Tonic inhibition of neuronal calcium channels by G proteins removed during whole-cell patch-clamp experiments
Autor: | Pascal Pflimlin, Rainer Netzer, Gerhard Trube |
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Rok vydání: | 1994 |
Předmět: |
GTP'
Physiology G protein Clinical Biochemistry chemistry.chemical_element Calcium Guanosine Diphosphate GTP-Binding Proteins Physiology (medical) Animals Virulence Factors Bordetella Patch clamp Cells Cultured Ion transporter Neurons Voltage-dependent calcium channel Chemistry Calcium channel Cell Membrane Thionucleotides Calcium Channel Blockers Rats Electrophysiology Biochemistry Barium Guanosine 5'-O-(3-Thiotriphosphate) Biophysics Calcium Channels Guanosine Triphosphate |
Zdroj: | Pfl�gers Archiv European Journal of Physiology. 426:206-213 |
ISSN: | 1432-2013 0031-6768 |
DOI: | 10.1007/bf00374773 |
Popis: | The barium current through voltage-dependent calcium channels was recorded from cultured rat cortical neurons with the whole-cell configuration of the patch-clamp technique. The maximal current evoked by depolarising pulses from -80 mV to 0 mV was divided into inactivating and non-inactivating fractions. During the first minutes of whole-cell recording, the amplitude of the inactivating fraction increased from less than 0.1 nA to an average value of 1 nA, whereas the amplitude of the non-inactivating component remained essentially the same. This increase in amplitude was prevented when the "perforated-patch technique" was used, suggesting that some intracellular factor that inhibited the barium current was lost or destroyed during conventional whole-cell experiments. When GTP[gamma-S] or GTP was added to the pipette solution, no increase or only a weak rise of the inactivating current was seen, whereas GDP[beta-S] accelerated its increase. The results suggest that some of the calcium channels expressed in cultured cortical neurons are inhibited by a G protein even in the absence of added neurotransmitter. The current increase observed during whole-cell recordings may be due to a loss of intracellular GTP and the subsequent inactivation of an inhibitory G protein. |
Databáze: | OpenAIRE |
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