Ethanol actions on the mechanisms of Ca2+ mobilization in rat hippocampal cells are mediated by protein kinase C
| Autor: | Sergej L. Mironov, Anton Hermann |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_element
Calcium Hippocampus Rats Sprague-Dawley chemistry.chemical_compound Phorbol Esters Animals Receptor Molecular Biology Protein kinase C Cells Cultured Protein Kinase C Ethanol Ryanodine receptor General Neuroscience Rats Biochemistry chemistry Biophysics Liberation Phosphorylation Neurology (clinical) Intracellular Developmental Biology |
| Zdroj: | Brain research. 714(1-2) |
| ISSN: | 0006-8993 |
| Popis: | The effects of ethanol on intracellular free Ca(2+) concentration, [Ca](i), were studied in cultured rat hippocampal neurons using fluo-3 and confocal microscopy. Ethanol application transiently elevAted [Ca](i) due to Ca(2+)-induced Ca(2+) release from internal stores since the effect was observed also in solutions containing zero Ca(2+) or 0.3 mM La(3+) and restoration of external Ca(2+) content led to secondary response in presence of ethanol. The sites of highest [Ca]i increases correlated well with those obtained after Ca(2+) release from caffeine-and IP3-sensitive internal stores. After single ethanol exposure the caffeine-evoked [Ca](i) transients were potentiated whereas Ca(2+) release induced by IP(3)-mobilizing agonists was suppressed. Similar effects were observed by activation of protein kinase C (PKC) by phorbol esters which also occluded ethanol actions. Ethanol increased fluorescence of Rim-1, a PKC indicator dye. The data obtained are consistent with ethanol activation of PKC whereby Ca(2+) release via ryanodine receptors is potentiated and IP(3) receptors are down-modulated. Since the effects of both ethanol and phorbol esters were mimicked by cytochalasins B and D, PKC-induced cytoskeleton phosphorylation and its subsequent rearrangements can be responsible for observed effects. |
| Databáze: | OpenAIRE |
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