Abstract:
:We report here a direct modulation by mast cell tryptase of endothelial barrier function through activation of proteinase-activated receptor-2 (PAR-2). In cultured bovine aortic endothelial cells (BAECs), tryptase, trypsin and PAR-2 activating peptide impaired the barrier function as determined by the permeability of protein-conjugated Evans blue. The tryptase-induced barrier dysfunction was completely blocked by U73122, and partially reversed by xestospongin C, calphostin C or Y27632. The intracellular Ca(2+) was elevated by tryptase. It was notable that ioxaglate, a contrast material that degranulates mast cells, markedly increased the permeability when applied to BAECs in combination with mast cells, an action that was blocked by nafamostat, a potent tryptase inhibitor. Immunofluorescence analysis showed that actin stress fibre formation and disruption of VE-cadherin were observed after exposure to tryptase or ioxaglate in combination with mast cells. Therefore, it is suggested that mast cell tryptase impairs endothelial barrier function through activation of endothelial PAR-2 in a manner dependent on the phospholipase C activity.
journal_name
Cell Signaljournal_title
Cellular signallingauthors
Sendo T,Sumimura T,Itoh Y,Goromaru T,Aki K,Yano T,Oike M,Ito Y,Mori S,Nishibori M,Oishi Rdoi
10.1016/s0898-6568(03)00014-7subject
Has Abstractpub_date
2003-08-01 00:00:00pages
773-81issue
8eissn
0898-6568issn
1873-3913pii
S0898656803000147journal_volume
15pub_type
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