Synthesis of kininogen and degradation of bradykinin by PC12 cells

British Journal of Pharmacology
A DendorferP Dominiak

Abstract

1. In this study, the abilities of PC12 cells to synthesize and degrade kinins were investigated. Kinin formation was assessed as kinin and kininogen content of cells and supernatants in serum-free incubations by use of a bradykinin-specific radioimmunoassay. Expression of kininogen mRNA was demonstrated by reverse-transcriptase PCR. Kinin degradation pathways of intact PC12 cells were characterized by identification of the kinin fragments generated from tritiated bradykinin either in the absence or presence of the angiotensin I-converting enzyme inhibitor ramiprilat. 2. Kinin immunoreactivity in the supernatant of PC12 cell cultures accumulated in a time-dependent fashion during incubations in serum-free media. This effect was solely due to de novo synthesis and release of kininogen (35 pg bradykinin h-1 mg-1 protein) since it could be suppressed by cycloheximide. Continuous synthesis of kininogen was a specific property of PC12 cells, as it was not observed in cultured macro- or microvascular endothelial cells. PC12 cells contained only minor amounts of stored kininogen. The rate of kininogen synthesis was not affected by ramiprilat, bacterial lipopolysaccharide, nerve growth factor or dexamethasone, but was stimulated 1.4 fo...Continue Reading

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Citations

Jan 12, 2002·Peptides·T A MorinelliH S Margolius
Dec 20, 2002·International Immunopharmacology·Y J I JongN L Baenziger
Feb 28, 2008·Cytometry. Part a : the Journal of the International Society for Analytical Cytology·Antonio H MartinsHenning Ulrich
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Jan 2, 2019·Cancer Cell International·Silvia Gutierrez, M Danilo Boada

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