ArticleThe Journal of membrane biology2003
Monovalent cations contribute to T-type calcium channel (Cav3.1 and Cav3.2) selectivity.
Article in The Journal of membrane biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Role of individual S4 segments in gating of CaChannels (Austin, Tex.) · 2018Article
- Models of calcium permeation through T-type channels.Pflugers Archiv : European journal of physiology · 2014Review
- The relationship between single-channel and whole-cell conductance in the T-type Ca2+ channel CaV3.1.Biophysical journal · 2008Article
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2 authors.
Funding
Abstract
Low voltage-activated (LVA) Ca2+ channels regulate chemical signaling by their ability to select for Ca2+. Whereas Ca2+ is the main permeating species through Ca2+ channels, Ca2+ permeation may be modified by abundant intra- and extracellular monovalent cations. Therefore, we explored monovalent cation regulation of LVA Ca2+ permeation in the cloned T-type Ca2+ channels alpha1G (Cav3.1) and alpha1H (Cav3.2). In physiological [Ca2+], the reversal potential in symmetrical Li+ was 19 mV in alpha1G and 18 mV in alpha1H, in symmetrical Cs+ the reversal potential was 36 mV in alpha1G and 37 mV in alpha1H, and in the bi-ionic condition with Li+ in the bath and Cs+ in the pipette, the reversal potential was 46 mV in both alpha1G and alpha1H. When Cs+ was used in the pipette, replacement of external Cs+ with Li+ (or Na+) shifted the reversal potential positive by 5-6 mV and increased the net inward current in alpha1G. Taken together the data indicate that in physiological [Ca2+], external Li+ (or Na+) permeates more readily than external Cs+, resulting in a positive shift of the reversal potential. We conclude that external monovalent cations dictate T-type Ca2+ channel selectivity by permeating through the channel. Similar to Li+, we previously reported that external [H+] can regulate T-type Ca2+ channel selectivity. Alpha1H's selectivity was more sensitive to external pH changes compared to alpha1G. When Cs+ was used in the pipette and Li+ was used in the bath external acidification from pHo 7.4 to 6.0 caused a negative shift of the reversal by 8 mV in alpha1H. Replacement of internal Cs+ with Li+ reduced the pH-induced shift of the reversal potential to 2 mV. We conclude that, similar to other external monovalent cations, H+ can modify T-type Ca2+ channel selectivity. However, in contrast to external monovalent ions that readily permeate, H+ regulate T-type Ca2+ channel selectivity by increasing the relative permeability of the internal monovalent cation.
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