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Tyrosine phosphorylation and bradykinin-induced signaling in endothelial cells

, : Tyrosine phosphorylation and bradykinin-induced signaling in endothelial cells. American Journal of Cardiology 80(SUPPL 3A): 102A-109A

It is generally accepted that in endothelial cells the occupation of bradykinin B-2 receptors, which are linked to the guanine nucleotide-dependent regulatory proteins, G-i and G-q, results in the activation of phospholipase C-beta-i (PLC-beta-1), followed by a transient increase in the formation of inositol 1,4,5-trisphosphate (IP-3) and diacylglycerol. The PLC-beta-1 isoform, in contrast to the gamma-1 isoform, is present only at a low level in cultured endothelial cells, implying that PLC-gamma-1 activation may play an important role in endothelial signaling pathways. In cultured human endothelial cells, bradykinin induced a rapid increase in the tyrosine phosphorylation of several Triton-soluble proteins. Immunoprecipitation of tyrosine-phosphorylated proteins from bradykinin-stimulated cells followed by Western blotting using the respective antibodies facilitated the identification of a 77 kiloDalton (kDa) protein as paxillin, a 130 kDa protein as PLC-gamma-1, and a 42/44 kDa doublet as mitogen-activated protein (MAP) kinase. The bradykinin-induced tyrosine phosphorylation of PLC-gamma-1 was relatively transient and was associated with an increase in intracellular levels of IP-3. Bradykinin also induced the rapid and transient activation of phosphotyrosine phosphatases localized mainly in the Triton X-100-soluble cell fraction; this tyrosine phosphatase activity was apparently initiated after the release of Ca-2+ from intracellular stores.


PMID: 9293962

DOI: 10.1016/s0002-9149(97)00464-5

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