium, and that the main␣fibrinolytic proteases, plasmin and elastase, may regulate PAR‐2 signalling under pathological conditions." @default.
• W2090515057 created "2016-06-24" @default.
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• W2090515057 date "2002-03-01" @default.
• W2090515057 modified "2023-09-29" @default.
• W2090515057 title "Protease-activated receptor-2 (PAR-2) in brain microvascular endothelium and its regulation by plasmin and elastase" @default.
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• W2090515057 doi "https://doi.org/10.1046/j.0022-3042.2002.00759.x" @default.
• W2090515057 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11948237" @default.
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