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Translocation of protein kinase C by halothane in cholinergic cells

Protein kinase C (PKC) is a signal transducing enzyme that is an important regulator of multiple physiologic processes and a potential molecular target for volatile anaesthetic actions. However, the effects of these agents on PKC activity are not yet fully understood. Volatile anaesthetics increase...

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Bibliographic Details
Published in:Brain research bulletin 2002-05, Vol.58 (1), p.55-59
Main Authors: Gomez, R.S, Barbosa, J, Guatimosim, C, Massensini, A.R, Gomez, M.V, Prado, M.A.M
Format: Article
Language:English
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Summary:Protein kinase C (PKC) is a signal transducing enzyme that is an important regulator of multiple physiologic processes and a potential molecular target for volatile anaesthetic actions. However, the effects of these agents on PKC activity are not yet fully understood. Volatile anaesthetics increase intracellular calcium concentration ([Ca 2+] i) in a variety of cells, thus their effects on PKC activity may be indirect due to [Ca 2+] i increase. Alternatively, the anaesthetics could directly stimulate PKC activity. In order to distinguish these two possibilities in intact cells, we used a fully functional green fluorescent protein conjugated PKC βII (GFP-PKC βII) and confocal microscopy to evaluate the dynamic redistribution of PKC in living SN56 cells, a cholinergic cell line, in response to halothane. Halothane induced PKC translocation in SN56 cells transfected with GFP-PKC βII. This effect was not suppressed by dantrolene, a drug that blocks halothane-induced Ca 2+ release from intracellular stores in these cells. These findings indicate that halothane induces PKC translocation in SN56 cells independently of its ability to release calcium from internal stores.
ISSN:0361-9230
1873-2747
DOI:10.1016/S0361-9230(02)00755-4