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• W2111777906 abstract "Membrane-associated cytoskeletal proteins provide support for endothelial cell (EC) junctional cell adhesion molecules. Nonmuscle filamin is a dimeric actin cross-linking protein that interacts with F-actin and membrane glycoproteins. Both bradykinin and des-Arg9-bradykinin cause filamin redistribution from the plasma membrane to the cytosol of confluent EC. Kinin-induced filamin translocation parallels the dynamics of intracellular Ca2+ increases. Pretreatment with kinin receptor antagonists blocks the Ca2+ response as well as filamin translocation induced by kinins. Protein kinase C activation prior to kinin stimulation attenuates intracellular Ca2+ increases and filamin translocation. BAPTA, a cell-permeable Ca2+ chelator, attenuates bradykinin-induced intracellular Ca2+ increases and filamin translocation. This study demonstrates that bovine pulmonary artery ECs express both kinin B1 and B2 receptors, and that activation of either receptor leads to intracellular Ca2+ increases. This Ca2+ signalling, which is downregulated by protein kinase C activation, is essential for kinin-induced filamin translocation." @default.
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• W2111777906 date "1997-12-01" @default.
• W2111777906 modified "2023-10-16" @default.
• W2111777906 title "Activation of Endothelial Cell Kinin Receptors Leads to Intracellular Calcium Increases and Filamin Translocation: Regulation by Protein Kinase C" @default.
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• W2111777906 doi "https://doi.org/10.1016/s0898-6568(97)00051-x" @default.
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