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- W88072457 abstract "The vasoactive peptide bradykinin (BK) is a mitogen for normal renal cells. We explored the effects of BK in orpk cilia (+) and orpk cilia (−) collecting duct cell lines, which were derived from a mouse model of polycystic kidney disease (PKD). mRNAs for BK B1 and BK B2 receptors were demonstrated by RT-PCR in both cell lines. To study BK signaling pathways, we employed fluorescent measurements of intracellular Ca2+, a Cytosensor microphysiometer to measure changes in extracellular pH as a reflection of activation of the Na+/H+ exchanger (NHE), and Western blotting to assess extracellular signal regulated kinase (ERK) activation. Exposure to 100 nM BK resulted in rapid elevation of intracellular Ca2+, caused a ≥ 20% increase in NHE activity, and a ≥ 200% increase in ERK phosphorylation. While BK-induced Ca2+ signals and NHE activation were similar in orpk cilia (+) and orpk cilia (−) cell lines, BK-induced ERK phosphorylation was less pronounced in orpk cilia (−) cells. The BK B2 receptor antagonist and an epidermal growth factor receptor (EGFR) tyrosine kinase inhibitor blocked BK-induced ERK phosphorylation suggesting a role for the B2 receptor-induced EGFR transactivation in the mitogenic ERK pathway. We speculate that cilium is required for effective transactivation of EGFR and ERK activation by BK B2 receptors in PKD cells. These studies are important because of proposed role of ERK pathway in pathophysiology of PKD." @default.
- W88072457 created "2016-06-24" @default.
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- W88072457 date "2010-04-01" @default.
- W88072457 modified "2023-09-27" @default.
- W88072457 title "Bradykinin B2 receptor activates extracellular signal regulated kinase in renal cells from a mouse model of polycystic kidney disease" @default.
- W88072457 doi "https://doi.org/10.1096/fasebj.24.1_supplement.lb703" @default.
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